Prof. Dr. S. Backert

Research areas: Host/pathogen interaction

Molecular function and signal transduction of the serine protease HtrA: a novel secreted effector protein of bacterial pathogens

Stable adhesion complexes are crucial for maintenance of the cell-to-cell integrity in healthy epithelia of humans and represent the first barrier for microbial pathogens. Alterations in these complexes are key events in the development and progression of many diseases including various cancers. One of the major proteins involved in maintaining epithelial adhesion is the tumor-suppressor and junctional transmembrane protein E-cadherin. E-cadherin also controls the transcription factor b-catenin and other signaling components, and is involved in cell morphogenesis, adhesion, recognition and communication. Inactivation of E-cadherin’s adhesive properties is often a key step in various infections, tumor progression and metastasis. We have recently identified a novel secreted effector protein, the serine protease HtrA, ofthe foodborne pathogen Campylobacter jejuni and the gastric pathogen and type-I carcinogen Helicobacter pylori. HtrA of these microbes can be secreted into the extracellular space where it can cleave-off the extracellular domain of E-cadherin on polarized gastric or intestinal epithelial cells. Since the htrA gene is conserved in many bacterial pathogens our findings could provide a potential novel mechanism how these microbes may destroy cellular junctions in mucosal epithelial cells, in order to get access to deeper tissues and cause disease by degrading E-cadherin and probably other cellular factors. This project is therefore designed to contribute to the understanding of mechanisms underlying basic HtrA functions in bacterial pathogenesis. In particular, we investigate the molecular mechanisms/requirements for HtrA proteolytic activity, pinpoint novel HtrA targets on host cells and to study downstream signaling events. In addition, we aim to identify the secretion pathway of HtrA across the two bacterial membranes because this could give hints how HtrA is transported. Our studies will take advantage of powerful technologies including fluorescence microscopy and live cell imaging as well as proteomics-based and cellular signal transduction approaches.

Structure and Function of the H. pylori cag type IV secretion system

Helicobacter pylori is a highly successful pathogen uniquely adapted to colonize humans. Gastric infections with this bacterium can induce pathology ranging from chronic gastritis and peptic ulcers to gastric cancer. More virulent H. pylori isolates harbour numerous well-known adhesins (BabA/B, SabA, AlpA/B, OipA and HopZ) and the cag (cytotoxin-associated genes) pathogenicity island (PAI) encoding a type IV secretion system (T4SS). The adhesins establish tight bacterial contact with host target cells and the T4SS represents a needle-like pilus device for the delivery of effector proteins into host target cells such as CagA. BabA and SabA can bind to blood group antigen and sialylated proteins respectively, and a series of T4SS components including CagI, CagL, CagY and CagA have been shown to target the integrin β1 receptor followed by injection of CagA across the host cell membrane. The interaction of CagA with membrane-anchored phosphatidylserine may also play a role in the delivery process. While substantial progress has been made in our current understanding of many of the above factors, the host cell receptors for OipA, HopZ and AlpA/B during infection are still unknown. We are interested in characterizing the interactions of the various adhesins and structural T4SS proteins with host cell factors. Of particular interest is the T4SS encoded by the cagPAI. T4SSs are macromolecular assemblies used by numerous bacteria to transport molecules across their membranes including proteins and DNA. T4SS are generally composed of a set of 12 proteins (VirB1-11 and the VirD4 coupling factor) plus some accessory proteins. This together represents a dynamic membrane-anchored machinery powered by three encoded NTPases. Since T4SSs are widespread in many pathogenic bacteria where they are often used to deliver effectors into host cells, we investigate the unique and complex interaction of various components of the H. pylori T4SS as a model system. Its interaction with the integrin β1 receptor will help to better understand the molecular mechanisms of how protein translocation events work in H. pylori. We therefore use specific bacterial mutant strains, proteomics-based methods, protein-protein interaction studies such as Biacore and sophisticated microscopic technologies.

Identification and characterization of novel Helicobacter species in mammals

As Helicobacter pylori was the first bacterium cultivated from human gastric biopsy specimens in 1982, it has become apparent that Helicobacter subspecies exhibit a broad host spectrum and can be isolated from the gastrointestinal tracts of humans, non-human primates, cats, dogs, cheetahs, ferrets, rodents, cows, sheep, pigs, dolphins, and birds. Currently there are 32 validated Helicobacter species and several other described isolated candidates. Members of the genus Helicobacter are helical curved, spiral or fusiform, Gram-negative bacteria with or without helical periplasmic fibers. We are interested in the investigation and characterization of novel enterohepatic Helicobacter subspecies (EHS), which are an emerging group of microaerobic, motile pathogens carrying flagella with variable styles in number and locations. EHS are known to persistently colonize multiple animal species. They can be isolated from the lower intestine, hepatobiliary system, and diarrheic feces and are potentially associated with chronic inflammation and epithelial cell hyperproliferation leading to neoplasic disease. Helicobacter hepaticus, considered the prototype of all known EHS, has been shown to induce chronic active hepatitis and hepatocellular carcinoma in A⁄JCr and B6C3F1 mice strains as well as typhlocolitis in A⁄JCr inbred mice. This species is also used experimentally to induce cholesterol gallstones, inflammatory bowel disease (IBD), and in certain strains of mice induces colon cancer. Because lesions caused by EHS in mice often mimic those seen in humans with cholecystitis, their possible role in hepatobiliary disease in humans has been proposed. In addition, the possible zoonotic origin of important clinical manifestations in humans and the health status of mice housed in research facilities have recently attracted the attention of scientists. In contrast to H. pylori, almost nothing is known about potential virulence factors in EHS. To evaluate the prevalence of EHS infections in mouse strains harbored in specific-pathogen-free (SPF) facilities, we tested 40 mouse lines that were permanently living in nine colony rooms using a group-specific PCR, which detects all Helicobacter species currently known. When Helicobacter-negative and infected mice shared the same cage, transmission of the infection occurred within two weeks at very high frequency (100%). Furthermore, we found that mice from commercial breeding facilities may carry undetected Helicobacter infections. We also showed that infection with EHS may occur and spread frequently in mice under SPF conditions, and despite extensive safety conditions. Due to the lack of available methods, EHS infections often remain unrecognized but can cause severe health complications or more subtle host immune perturbations and therefore can confound the results of animal experiments. We therefore isolate and investigate live pathogens, and develop methods to rapidly identify novel EHS.


Original papers


Original research papers

1.) Backert, S., Dörfel, P., Börner, T. (1995).
Investigation of plant organellar DNAs by pulsed-field gel electrophoresis. Current Genetics 28: 390-399. doi:10.1007/bf00326439.

2.) Backert, S., Lurz, R., Börner, T. (1996).
Electron microscopic investigation of mitochondrial DNA from Chenopodium album (L.). Current Genetics 29: 427-436. doi:10.1007/bf02221510.

3.) Backert, S., Dörfel, P., Lurz, R., Börner, T. (1996).
Rolling circle replication of mitochondrial DNA in the higher plant Chenopodium album (L.). Molecular and Cellular Biology 16: 6285-6294. doi:10.1128/mcb.16.11.6285.

4.) Backert, S., Meißner, K., Börner, T. (1997).
Unique features of the mitochondrial rolling circle-plasmid mp1 from the higher plant Chenopodium album (L.). Nucleic Acids Research 25: 582-589. doi:10.1093/nar/25.3.582.

5.) Backert, S., Lurz, R., Oyarzabal, O.A., Börner, T. (1997).
High content, size and distribution of single-stranded DNA in the mitochondria of Chenopodium album (L.). Plant Molecular Biology 33: 1037-1050. doi:10.1023/a:1005791310886.

6.) Backert, S., Dörfel, P., Börner, T. (1997).
Investigation of plant organellar DNA by pulsed-field gel electrophoresis, Tobacco Abstracts 84: 96-97.

7.) Oyarzabal, O.A., Wesley, L.V., Harmon, K.M., Tucker, L., Barbaree, J.M., Lauerman, L.H.,  Backert, S., Conner, D.E. (1997).
Specific identification of Campylobacter fetus by PCR targeting variable regions of the 16S rRNA. Journal of Veterinary Microbiology 58: 61-71. doi:10.1016/s0378-1135(97)00148-x.

8.) Scissum-Gunn, D.K., Gandhi, M., Backert, S., Nielsen, B.L. (1998).
Separation of different conformations of plant mitochondrial DNA molecules by field inversion gel electrophoresis. Plant Molecular Biology Reporter 16: 219-229. doi:10.1023/A:1007512108373.

9.) Gandhi, M., Hammett, L., Scissum-Gunn, K., Backert, S., Nielsen, B.L. (1998).
Analysis of genome structure and gene copy number in Brassica campestris mitochondrial DNA. FASEB Journal 12(8), Supplement S: A1355.

10.) Backert, S., Kunnimalaiyaan, M., Börner, T., Nielsen, B.L. (1998).
In vitro replication of mitochondrial plasmid mp1 from the higher plant Chenopodium album (L.): A remnant of bacterial rolling circle and conjugative plasmids? Journal of Molecular Biology 284: 1005-1015. doi:10.1006/jmbi.1998.2254.

11.) Backert, S., von Nickisch-Rosenegk, E., Meyer, T.F. (1998).
Potential role of two Helicobacter pylori relaxases in DNA transfer? Molecular Microbiology 30: 673-674. doi:10.1046/j.1365-2958.1998.01086.x.

12.) Gratchev, A., Böhm, C., Riede, E., Foss H.D., Hummel, M., Mann, B., Backert, S., Buhr, H.J., Stein, H., Riecken, E.-O., Hanski, C. (1998).
Regulation of mucin MUC2 gene expression during colon carcinogenesis. Annals of the New York Academy of Sciences 859: 180-183. doi:10.1111/j.1749-6632.1998.tb11122.x.

13.) Gelos, M., Backert, S., Klussmann, E., Gratchev, A., Kobalz, U., Mann, B., Moyer, M.P., Böhm, C., Riecken, E.O., Hanski, C. (1998).
Detection of differential gene expression in colorectal cancer cell lines: comparison of three methods. Journal of Molecular Medicine 76(6): B13.

14.) Backert, S., Gelos, M., Kobalz, U., Hanski, M.L., Böhm, C., Mann, B., Lövin, N., Gratchev, A., Mansmann, U., Moyer, M.P., Riecken, E.O., Hanski, C. (1999).
Differential gene expression in colon carcinoma cells and tissues detected with a cDNA array. International Journal of Cancer 82: 868-874. doi:10.1002/(sici)1097-0215(19990909)82:6<868::aid-ijc16>;2-w.

15.) Backert, S., Börner, T. (2000).
Phage T4-like intermediates of DNA replication and recombination in the mitochondria of the higher plant Chenopodium album (L.). Current Genetics 37: 304-314. doi:10.1007/s002940050532.

16.) Backert, S., Ziska, E., Brinkmann, V., Zimny-Arndt, U., Fauconnier, A., Jungblut, P.R., Naumann, M., Meyer, T.F. (2000).
Translocation of the Helicobacter pylori CagA protein in gastric epithelial cells by a type IV secretion apparatus. Cellular Microbiology 2: 155-164. doi:10.1046/j.1462-5822.2000.00043.x.

17.) Backert, S. (2000).
Strand-switching during rolling circle replication of plasmid-like DNA minicircles in the mitochondria of the higher plant Chenopodium album (L.). Plasmid 43: 166-170. doi:10.1006/plas.1999.1437.

18.) Ramarao, N., Gray-Owen, S.D., Backert, S., Meyer, T.F. (2000).
Helicobacter pylori inhibits phagocytosis by professional phagocytes involving type IV secretion components. Molecular Microbiology 37: 1389-1404. doi:10.1046/j.1365-2958.2000.02089.x.

19.) Backert, S., Müller, E.-C., Jungblut, P.R., Meyer, T.F. (2001).
Tyrosine phosphorylation patterns and size modification of the Helicobacter pylori CagA protein after translocation into gastric epithelial cells. Proteomics 1: 608-617. doi:10.1002/1615-9861(200104)1:4<608::AID-PROT608>3.0.CO;2-G.

20.) Moese, S., Selbach, M., Zimny-Arndt, U., Jungblut, P.R., Meyer, T.F., Backert, S. (2001).
Identification of a tyrosine-phosphorylated 35 kDa carboxy-terminal fragment (p35CagA) of the Helicobacter CagA protein in phagocytic cells: Processing or breakage? Proteomics 1: 618-629. doi:10.1002/1615-9861(200104)1:4<618::AID-PROT618>3.0.CO;2-C.

21.) Backert, S., Moese, S., Selbach, M., Brinkmann V,  Meyer, T.F. (2001).
Phosphorylation of tyrosine 972 of the Helicobacter pylori CagA protein is essential for induction of a scattering phenotype in gastric epithelial cells. Molecular Microbiology 42: 631-644. doi:10.1046/j.1365-2958.2001.02649.x.

22.) Kwok, T., Backert, S., Schwarz, H., Berger, J., Meyer, T.F. (2002).
Specific entry of Helicobacter pylori into cultured gastric epithelial cells via a zipper-like mechanism. Infection & Immunity 70: 2108-2120. doi:10.1128/iai.70.4.2108-2120.2002.

23.) Selbach, M., Moese, S., Meyer, T.F., Backert, S. (2002).
Functional analysis of the Helicobacter pylori cag pathogenicity island reveals both VirD4/CagA-dependent and VirD4/CagA-independent mechanisms. Infection & Immunity 70: 665-671. doi:10.1128/iai.70.2.665-671.2002.

24.) Selbach, M., Moese, S., Hauck, C.R., Meyer, T.F., Backert, S. (2002).
Src is the kinase of the Helicobacter pylori CagA protein in vivo and in vitro. Journal of Biological Chemistry 277: 6775-6778. doi:10.1074/jbc.C100754200.

25.) Moese, S., Selbach, M., Meyer, T.F., Backert, S. (2002).
cag+ Helicobacter pylori induce a homotypic aggregation phenotype in macrophage-like cells by upregulation and recruitment of intracellular adhesion molecule 1 to the cell surface. Infection & Immunity 70: 4687-4691. doi:10.1128/iai.70.8.4687-4691.2002.

26.) Backert, S. (2002).
R-loop dependent rolling-circle replication and a new model for DNA concatemer resolution by mitochondrial plasmid mp1. EMBO Journal 21: 3128-3136. doi:10.1093/emboj/cdf311.

27.) Selbach, M., Moese, S., Hauck, C.R., Meyer, T.F., Backert, S. (2003).
The Helicobacter pylori CagA protein induces cortactin dephosphorylation and actin rearrangement by c-Src inactivation. EMBO Journal 22: 515-528. doi:10.1093/emboj/cdg050.

28.) Zawilak, A.,  Durrant, M.C., Jakimowicz, P., Backert, S., Zakrzewska-Czerwińska J. (2003).
DNA binding specificity of the replication initiator protein, DnaA from Helicobacter pylori. Journal of Molecular Biology 334: 933-947. doi:10.1016/j.jmb.2003.10.018.

29.) Backert, S., Schwarz, T., Miehlke, S., Kirsch, C., Sommer, Ch., Kwok, T., Gerhard M., Goebel, U., Lehn, N., König, W., Meyer, T.F. (2004).
Functional analysis of the cag pathogenicity island in Helicobacter pylori isolates from patients with gastritis, peptic ulcer and gastric cancer. Infection & Immunity 72: 1043-1056. doi:10.1128/iai.72.2.1043-1056.2004.

30.) Moese, S., Selbach, M. Kwok, T., Brinkmann, V., König, W., Meyer, T.F. Backert, S. (2004).
Helicobacter pylori induces AGS cell motility and elongation via independent pathways. Infection & Immunity 72: 3646-3649. doi:10.1128/IAI.72.6.3646-3649.2004.

31.) Selbach, M., Moese, S., Backert, S., Jungblut, P.R., Meyer, T.F. (2004).
The Helicobacter pylori CagA protein induces tyrosine dephosphorylation of ezrin. Proteomics 4: 2961-2968. doi:10.1002/pmic.200400915.

32.) Backert, S., Gressmann, H., Kwok, T., Zimmy-Arndt, U., König, W., Jungblut, P.R.; Meyer, T.F. (2005).
Gene expression and protein profiling of AGS gastric epithelial cells upon infection with Helicobacter pylori. Proteomics 5: 3902-3918. doi:10.1002/pmic.200401240.

33.) Backert, S., Kwok, T., Schmid, M., Selbach, M., Moese, S., Peek, R.M. Jr, König, W., Meyer, T.F., Jungblut, P.R. (2005).
Subproteomes of soluble and structure-bound Helicobacter pylori proteins analysed by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 5: 1331-1345. doi:10.1002/pmic.200401019.

34.) Enarsson, K., Brisslert, M., Backert, S., Quiding-Järbrink, M. (2005).
Helicobacter pylori induce transendothelial migration of activated memory T cells. Infection & Immunity 73: 761-769. doi:10.1128/IAI.73.2.761-769.2005.

35.) Brisslert, M., Enarsson, K., Lundin, B.S., Karlsson, A., Kusters J., Svennerholm, A.-M., Backert, S., Quiding-Järbrink, M. (2005).
Helicobacter pylori induce neutrophil transendothelial migration: role of the bacterial HP-NAP. FEMS Microbiology Letters 249: 95-103. doi:10.1016/j.femsle.2005.06.008.

36.) Gieseler, S., König, B., König, W., Backert, S. (2005).
Strain-specific expression profiles of virulence genes in Helicobacter pylori during infection of gastric epithelial cells and granulocytes. Microbes & Infection 7: 437-447. doi:10.1016/j.micinf.2004.11.018.

37.) Backert, S., Kwok, T., König, W. (2005).
Conjugative plasmid DNA transfer in Helicobacter pylori mediated by chromosomally encoded relaxase and TraG-like proteins. Microbiology 151(Pt 11): 3493-3503. doi:10.1099/mic.0.28250-0.

38.) Brandt, S., Kwok, T., Hartig, R., König, W., Backert, S. (2005).
NF-kB-activation and potentiation of proinflammatory responses by the Helicobacter pylori CagA protein. Proceedings of the National Academy of Sciences USA 102: 9200-9205. doi:10.1073/pnas.0409873102.

39.) Dossumbekova, A., Prinz, C., Gerhard, M., Brenner, L., Backert, S., Kusters, J.G., Schmid, R.M., Rad, R. (2006).
Helicobacter pylori outer membrane proteins and gastric inflammation. Gut 55: 1360-1361.

40.) Dossumbekova, A., Prinz, C., Mages, J., Lang, R., Kusters, J.G., vanVliet, A.H., Reindl, W., Backert, S., Saur, D., Schmid, R.M., Rad, R. (2006).
Helicobacter pylori HopH (OipA) and bacterial pathogenicity: genetic and functional genomic analysis of hopH gene polymorphisms. Journal of Infectious Diseases 194: 1346-1355. doi:10.1086/508426.

41.) Backert, S. (2006).
Interaction of Helicobacter pylori with its host: role of the cag pathogenicity island and multiple functions of the CagA protein. European Journal of Cell Biology 85 (Suppl.): 117-118.

42.) Bohr, U.R.M., Selgrad, M., Ochman, C., Backert, S., König, W., Fenske, A., Wex, T., Malfertheimer, P. (2006).
Prevalence and spread of enterohepatic Helicobacter in mice reared in a specific pathogen-free facility. Journal of Clinical Microbiology 44: 738-742. doi:10.1128/JCM.44.3.738-742.2006.

43.) Krause-Gruszczynska, M., Rohde, M., Hartig, R., Genth, H., Schmidt, G., Keo, T., König, W., Miller, W.G., Konkel, M.E., Backert, S. (2007).
Role of the small Rho GTPases Rac1 and Cdc42 in host cell invasion of Campylobacter jejuni. Cellular Microbiology 9: 2431-2444. doi:10.1111/j.1462-5822.2007.00971.x.

44.) Krause-Gruszczynska, M., van Alphen, L.B., Oyarzabal, O.A., Alter, T. Hänel, I., Schliephake, A., König, W.,van Putten, J., Konkel, M.E., Backert, S. (2007).
Expression Patterns and Role of the CadF protein in Campylobacter jejuni and Campylobacter coli. FEMS Microbiology Letters 274: 9-16. doi:10.1111/j.1574-6968.2007.00802.x.

45.) Oyarzabal, O.A., Rad, R., Backert, S. (2007).
Conjugative Transfer of Chromosomally-Encoded Antibiotic Resistance from Helicobacter pylori to Campylobacter jejuni. Journal of Clinical Microbiology 45: 402-408. doi:10.1128/JCM.01456-06.

46.) Oyarzabal, O.A., Backert, S., Nagaraj, M., Miller, R.S., Hussain, K.S., Oyarzabal, E.A. (2007).
Efficacy of Supplemented Buffered Peptone Water for the Isolation of Campylobacter jejuni and C. coli from Broiler Retail Products. Journal of Microbiological Methods 69: 129-136. doi:10.1016/j.mimet.2006.12.011.

47.) Brandt, S., Shafikhani, S., Balachandran, P., Jin, S., Hartig R., König, W., Engel, J., Backert, S. (2007).
Use of a novel co-infection system reveals a role for Rac1, H-Ras, and CrkII phosphorylation in Helicobacter pylori-induced host cell actin cytoskeletal rearrangements. FEMS Immunology and Microbiology 50: 190-205. doi:10.1111/j.1574-695X.2007.00234.x.

48.) Blumenthal, B., Hoffmann, C., Aktories, K., Backert, S., Schmidt, G. (2007).
The Cytotoxic Necrotizing Factors from Yersinia pseudotuberculosis and from Escherichia coli Bind to Different Cellular Receptors but Take the Same Route to the Cytosol. Infection & Immunity 75: 3344-3353. doi:10.1128/IAI.01937-06.

49.) Moese, S., Selbach, M., Brinkmann, V., Karlas, A., Haimovich, B., Backert, S., Meyer, T.F. (2007).
The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin. Cellular Microbiology 9: 1148-1161. doi:10.1111/j.1462-5822.2006.00856.x.

50.) Tammer, I., Brandt, S., Hartig, R., König, W., Backert, S. (2007).
Activation of c-Abl by Helicobacter pylori: a novel kinase for CagA and crucial mediator of host cell scattering. Gastroenterology 132: 1309-1319. doi:10.1053/j.gastro.2007.01.050.

51.) Potturi-Venkata, L.P., Backert, S., Vieira, S.L., Oyarzabal, O.A. (2007).
Evaluation of logistic processing to reduce cross-contamination of commercial broiler carcasses with Campylobacter spp. Journal of Food Protection 70: 2549- 2554. doi:10.4315/0362-028x-70.11.2549.

52.) Kwok, T., Zabler, D., Urman, S., Rohde, M., Hartig, R., Wessler, S., Misselwitz, R., Berger, J., Sewald, N., König, W., Backert, S. (2007).
Helicobacter exploits integrin for type IV secretion and kinase activation. Nature 449: 862-866. doi:10.1038/nature06187.

53.) Potturi-Venkata, L.P., Backert, S., Lastovica, A.J., Vieira, S.L., Norton, R.A., Miller, R.S., Pierce, S., Oyarzabal, O.A. (2007).
Evaluation of different plate media for direct cultivation of Campylobacter species from live broilers. Poultry Science 86: 1304-1311. doi:10.1093/ps/86.7.1304.

54.) Knauer, O., Binai, N.A., Carra, G., Beckhaus, T., Hanschmann, K.M., Renné, T., Backert, S., Karas, M., Wessler, S. (2008).
Differential phosphoproteome profiling reveals a functional role for VASP in Helicobacter pylori-induced cytoskeleton turnover in gastric epithelial cells. Cellular Microbiology 10: 2285-2296. doi:10.1111/j.1462-5822.2008.01207.x.

55.) Oyarzabal, O.A., Backert, S., Williams, L.L., Lastovica, A.J., Miller, R.S., Pierce, S.J., Vieira, S.L., Rebollo-Carrato, F. (2008).
Molecular typing, serotyping and cytotoxicity testing of Campylobacter jejuni strains isolated from commercial broilers in Puerto Rico. Journal of Applied Microbiology 105: 800-812. doi:10.1111/j.1365-2672.2008.03809.x.

56.) Speegle, L., Miller, M.E., Backert, S., Oyarzabal, O.A. (2009).
Use of cellulose filters to isolate Campylobacter spp. from naturally contaminated retail broiler meat. Journal of Food Protection 72: 2592-2596. doi:10.4315/0362-028x-72.12.2592.

57.) Tegtmeyer, N., Backert, S. (2009).
Bacterial type III effectors inhibit cell lifting by targeting integrin-linked kinase. CELL host & microbe 5: 514-516. doi:10.1016/j.chom.2009.06.001.

58.) Brandt, S., Kenny, B., Rohde, M., Martinez-Quiles, N., Backert, S. (2009).
Dual infection system identifies a crucial role for PKA-mediated serine phosphorylation of the EPEC-Tir-injected effector protein in regulating Rac1 function. Cellular Microbiology 11: 1254-1271. doi:10.1111/j.1462-5822.2009.01330.x.

59.) Brandt, S., Wessler, S., Hartig, R., Backert, S. (2009).
Helicobacter pylori activates protein kinase C delta to control Raf in MAP kinase signalling: role in AGS epithelial cell scattering and elongation. Cell Motility and the Cytoskeleton 66: 874-892. doi:10.1002/cm.20373.

60.) Svensson, H., Hansson, M., Kilhamn, J., Backert, S., Quiding-Järbrink, M. (2009).
Selective upregulation of endothelial E-selectin in response to Helicobacter pylori-induced gastritis. Infection and Immunity 77: 3109-3116. doi:10.1128/IAI.01460-08.

61.) Selbach, M., Paul, F.E., Brandt, S., Guye, P., Daumke, O., Backert, S., Dehio, C., Mann, M. (2009).
Host cell interactome of tyrosine-phosphorylated bacterial proteins. CELL host & microbe 5: 397-403. doi:10.1016/j.chom.2009.03.004.

62.) Tegtmeyer, N., Zabler, D., Schmidt, D., Hartig, R., Brandt, S., Backert, S. (2009).
Importance of EGF receptor, HER2/Neu and Erk1/2 kinase signalling for host cell elongation and scattering induced by the Helicobacter pylori CagA protein: antagonistic effects of the vacuolating cytotoxin VacA. Cellular Microbiology 11: 488-505. doi:10.1111/j.1462-5822.2008.01269.x.

63.) Sason, H., Milgrom, M., Weiss, A.M., Melamed-Book, N., Balla, T., Grinstein, S., Backert, S., Rosenshine, I., Aroeti, B. (2009).
Enteropathogenic Escherichia coli subverts phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate upon epithelial cell infection. Molecular Biology of the Cell 20: 544-555. Erratum in: Molecular Biology of the Cell 20: 2638. doi:10.1091/mbc.e08-05-0516.

64.) Manchekar, M., Scissum-Gunn, K.D., Hammett, L.A., Backert, S., Nielsen, B.L. (2009).
Mitochondrial DNA recombination in Brassica campestris. Plant Science 177: 629-635. doi:10.1016/j.plantsci.2009.08.002.

65.) Olofsson, A., Vallström, A., Petzold, K., Tegtmeyer, N., Schleucher, J., Carlsson, S., Haas, R., Backert, S., Wai, S.N., Gröbner, G., Arnqvist, A. (2010).Biochemical and functional characterization of Helicobacter pylori vesicles. Molecular Microbiology 77: 1539-1555. doi:10.1111/j.1365-2958.2010.07307.x.

66.) Backert, S., Tegtmeyer, N., Selbach, M. (2010).
The versatility of Helicobacter pylori CagA effector protein functions: The master key hypothesis. Helicobacter 15: 163-176. doi:10.1111/j.1523-5378.2010.00759.x.

67.) Tegtmeyer, N., Hartig, R., Delahay, R.M., Rohde, M., Brandt, S., Conradi, J., Takahashi, S., Smolka, A.J., Sewald, N., Backert, S. (2010).
A small fibronectin-mimicking protein from bacteria induces cell spreading and focal adhesion formation. Journal of Biological Chemistry 285: 23515-23526. doi:10.1074/jbc.M109.096214.

68.) Saha, A., Backert, S., Hammond, C.E., Gooz, M., Smolka, A.J. (2010).
Helicobacter pylori CagL activates ADAM17 to induce repression of the gastric H, K-ATPase alpha subunit. Gastroenterology 139: 239-248. doi:10.1053/j.gastro.2010.03.036.

69.) Hoy, B., Löwer, M., Weydig, C., Carra, G., Tegtmeyer, N., Geppert, T.,Schröder, P.,  Sewald, N., Backert, S., Schneider, G., Wessler, S. (2010).
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83.) Conradi, J., Tegtmeyer, N., Woźna, M., Wissbrock, M., Michalek, C., Gagell, C., Cover, T.L., Frank, R., Sewald, N., Backert, S. (2012).
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84.) Hirsch, C., Tegtmeyer, N., Rohde, M., Rowland, M., Oyarzabal, O.A., Backert, S., (2012).
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85.) Tegtmeyer, N., Rivas Traverso, F., Rohde, M., Oyarzabal, O.A., Lehn, N., Berg. D.E., Fox, J.G., Backert, S. (2013).
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88.) Barden, S., Lange, S., Tegtmeyer, N., Conradi, J., Sewald, N., Backert, S., Niemann, H.H. (2013).
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93.) Zhang, Y.M., Noto, J.M., Hammond, C.E., Barth, J.L., Argraves, W.S., Backert, S., Peek, R.M. Jr., Smolka, A.J. (2014).
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96.) Zhang, X.S., Tegtmeyer, N., Traube, L., Jindal, S., Perez-Perez, G., Sticht, H., Backert, S., Blaser, M.J. (2015).
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98.) Koch, K.N., Hartung, M.L., Urban, S., Kyburz, A., Bahlmann, A.S., Lind, J., Backert, S., Taube, C., Müller, A. (2015).
Helicobacter urease-induced activation of the TLR2/NLRP3/IL-18 axis protects against asthma. The Journal of Clinical Investigation 125: 3297-3302. doi:10.1172/JCI79337.

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101.) Hartung, M.L., Gruber, D.C., Koch, K.N., Grüter, L., Rehrauer, H., Tegtmeyer, N., Backert, S., Müller, A. (2015).
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103.) Tegtmeyer, N., Moodley, Y., Yamaoka, Y., Pernitzsch, S.R., Schmidt, V., Rivas Traverso, F., Schmidt, T.P., Rad, R., Yeoh, K.G., Bow, H., Torres, J., Gerhard, M., Schneider, G., Wessler, S., Backert, S. (2016).
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104.) Pachathundikandi, S.K., Backert, S. (2016).
Differential expression of Interleukin 1β during Helicobacter pylori infection of Toll-like receptor 2 (TLR2) and TLR10-expressing HEK293 cell lines. The Journal of Infectious Diseases 214: 166-167. doi:10.1093/infdis/jiw154.

105.) Schmidt, T.P., Perna, A.M., Fugmann, T., Böhm, M., Hiss, J., Haller, S., Götz, C., Tegtmeyer, N., Hoy, B., Rau, T.T., Neri, D., Backert, S., Schneider, G., Wessler, S. (2016).
Identification of E-cadherin signature motifs functioning as cleavage sites for Helicobacter pylori HtrA. Scientific Reports 6: 23264. doi:10.1038/srep23264.

106.) Javaheri, A., Kruse, T., Moonen,s K., Mejías-Luque, R., Debraekeleer, A., Asche, C.I., Tegtmeyer, N., Kalali, B., Bach, N.C., Sieber, S.A., Hill, D.J., Königer, V., Hauck, C.R., Moskalenko, R., Haas, R., Busch, D.H., Klaile, E., Slevogt H., Schmidt, A., Backert, S., Remaut, H., Singer, B.B., Gerhard, M. (2016).
Helicobacter pylori adhesin HopQ engages in a virulence-enhancing interaction with human CEACAMs. Nature Microbiology 2: 16189. doi:10.1038/nmicrobiol.2016.189. Erratum in: Nature Microbiology 2: 16243. doi:10.1038/nmicrobiol.2016.243.

107.) Lim, M.C.C., Maubach, G., Sokolova, O., Feige, M.H., Diezko, R., Buchbinder, J., Backert, S., Schlüter, D., Lavrik, I.N., Naumann, M. (2017).
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114.) Backert, S., Tegtmeyer, N., Oyarzabal, O.A., Osman, D., Rohde, M., Grützmann, R., Vieth M. (2018).
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115.) Moonens, K., Hamway, Y., Neddermann, M., Reschke, M., Tegtmeyer, N., Kruse, T., Kammerer, R., Mejías-Luque, R., Singer, B.B., Backert, S., Gerhard, M., Remaut, H. (2018).
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116.) Dunne, C., Naughton, J., Duggan, G., Loughrey, C., Kilcoyne, M., Joshi, L., Carrinton, S., Earley, H., Backert, S., Robbe Masselot, C., May, F.E.B., Clyne, M. (2018).
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117.) Albrecht, N., Tegtmeyer, N., Sticht, H., Skórko-Glonek, J., Backert, S. (2018).
Amino-Terminal Processing of Helicobacter pylori Serine Protease HtrA: Role in Oligomerization and Activity Regulation. Frontiers in Microbiology 9: 642. doi:10.3389/fmicb.2018.00642.

118.) Zarzecka, U., Modrak-Wojcik, A., Bayassi, M., Szewczyk, M., Gieldon, A., Lesner, A., Koper, T., Bzowska, A., Sanguinetti, M., Backert, S., Lipinska, B., Skorko-Glonek, J. (2018).
Biochemical properties of the HtrA homolog from bacterium Stenotrophomonas maltophilia. International Journal of Biological Macromolecules. 109: 992-1005. doi:10.1016/j.ijbiomac.2017.11.086.

119.) Bauwens, E., Joosten, M., Taganna, J., Rossi, M., Debraekeleer, A., Tay, A., Peters, F., Backert, S., Fox, J., Ducatelle, R., Remaut, H., Haesebrouck, F., Smet, A. (2018).
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120.) Harrer, A., Bücker, R., Boehm, M., Zarzecka, U., Tegtmeyer, N., Sticht, H., Schulzke, J.D., Backert, S. (2019).
Campylobacter jejuni enters gut epithelial cells and impairs intestinal barrier function through cleavage of occludin by serine protease HtrA. Gut Pathogens 11: 4. doi:10.1186/s13099-019-0283-z.

121.) Tegtmeyer, N., Harrer, A., Schmitt, V., Singer, B.B., Backert, S. (2019).
Expression of CEACAM1 or CEACAM5 in AZ-521 cells restores the type IV secretion deficiency for translocation of CagA by Helicobacter pylori. Cellular Microbiology 21: e12965. doi: 10.1111/cmi.12965.

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How many protein molecules are secreted by single Helicobacter pylori cells: quantification of serine protease HtrA. Cellular Microbiology 1: e13022. doi:10.1111/cmi.13022.

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Quantification of serine protease HtrA molecules secreted by the foodborne pathogen Campylobacter jejuni. Gut Pathogens 11: 14. doi:10.1186/s13099-019-0295-8.

124.) Gutiérrez-Escobar, A.J., Bravo, M.M., Acevedo, O., Backert, S. (2019).
Molecular evolution of the VacA p55 binding domain of Helicobacter pylori in mestizos from a high gastric cancer region of Colombia. Peer J. 7: e6634. doi:10.7717/peerj.6634.

125.) Pachathundikandi, S.K., Tegtmeyer, N., Arnold, I.C., Lind, J., Neddermann, M., Falkeis-Veits, C., Chattopadhyay, S., Brönstrup, M., Tegge, W., Hong, M., Sticht, H., Vieth, M., Müller, A., Backert, S. (2019).
T4SS-dependent TLR5 activation by Helicobacter pylori infection. Nature Commununications 10: 5717. doi:10.1038/s41467-019-13506-6.

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127.) Zarzecka, U., Modrak-Wójcik, A., Figaj, D., Apanowicz, M., Lesner, A., Bzowska, A., Lipinska, B., Zawilak-Pawlik, A., Backert, S., Skorko-Glonek, J. (2019).
Properties of the HtrA Protease From Bacterium Helicobacter pylori Whose Activity Is Indispensable for Growth Under Stress Conditions. Frontiers in Microbiology 10: 961. doi:10.3389/fmicb.2019.00961.

128.) Zawilak-Pawlik, A., Zarzecka, U., Żyła-Uklejewicz, D., Lach, J., Strapagiel, D., Tegtmeyer, N., Böhm, M., Backert, S., Skorko-Glonek, J. (2019).
Establishment of serine protease htrA mutants in Helicobacter pylori is associated with secA mutations. Science Reports 9(1): 11794. doi:10.1038/s41598-019-48030-6.

129.) Buß, M., Tegtmeyer, N., Schnieder, J, Dong, X., Li, J., Springer, T.A., Backert, S., Niemann, H.H. (2019).
Specific high affinity interaction of Helicobacter pylori CagL with integrin αV β6 promotes type IV secretion of CagA into human cells. FEBS Journal 286(20): 3980-3997. doi:10.1111/febs.14962.

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Immunopathological properties of the Campylobacter jejuni flagellins and the adhesin CadF as assessed in a clinical murine infection model. Gut Pathogogens 11:24. doi:10.1186/s13099-019-0306-9.

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Campylobacter jejuni Serine Protease HtrA Cleaves the Tight Junction Component Claudin-8. Frontiers in Cellular and Infection Microbiology 8(10): 590186. doi:10.3389/fcimb.2020.590186.

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SHP2-Independent Tyrosine Dephosphorylation of Cortactin and Vinculin during Infection with Helicobacter pylori. European Journal of Microbiology and Immunology (Bp) 10(1): 20-27. doi:10.1556/1886.2020.00001.

138.) Heimesaat, M.M., Schmidt, A.M., Mousavi, S., Escher, U., Tegtmeyer, N., Wessler, S., Gadermaier, G., Briza, P., Hofreuter, D., Bereswill, S., Backert, S. (2020).
Peptidase PepP is a novel virulence factor of Campylobacter jejuni contributing to murine campylobacteriosis. Gut Microbes 12(1): 1770017. doi:10.1080/19490976.2020.1770017.

139.) Tegtmeyer, N., Backert, S. (2020).
Different roles of integrin-β1 and integrin-αv for type IV secretion of CagA versus cell elongation phenotype and cell lifting by Helicobacter pylori. PLoS Pathogens 16(7): e1008135. doi:10.1371/journal.ppat.1008135.

140.) Pachathundikandi, S.K., Blaser, N., Bruns, H., Backert, S. (2020).
Helicobacter pylori Avoids the Critical Activation of NLRP3 Inflammasome-Mediated Production of Oncogenic Mature IL-1β in Human Immune Cells. Cancers (Basel) 12(4): 803. doi:10.3390/cancers12040803.

141.) Hollandsworth, H.M., Schmitt, V., Amirfakhri, S., Filemoni, F., Schmidt, A., Landström, M., Lyndin, M., Backert, S., Gerhard, M., Wennemuth, G., Hoffman, R.M., Singer, B.B., Bouvet, M. (2020).
Fluorophore-conjugated Helicobacter pylori recombinant membrane protein (HopQ) labels primary colon cancer and metastases in orthotopic mouse models by binding CEA-related cell adhesion molecules. Translational Oncology 13(12): 100857.  doi:10.1016/j.tranon.2020.100857.

142.) Tegtmeyer, N., Ghete, T.D., Schmitt, V., Remmerbach, T., Cortes, M.C.C., Bondoc, E.M., Graf, H.L., Singer, B.B., Hirsch, C., Backert, S. (2020).
Type IV secretion of Helicobacter pylori CagA into oral epithelial cells is prevented by the absence of CEACAM receptor expression. Gut Pathogens 12: 25. doi:10.1186/s13099-020-00363-8.

143.) Zarzecka, U., Matkowska, D., Backert, S., Skorko-Glonek, J. (2020).
Importance of two PDZ domains for the proteolytic and chaperone activities of Helicobacter pylori serine protease HtrA. Cellular Microbiology. 23(4): e13299. doi:10.1111/cmi.13299.

144.) Berlamont, H., De Witte, C., De Bruyckere, S., Fox, J.G., Backert, S., Smet, A., Boyen, F., Haesebrouck, F. (2021).
Differentiation of Gastric Helicobacter Species Using MALDI-TOF Mass Spectrometry. Pathogens 10(3): 366. doi:10.3390/pathogens10030366.

145.) Maubach, G., Lim, M.C.C., Sokolova, O., Backert, S., Meyer, T.F., Naumann, M. (2021).
TIFA has dual functions in Helicobacter pylori-induced classical and alternative NF-κB pathways. EMBO Reports 22(9): e52878. doi:10.15252/embr.202152878.

146.) Lobo de Sá, F.D., Backert, S., Nattramilarasu, P.K., Mousavi, S., Sandle, G.I., Bereswill, S., Heimesaat, M.M., Schulzke, J.D., Bücker, R. (2021).
Vitamin D Reverses Disruption of Gut Epithelial Barrier Function Caused by Campylobacter jejuni. International Journal of Molecular Sciences 22(16): 8872. doi:10.3390/ijms22168872.

147.) Tegtmeyer, N., Harrer, A., Rottner, K., Backert, S. (2021).
Helicobacter pylori CagA Induces Cortactin Y-470 Phosphorylation-Dependent Gastric Epithelial Cell Scattering via Abl, Vav2 and Rac1 Activation. Cancers (Basel) 13(16): 4241. doi:10.3390/cancers13164241.

148.) Sharafutdinov, I., Backert, S., Tegtmeyer, N. (2021).
The Helicobacter pylori type IV secretion system upregulates epithelial cortactin expression by a CagA- and JNK-dependent pathway. Cellular Microbiology 23(10): e13376.  doi:10.1111/cmi.13376.

149.) Knorr, J., Sharafutdinov, I., Fiedler, F., Soltan Esmaeili, D., Rohde, M., Rottner, K., Backert, S., Tegtmeyer, N. (2021).
Cortactin Is Required for Efficient FAK, Src and Abl Tyrosine Kinase Activation and Phosphorylation of Helicobacter pylori CagA. International Journal of Molecular Sciences 22(11): 6045. doi:10.3390/ijms22116045.

150.) Sharafutdinov, I., Knorr, J., Soltan Esmaeilii, D., Backert, S., Tegtmeyer, N. (2021).
Cortactin Promotes Effective AGS Cell Scattering by Helicobacter pylori CagA, but not Cellular Vacuolization and Apoptosis Induced by the Vacuolating Cytotoxin VacA. Pathogens  11(1): 3.  doi:10.3390/pathogens11010003.

151.) Tegtmeyer, N., Soltan Esmaeilii, D., Sharafutdinov, I., Knorr, J., Naumann, N., Backert, S. (2022).
Importance of cortactin for efficient epithelial NF-κβ activation by Helicobacter pylori, Salmonella enterica and Pseudomonas aeruginosa, but not Campylobacter spp. European Journal of Microbiology and Immunology  11(4): 95-103.  doi:10.1556/1886.2021.00023.

152.) Tegtmeyer, N., Linz, B., Yamaoka, Y., N., Backert, S. (2022).
Unique TLR9 Activation by Helicobacter pylori Depends on the cag T4SS, But Not on VirD2 Relaxases or VirD4 Coupling Proteins. Current Microbiology 79(4): 121. doi:10.1007/s00284-002-0213-9.

153.) Haumaier, F., Schneider-Fuchs, A., Backert, S., Vieth, M., Sterlacci, W., Wöhrl, B.M. (2022).
Rapid Detection of Quinolone Resistance Mutations in gyrA of Helicobacter pylori by Real-Time PCR. Pathogens 11(1): 59. doi:10.3390/pathogens11010059.

154.) Sharafutdinov, I., Tegtmeyer, N., Müsken, M., Backert, S. (2022).
Campylobacter jejuni Serine Protease HtrA Induces Paracellular Transmigration of Microbiota across Polarized Intestinal Epithelial Cell. Biomolecules 12(4). 521. doi: 10.3390/biom12040521.

155.) Sharafutdinov, I., Ekici, A., Vieth, M.,  Backert, S., Linz, B. (2022).
Early and late genome-wide gastric epithelial transciptome response during infection with the human carcinogen Helicobacter pylori. Cell Insight 1: 100032. doi: 10.1016/j.cellin.2022.100032.

156.) Zarzecka, U. Tegtmeyer, N., Sticht, H., Backert, S. (2023).
Trimer stability of Helicobacter pylori  HtrA is regulated by a natural mutation in the protease domain. Medical Microbiology and Immunology 212: 241–252. doi:10.1007/s00430-023-00766-9.

157.) Sharafutdinov I., Tegtmeyer N.,  Linz B., Rohde M., Vieth M., Tay A.C.-Y., Lamichane B., Tuan V.P., Fauzia K.A., Sticht H., Yamaoka Y., Marshall B.J., Backert S. (2023).
A single nucleotide polymorphism in Helicobacter pylori promotes gastric cancer development. Cell Host & Microbe 31. doi: 10.1016/j.chom.2023.06.016.

158.) Thorell, K., Muñoz-Ramírez, Z.Y., Wang, D., Sandoval-Motta, S., Boscolo Agostini, R., Ghirotto, S., Torres, R.C.; HpGP Research Network; Falush, D., Camargo, M.C., Rabkin, C.S. (2023). 
The Helicobacter pylori Genome Project: insights into H. pylori population structure from analysis of a worldwide collection of complete genomes. Nature Communications 11; 14(1): 8184. doi: 10.1038/s41467-023-43562-y.

159.) Dregelies, T., Haumaier, F., Sterlacci, W., Backert, S., Vieth, M. (2023).                      
Detection of Fusobacterium nucleatum in Patients with Colitis-Associated Colorectal Cancer. Current Microbiology 80(9): 293. doi: 10.1007/s00284-023-03398-7.

160.) Sharafutdinov, I., Tegtmeyer, N., Rohde, M., Olofson, A., Rehmann, Z.U., Arnquist, A., Backert S.
Campylobacter jejuni Surface-Bound Protease HtrA, but Not the Secreted Protease nor Protease in Shed Membrane Vesicles, Disrupts Epithelial Cell-to-Cell Junctions. (2024). Cells 13(3): 224. doi: 10.3390/cells13030224.

161.) Sharafutdinov I., Harrer, A., Müsken, N., Rottner, K. Sticht H., Täger, C., Naumann, M., Tegtmeyer N., Backert S. (2024).
Cortactin-dependent control of Par1b-regulated epithelial cell polarity in Helicobacter infection. Cell Insight 3(3): 100161. doi: 10.1016/j.cellin.2024.100161.


Review Articles

162.) Backert, S., Nielsen, B.L., Börner, T. (1997).
The mystery of the rings: structure and replication of the mitochondrial genome in higher plants. Trends in Plant Sciences 2: 477-483. doi:10.1016/S1360-1385(97)01148-5.

163.) Backert, S., Churin Y., Meyer, T.F. (2002).
Helicobacter pylori type IV secretion, host cell signalling and vaccine development. Keio Journal of Medicine 51 Suppl. 2: 6-14. doi:10.2302/kjm.51.supplement2_6.

164.) Selbach, M., Backert, S. (2005).
Cortactin: an Achilles´ heel of the actin cytoskeleton targeted by pathogens. Trends in Microbiology 13: 181-189. doi:10.1016/j.tim.2005.02.007.

165.) König, W., H. Lauf, U. Arnold, I. Tammer, B. Ghebremedhin, A. Clarici, F.L. Thies, A. Drynda, A. Schmalcz, T. Kwok, R. Arnold, S. Backert, Werchau, H., König, B. (2004).
Natürliche und adaptive Immunität des Respirationstraktes – Bedeutung mikrobieller Faktoren für Infektabwehr und Sensibilisierung, Atemwegs & Lungenkrankungen, 30, Teil 1 Nr. 11: 551–568.

166.) König, W., Lauf, H., Arnold, U., Tammer, I., Ghebremedhin, B., Clarici, A., Thies, F.L., Drynda, A., Schmalcz, A., Kwok, T., Arnold, R., Backert, S., Werchau, H., König, B. (2004).
Natürliche und adaptive Immunität des Respirationstraktes – Bedeutung mikrobieller Faktoren für Infektabwehr und Sensibilisierung, Atemwegs & Lungenkrankungen 30, Teil 2 Nr. 12: 605-620.

167.) König, W., H. Lauf, U. Arnold, I. Tammer, B. Ghebremedhin, A. Clarici, F.L. Thies, A. Drynda, A. Schmalcz, T. Kwok, R. Arnold, Backert, S., Werchau, H., König, B. (2005).
Natürliche und adaptive Immunität des Respirationstraktes – Bedeutung mikrobieller Faktoren für Infektabwehr und Sensibilisierung, Atemwegs & Lungenkrankungen 31, Teil3 Nr. 4: 188-203.

168.) Backert, S., Selbach, M. (2005).
Tyrosine-phosphorylated microbial effector proteins: the enemies within. Trends in Microbiology 13: 476-484. doi:10.1016/j.tim.2005.08.002.

169.) Backert, S., König, W. (2005).
Interplay of bacterial toxins with host defence: molecular mechanisms of immunomodulatory signaling. International Journal of Medical Microbiology 295: 519-530. doi:10.1016/j.ijmm.2005.06.011.

170.) Backert, S., Meyer, T.F. (2006).
Type IV secretion systems and their effector proteins in bacterial pathogenesis. Current Opinion in Microbiology 9: 207-217. doi:10.1016/j.mib.2006.02.008.

171.) Backert, S., Fischer, W. (2007).
Transport von Proteinen und DNA: Typ IV-Sekretion bei Gram-negativen Bakterien. Naturwissenschaftliche Rundschau 60: 10-17.

172.) Backert, S., Feller, S.M., Wessler, S. (2008).
Emerging roles of Abl family tyrosine kinases in microbial pathogenesis.
Trends in Biochemical Sciences 33: 80-90. doi:10.1016/j.tibs.2007.10.006.

173.) Hänel, I., Alter, T., Backert, S. (2008).
25th Jenaer Symposium: Campylobacter Infections. Bundesgesundheitsblatt Gesundheitsforschung Gesundheitsschutz. 51: 1347-1352. doi:10.1007/s00103-008-0705-4.

174.) Wessler, S., Backert, S. (2008).
Molecular mechanisms of epithelial-barrier disruption by Helicobacter pylori. Trends in Microbiology 16: 397-405. doi:10.1016/j.tim.2008.05.005.

175.) Backert, S., Selbach, M. (2008).
Role of type IV secretion in Helicobacter pylori pathogenesis. Cellular Microbiology 10: 1573-1581. doi:10.1111/j.1462-5822.2008.01156.x.

176.) Torres, J., Backert, S. (2008).
Pathogenesis of Helicobacter pylori infection. Helicobacter 13 (Suppl. 1): 13-17. doi:10.1111/j.1523-5378.2008.00630.x.

177.) Backert, S., Fronzes, R., Waksman, G. (2008).
VirB2 and VirB5 proteins: specialized adhesins in bacterial type-IV secretion systems? Trends in Microbiology 16: 409-413. doi:10.1016/j.tim.2008.07.001.

178.) Backert, S., Kenny, B., Gerhard, R., Tegtmeyer, N., Brandt, S. (2010).
PKA-mediated phosphorylation of EPEC-Tir at serine residues 434 and 463: A novel pathway in regulating Rac1 GTPase function. Gut Microbes 1: 94-99. doi:10.4161/gmic.1.2.11437.

179.) Backert, S., Tegtmeyer, N. (2010).
The Versatility of the Helicobacter pylori Vacuolating Cytotoxin VacA in Signal Transduction and Molecular Crosstalk. Toxins 2: 69-92. doi:10.3390/toxins2010069.

180.) Stradal. T.E.B., Backert, S. (2010).
Wie EHEC das Aktinzytoskelett der Wirtszelle beeinflussen. Biospektrum 16: 624-627.

181.) Backert, S., Naumann, M., (2010).
What a disorder: pro-inflammatory signaling pathways  induced by Helicobacter pylori . Trends in Microbiology 18: 479-486. doi:10.1016/j.tim.2010.08.003.

182.) Tegtmeyer, N., Backert, S., (2011).
Role of Abl and Src family kinases in actin-cytoskeletal rearrangements induced by the Helicobacter pylori CagA protein. European Journal of Cell Biology 90: 880-890. doi:10.1016/j.ejcb.2010.11.006.

183.) Backert, S., Clyne., M (2011).
Pathogenesis of Helicobacter pylori infection. Helicobacter 16: 19-25. doi:10.1111/j.1523-5378.2011.00876.x.

184.) Backert, S., Clyne, M., Tegtmeyer, N. (2011).
Molecular mechanisms of gastric epithelial cell adhesion and injection of CagA by Helicobacter pylori. Cell Communication & Signaling 9: 28-35. doi:10.1186/1478-811X-9-28.

185.) Tegtmeyer, N., Wessler, S., Backert, S. (2011).
Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis. FEBS Journal 278: 1190-1202. doi:10.1111/j.1742-4658.2011.08035.x.

186.) Ó Cróinín, T., Backert, S. (2012).
Host epithelial cell invasion by Campylobacter jejuni: trigger or zipper mechanism? Frontiers in Cellular & Infection Microbiology 2: 25. doi:10.3389/fcimb.2012.00025.

187.) Gölz, S., Sharbati, S., Backert, S., Alter T. (2012).
Quorum sensing dependant phenotypes and their molecular mechanisms in Campylobacterales. European Journal of Microbiology & Immunology 2: 50-60. doi:10.1556/EuJMI.2.2012.1.8.

188.) Backert, S., Tegtmeyer, N. (2012).
Helicobacter pylori CagA tertiary structure reveals functional insights. CELL host & microbe 12: 3-5. doi:10.1016/j.chom.2012.07.001.

189.) Smolka, A.J., Backert, S. (2012).
How Helicobacter pylori infection controls gastric acid secretion. Journal of Gastroenterology 47: 609-618. doi:10.1007/s00535-012-0592-1.

190.) Backert, S., Hofreuter, D. (2013).
Molecular methods to investigate adhesion, transmigration, invasion and intracellular survival of the foodborne pathogen Campylobacter jejuni. Journal of Microbiological Methods 95: 8-23. doi:10.1016/j.mimet.2013.06.031.

191.) Backert, S., Boehm, M., Wessler, S., Tegtmeyer, N. (2013).
Transmigration route of Campylobacter jejuni across polarized intestinal epithelial cells: paracellular, transcellular or both? CELL Communication and Signaling 11: 72. doi:10.1186/1478-811X-11-72.

192.) Posselt, G., Backert, S., Wessler, S. (2013).
The functional interplay of Helicobacter pylori factors with gastric epithelial cells induces a multi-step process in pathogenesis. CELL Communication and Signaling 11: 77. doi:10.1186/1478-811X-11-77.

193.) Pachathundikandi, S.K., Tegtmeyer, N., Backert, S. (2013).
Signal transduction of Helicobacter pylori during interaction with host cell protein receptors of epithelial and immune cells. Gut Microbes 4: 454-474. doi:10.4161/gmic.27001.

194.) Fernandez-Gonzalez, E., Backert, S. (2014).
DNA transfer in the gastric pathogen Helicobacter pylori. Journal of Gastroenterology 49: 594-604. doi:10.1007/s00535-014-0938-y.

195.) Pachathundikandi, S.K., Lind, J., Tegtmeyer, N., El-Omar, E.M., Backert, S. (2015).
Interplay of the gastric pathogen Helicobacter pylori with Toll-like receptors. BioMedical Research International 2015: 192420. doi:10.1155/2015/192420.

196.) Backert, S., Tegtmeyer, N., Fischer, W. (2015).
Composition, structure and function of the Helicobacter pylori cag pathogenicity island encoded type IV secretion system. Future Microbiology 10: 955-965. doi:10.2217/fmb.15.32.

197.) Backert, S., Neddermann, M., Maubach, G., Naumann, M. (2016).
Pathogenesis of Helicobacter pylori infection. Helicobacter 21 (Suppl 1): 19-25. doi:10.1111/hel.12335.

198.) Backert, S., Blaser, M.J. (2016).
The Role of CagA in the Gastric Biology of Helicobacter pylori. Cancer Research 76: 4028-4031. doi:10.1158/0008-5472.CAN-16-1680.

199.) Pachathundikandi, S.K., Müller, A., Backert, S. (2016).
Inflammasome Activation by Helicobacter pylori and Its Implications for Persistence and Immunity. Current Topics in Microbiology and Immunology 397: 117-131. doi:10.1007/978-3-319-41171-2_6.

200.) Tegtmeyer, N., Neddermann, M., Asche, C.I., Backert, S. (2017).
Subversion of host kinases: a key network in cellular signaling hijacked by Helicobacter pylori CagA. Molecular Microbiology 105: 358-372. doi:10.1111/mmi.13707.

201.) Backert, S., Tegtmeyer, N. (2017).
Type IV Secretion and Signal Transduction of Helicobacter pylori CagA through Interactions with Host Cell Receptors. Toxins (Basel) 9: 115. doi:10.3390/toxins9040115.

202.) Backert, S., Schmidt, T.P., Harrer, A, Wessler, S. (2017).
Exploiting the Gastric Epithelial Barrier: Helicobacter pylori’s Attack on Tight and Adherens Junctions. Current Topics in Microbiology and Immunology 400: 195-226. doi:10.1007/978-3-319-50520-6_9.

203.) Wessler, S., Schneider, G., Backert, S. (2017).
Bacterial serine protease HtrA as a promising new target for antimicrobial therapy? Journal of Cell Communication and Signaling 15: 4. doi:10.1186/s12964-017-0162-5.

204.) Naumann, M., Sokolova, O., Tegtmeyer, N., Backert, S. (2017).
Helicobacter pylori: A Paradigm Pathogen for Subverting Host Cell Signal Transmission. Trends in Microbiology 25: 316-328. doi:10.1016/j.tim.2016.12.004.

205.) Wessler, S., Backert, S. (2017).
A novel basolateral type IV secretion model for the CagA oncoprotein of Helicobacter pylori. Microbial Cell 5: 60-62. doi:10.15698/mic2018.01.611.

206.) Backert, S., Haas, R., Gerhard, M., Naumann, M. (2017).
The Helicobacter pylori Type IV Secretion System Encoded by the cag Pathogenicity Island: Architecture, Function, and Signaling. Current Topics in Microbiology and Immunology 413: 187-220. doi:10.1007/978-3-319-75241-9_8.

207.) Grohmann, E., Christie, P.J., Waksman, G., Backert, S. (2018).
Type IV Secretion in Gram-negative and Gram-positive Bacteria. Molecular Microbiology 107: 455-471. doi:10.1111/mmi.13896. Erratum in:  Current Topics in Microbiology and Immunology 2017; 413: E1. doi:10.1007/978-3-319-75241-9_14.

208.) Backert, S., Bernegger, S., Skórko-Glonek, J., Wessler, S. (2018).
Extracellular HtrA serine proteases: An emerging new strategy in bacterial pathogenesis. Cellular Microbiology 20: e12845. doi:10.1111/cmi.12845.

209.) Pachathundikandi, K., Backert, S. (2018).
Heptose 1,7-Bisphosphate Directed TIFA Oligomerization: A Novel PAMP-Recognizing Signaling Platform in the Control of Bacterial Infections. Gastroenterology 154: 778-783. doi:10.1053/j.gastro.2018.01.009.

210.) Boehm, M., Simson, D., Escher, U., Schmidt, A.M., Bereswill, S., Tegtmeyer, N., Backert, S., Heimesaat, M.M. (2018).
Function of Serine Protease HtrA in the Lifecycle of the Foodborne Pathogen Campylobacter jejuni. European Journal of Microbiology and Immunology (Bp) 8: 70-77. doi:10.1556/1886.2018.00011.

211.) Pachathundikandi, S.K., Blaser, N., Backert, S. (2019).
Mechanisms of Inflammasome Signaling, microRNA Induction and Resolution of Inflammation by Helicobacter pylori. Current Topics in Microbiology and Immunology 421: 267-302. doi:10.1007/978-3-030-15138-6_11.

212.) Rudnicka, K., Backert, S, Chmiela, M. (2019).
Genetic Polymorphisms in Inflammatory and Other Regulators in Gastric Cancer: Risks and Clinical Consequences. Current Topics in Microbiology and Immunology 421: 53-76. doi:10.1007/978-3-030-15138-6_3.

213.) Blaser, N., Backert S, Pachathundikandi, S.K. (2019).
Immune Cell Signaling by Helicobacter pylori: Impact on Gastric Pathology. Advances in Experimental Medical Biology 1149: 77-106. doi:10.1007/5584_2019_360.

214.) Knorr, J., Ricci, V., Hatakeyam,a M., Backert, S. (2019).
Classification of Helicobacter pylori Virulence Factors: Is CagA a Toxin or Not? Trends in Microbiology 27: 731-738. doi:10.1016/j.tim.2019.04.010.

215.) Sharafutdinov, I., Backert, S., Tegtmeyer, N. (2020).
Cortactin: A Major Cellular Target of the Gastric Carcinogen Helicobacter pylori. Cancers (Basel).12(1). pii: E159. doi:10.3390/cancers12010159.

216.) Fischer, W., Tegtmeyer, N., Stingl, K., Backert, S. (2020).
Four Chromosomal Type IV Secretion Systems in Helicobacter pylori: Composition, Structure and Function. Frontiers in Microbiology 11: 1592. doi:10.3389/fmicb.2020.01592.

217.) Tegtmeyer, N., Sharafutdinov, I., Harrer, A., Soltan Esmaeili, D., Linz, B., Backert, S. (2021).
Campylobacter Virulence Factors and Molecular Host-Pathogen Interactions. Current Topics in Microbiology and Immunology 431: 169-202. doi:10.1007/978-3-030-65481-8_7.

218.) Heimesaat, M.M., Backert, S., Alter, T., Bereswill, S. (2021).
Human Campylobacteriosis-A Serious Infectious Threat in a One Health Perspective. Current Topics in Microbiology and Immunology 431: 1-23. doi: 10.1007/978-3-030-65481-8_1.

219.) Alter, T., Bereswill, S., Backert, S. (2021).
Campylobacteriose – eine zoonotische Infektionskrankheit. Biospektrum 06: 591-593. 27. Jahrgang.

220.) Linz, B., Backert, S. (2021).
Helicobacter pylori and the gut microbiota. Microbiota Health Disease 3: e592. doi: 10.26355/mhd_20219_592.

221.) Sharafutdinov, I., Knorr, J., Rottner, K., Backert, S., Tegtmeyer, N. (2022).
Cortactin: A universal host cytoskeletal target of Gram-negative and Gram-positive bacterial pathogens. Molecular Microbiology 118 (6): 623-636. doi: 10.1111/mmi.15002.

222.) Heimesaat, M.M., Backert, S., Alter, T., Bereswill, S. (2023).
Molecular targets in Campylobacter Infections. Biomolecules 13 (3): 409. doi: 10.3390/biom13030409.

223.) Linz, B., Sharafutdinov, I., Tegtmeyer, N., Backert, S. (2023).
Evolution and Role of Proteases in Campylobacter jejuni Lifestyle and Pathogenesis. Biomolecules 13 (2): 323. doi: 10.3390/biom13020323.

224.) Pachathundikandi, S.K., Tegtmeyer, N., Backert, S. (2023).
Masking of typical TLR4 and TLR5 ligands modulates inflammation and resolution by Helicobacter pylori. Trends in Microbiology: S0966-842X(23)00089-6. doi: 10.1016/j.tim.2023.03.009.

225.) Linz, B., Sticht, H., Tegtmeyer, N., Backert, S. (2024).
Cancer-associated SNPs in bacteria: lessons from Helicobacter pylori. Trends in Microbiology: S0966-842X(24)00041-6. doi: 10.1016/j.tim.2024.02.001.

226.) Backert, S., Tegtmeyer, N., Horn, A.H.C., Sticht, H., Linz, B. (2024).
Two remarkable serine/leucine polymorphisms in Helicobacter pylori: functional importance for serine protease HtrA and adhesin BabA. Cell Commun Signal 22 (1): 250. doi: 10.1186/s12964-024-01635-5.

Books and book chapters

227.) Backert, S. (1996).
Untersuchungen zur Struktur und Replikation des Mitochondriengenoms von Chenopodium album (L.), Shaker-Verlag, Aachen ISBN 3-8265-1383-5.

228.) Backert, S., Moyer, P., Böhm, C., Riecken, E.-O., Hanski, C. (1998).
Differential gene expression in cell lines derived from colon carcinoma or normal colonic mucosa, Jahrbuch der 8. Wissenschaftswoche an der FU-Berlin. pp.45-46. ISBN 3-9806076-5-8.

229.) Backert, S., König, W., Arnold, R., König, B. (2006).
Induction and modulation of inflammatory networks by bacterial protein toxins. In “The Sourcebook of Bacterial Protein Toxins”, edited by J. E. Alouf, M. R. Popoff, Academic Press, New York. Section V, Chapter 54: pp. 887-918. ISBN 978-1-84593-594-8.

230.) Backert, S., H. Mimuro, D.A. Israel, R.M. Peek jr. (2010).
Virulence factors in Helicobacter pylori, in: Helicobacter pylori in the 21st century. CABI-Verlag, edited by: P. Sutton and H.M. Mitchell, pp. 212-247. ISBN 978-1-84593-594-8.

231.) Wessler, S., Backert, S., (2011).
The Abl Family of Tyrosine Kinases and Microbial Pathogenesis. International Reviews in Cell and Molecular Biology 286, Elsevier, edited by Kwang W. Jeon, pp. 271-300. ISBN 978-0-12385-859-7. doi:10.1016/B978-0-12-385859-7.00006-9.

232.) Oyarzabal, O.A., Backert, S. Eds. (2012).
Microbial Food Safety, Springer New York, ISBN 978-1-4614-1176-5.

233.) Tegtmeyer, N., Rohde, M., Backert, S. (2012).
Clinical presentations and pathogenicity mechanisms of bacterial foodborne diseases. In “Microbial Food Safety”, Springer New York, edited by O.A. Oyarzabal & S. Backert. ISBN 978-1-4614-1176-5.

234.) Oyarzabal, O.A., Backert, S. Eds. (2012).
Food safety resources. In “Microbial Food Safety”, Springer Nature Switzerland, edited by O.A. Oyarzabal & S. Backert. ISBN 978-1-4614-1176-5.

235.) Backert, S., Zanotti, G., Lind, J., Asche, C.I., Tegtmeyer, N. (2016).
Roles of the cagPAI and CagA on gastroduodenal diseases. In “Helicobacter pylori research: from bench to bedside”, Springer Nature Switzerland, edited by S. Backert & Y. Yamaoka, ISBN-10: 4431559345.

236.) Backert, S., Y. Yamaoka Eds. (2016).
Helicobacter pylori research: from bench to bedside”, Springer Nature Switzerland, edited by S. Backert & Y. Yamaoka, ISBN-10: 4431559345.

237.) Oyarzabal, O.A., Backert, S. (2016).
Control of Campylobacter spp. in Commercial Poultry Production. In “Campylobacter spp. and related organisms in poultry: relationship pathogen host, diagnosis and epidemiology”, Springer Nature Switzerland, edited by B.B. Fonseca, D.A. Rossi & H. Fernandez, ISBN 978-3-319-29907-5.

238.) Backert, S., Tegtmeyer, N., O’Croinin, T., Böhm, M., Heimesaat, M. (2016).
Human Campylobacteriosis. In ”Features, Detection and Prevention of Foodborne Disease: Campylobacter”, Elsevier, edited by G. Klein ISBN 978-0-12-803623-5.

239.) Backert, S. Ed. (2016).
“Inflammasome signalling and bacterial infections”, Springer Nature Switzerland, edited by S. Backert. ISBN 978-3-319-41170-5.

240.) Backert, S. (2016).
Preface in “Inflammasome signalling and bacterial infections”, Springer Nature Switzerland, edited by S. Backert. pp. 5-6, ISBN 978-3-319-41170-5.

241.) Oyarzabal, O.A., Backert, S. (2017).
Varying pathogenicity of Campylobacter jejuni isolates. In “Foodborne Pathogens: Virulence Factors and Host Susceptibility”, Springer Nature Switzerland, edited by J. Gurtler, ISBN 978-3-319-56836-2.

242.) Tegtmeyer, N., Backert, S. (2017).
Molecular pathogenesis and signal transduction by Helicobacter pylori, Springer Nature Switzerland, ISBN 978-3-319-505190.

243.) Tegtmeyer, N., Backert, S. (2017).
Preface in ”Molecular pathogenesis and signal transduction by Helicobacter pylori”. pp. 9-11. Springer, ISBN 978-3-319-50520-6.

244.) Backert, S., Grohmann, E. Eds. (2017).
Type IV Secretion in Gram-positive and Gram-negative Bacteria. Springer Nature Switzerland, ISBN 9783319752402.

245.) Backert, S. Ed. (2019).
Molecular mechanisms of inflammation: induction, resolution and escape by Helicobacter pylori. Springer Nature Switzerland, ISBN 978-3030151379.

246.) Kamiya, S., Backert S. Eds. (2019).
Helicobacter pylori in human diseases. Springer Nature Switzerland, ISBN 978-3-030-21916-1.

247.) Backert, S. Ed. (2021).
Fighting Campylobacter InfectionsTowards a One Health Approach. Springer Nature Switzerland, ISBN 978-3-030-65480-1. doi:10.1007/978-3-030-65481-8.

248.) Backert, S. Ed. (2023).
Helicobacter pylori and Gastric Cancer. Springer Nature Switzerland, ISBN 978-3-031-47330-2. doi: 10.1007/978-3-031-47331-9.

249.) Backert, S., Linz, B., Tegtmeyer, N. (2023).
Helicobacter pylori-Induced Host Cell DNA Damage and Genetics of Gastric Cancer Developement. In ” Helicobacter pylori and Gastric Cancer“. pp. 185-206, Springer Nature Switzerland, edited by S. Backert. ISBN 978-3-031-47330-2. doi:10.1007/978-3-031-47331-9_7.

250.) Naumann, M., Ferino, L., Sharafutdinov, I., Backert, S. (2023).
Gastric Epithelial Barrier Disruption, Inflammation and Oncogenic Signal Transduction by Helicobacter pylori. In ” Helicobacter pylori and Gastric Cancer“. pp. 207-238, Springer Nature Switzerland, edited by S. Backert. ISBN 978-3-031-47330-2. doi: 10.1007/978-3-031-47331-9_8.