{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T00:18:54Z","timestamp":1790036334418,"version":"4.0.1"},"reference-count":101,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2020,6,17]],"date-time":"2020-06-17T00:00:00Z","timestamp":1592352000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2020,6,17]],"date-time":"2020-06-17T00:00:00Z","timestamp":1592352000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Eur J Clin Microbiol Infect Dis"],"published-print":{"date-parts":[[2020,10]]},"DOI":"10.1007\/s10096-020-03948-y","type":"journal-article","created":{"date-parts":[[2020,7,8]],"date-time":"2020-07-08T06:03:43Z","timestamp":1594188223000},"page":"1821-1830","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":113,"title":["Virulence of Helicobacter pylori outer membrane proteins: an updated review"],"prefix":"10.1007","volume":"39","author":[{"given":"Chenjing","family":"Xu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Djaleel Muhammad","family":"Soyfoo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2975-3682","authenticated-orcid":false,"given":"Shunfu","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,6,17]]},"reference":[{"issue":"2","key":"3948_CR1","doi-asserted-by":"publisher","first-page":"420","DOI":"10.1053\/j.gastro.2017.04.022","volume":"153","author":"JKY Hooi","year":"2017","unstructured":"Hooi JKY, Lai WY, Ng WK, Suen MMY, Underwood FE, Tanyingoh D, Malfertheiner P, Graham DY, Wong VWS, Wu JCY, Chan FKL, Sung JJY, Kaplan GG (2017) Global prevalence of Helicobacter pylori infection: systematic review and meta-analysis. Gastroenterology 153(2):420\u2013429. https:\/\/doi.org\/10.1053\/j.gastro.2017.04.022","journal-title":"Gastroenterology"},{"issue":"7","key":"3948_CR2","doi-asserted-by":"publisher","first-page":"868","DOI":"10.1111\/apt.14561","volume":"47","author":"M Zamani","year":"2018","unstructured":"Zamani M, Ebrahimtabar F, Zamani V, Miller WH, Alizadeh-Navaei R, Shokri-Shirvani J (2018) Systematic review with meta-analysis: the worldwide prevalence of Helicobacter pylori infection. Aliment Pharmacol Ther 47(7):868\u2013876. https:\/\/doi.org\/10.1111\/apt.14561","journal-title":"Aliment Pharmacol Ther"},{"issue":"8","key":"3948_CR3","doi-asserted-by":"publisher","first-page":"e0137078","DOI":"10.1371\/journal.pone.0137078","volume":"10","author":"A Kim","year":"2015","unstructured":"Kim A, Servetas SL, Kang J, Kim J, Jang S, Cha HJ, Lee WJ, Kim J, Romero-Gallo J, Peek RM, Merrell DS (2015) Helicobacter pylori bab paralog distribution and association with cagA, vacA, and homA\/B genotypes in American and South Korean clinical isolates. PLoS One 10(8):e0137078. https:\/\/doi.org\/10.1371\/journal.pone.0137078","journal-title":"PLoS One"},{"key":"3948_CR4","doi-asserted-by":"publisher","unstructured":"Kalach N, Bontems P (2017) Helicobacter pylori infection in children. Helicobacter. https:\/\/doi.org\/10.1111\/hel.12414","DOI":"10.1111\/hel.12414"},{"issue":"2","key":"3948_CR5","doi-asserted-by":"publisher","first-page":"e12462","DOI":"10.1111\/hel.12462","volume":"23","author":"KF Boehnke","year":"2018","unstructured":"Boehnke KF, Brewster RK, S\u00e1nchez BN, Valdivieso M, Bussalleu A, Guevara M, Saenz CG, Alva SO, Gil E (2018) An assessment of drinking water contamination with Helicobacter pylori in Lima, Peru. Helicobacter 23(2):e12462. https:\/\/doi.org\/10.1111\/hel.12462","journal-title":"Helicobacter"},{"issue":"2","key":"3948_CR6","doi-asserted-by":"publisher","first-page":"e12471","DOI":"10.1111\/hel.12471","volume":"23","author":"F Siavoshi","year":"2018","unstructured":"Siavoshi F, Sahraee M, Ebrahimi H, Sarrafnejad A (2018) Natural fruits, flowers, honey, and honeybees harbor Helicobacter pylori-positive yeasts. Helicobacter 23(2):e12471. https:\/\/doi.org\/10.1111\/hel.12471","journal-title":"Helicobacter"},{"issue":"2","key":"3948_CR7","doi-asserted-by":"publisher","DOI":"10.1111\/hel.12563","volume":"24","author":"Q Chen","year":"2019","unstructured":"Chen Q, Liang X, Long X, Yu L, Liu W (2019) Cost-effectiveness analysis of screen-and-treat strategy in asymptomatic Chinese for preventing Helicobacter pylori-associated diseases. Helicobacter 24(2):e12563. https:\/\/doi.org\/10.1111\/hel.12563","journal-title":"Helicobacter"},{"issue":"7507","key":"3948_CR8","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1038\/nature13484","volume":"511","author":"S Qiao","year":"2014","unstructured":"Qiao S, Luo Q, Zhao Y, Zhang XC, Huang Y (2014) Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. Nature 511(7507):108\u2013111. https:\/\/doi.org\/10.1038\/nature13484","journal-title":"Nature"},{"issue":"6","key":"3948_CR9","doi-asserted-by":"publisher","first-page":"676","DOI":"10.1111\/mmi.13908","volume":"107","author":"AJF Egan","year":"2018","unstructured":"Egan AJF (2018) Bacterial outer membrane constriction. Mol Microbiol 107(6):676\u2013687. https:\/\/doi.org\/10.1111\/mmi.13908","journal-title":"Mol Microbiol"},{"key":"3948_CR10","doi-asserted-by":"publisher","unstructured":"Waskito LA, Salama NR (2018) Pathogenesis of Helicobacter pylori infection. Helicobacter:e12516. https:\/\/doi.org\/10.1111\/hel.12516","DOI":"10.1111\/hel.12516"},{"issue":"2","key":"3948_CR11","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1046\/j.1365-2958.2000.01983.x","volume":"37","author":"R Koebnik","year":"2000","unstructured":"Koebnik R, Locher KP (2000) Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37(2):239\u2013253. https:\/\/doi.org\/10.1046\/j.1365-2958.2000.01983.x","journal-title":"Mol Microbiol"},{"issue":"7","key":"3948_CR12","doi-asserted-by":"publisher","first-page":"4155","DOI":"10.1128\/iai.68.7.4155-4168.2000","volume":"68","author":"RA Alm","year":"2000","unstructured":"Alm RA, Bina J, Andrews BM, Doig P, Hancock RE (2000) Comparative genomics of Helicobacter pylori: analysis of the outer membrane protein families. Infect Immun 68(7):4155\u20134168. https:\/\/doi.org\/10.1128\/iai.68.7.4155-4168.2000","journal-title":"Infect Immun"},{"issue":"12","key":"3948_CR13","doi-asserted-by":"publisher","first-page":"4364","DOI":"10.1128\/iai.00977-12","volume":"80","author":"L Kennemann","year":"2012","unstructured":"Kennemann L, Brenneke B, Andres S, Engstrand L, Meyer TF, Aebischer T, Josenhans C (2012) In vivo sequence variation in HopZ, a phase-variable outer membrane protein of Helicobacter pylori. Infect Immun 80(12):4364\u20134373. https:\/\/doi.org\/10.1128\/iai.00977-12","journal-title":"Infect Immun"},{"key":"3948_CR14","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1186\/1471-2180-9-248","volume":"9","author":"M Oleastro","year":"2009","unstructured":"Oleastro M, Cordeiro R, M\u00e9nard A, Yamaoka Y, Queiroz D, M\u00e9graud F (2009) Allelic diversity and phylogeny of homB, a novel co-virulence marker of Helicobacter pylori. BMC Microbiol 9:248. https:\/\/doi.org\/10.1186\/1471-2180-9-248","journal-title":"BMC Microbiol"},{"issue":"19","key":"3948_CR15","doi-asserted-by":"publisher","first-page":"3421","DOI":"10.1128\/jb.01956-14","volume":"196","author":"VC Harvey","year":"2014","unstructured":"Harvey VC, Acio CR, Bredehoft AK, Zhu L, Hallinger DR, Quinlivan-Repasi V, Harvey SE (2014) Repetitive sequence variations in the promoter region of the adhesin-encoding gene sabA of Helicobacter pylori affect transcription. J Bacteriol 196(19):3421\u20133429. https:\/\/doi.org\/10.1128\/jb.01956-14","journal-title":"J Bacteriol"},{"issue":"1","key":"3948_CR16","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/j.chom.2015.12.004","volume":"19","author":"K Moonens","year":"2016","unstructured":"Moonens K, Gideonsson P, Subedi S, Bugaytsova J, Roma\u00f5 E, Mendez M, Nord\u00e9n J, Fallah M, Rakhimova L, Shevtsova A, Lahmann M, Castaldo G, Br\u00e4nnstr\u00f6m K, Coppens F, Lo AW, Ny T, Solnick JV, Vandenbussche G, Oscarson S, Hammarstr\u00f6m L, Arnqvist A, Berg DE, Muyldermans S, Bor\u00e9n T (2016) Structural insights into polymorphic ABO glycan binding by Helicobacter pylori. Cell Host Microbe 19(1):55\u201366. https:\/\/doi.org\/10.1016\/j.chom.2015.12.004","journal-title":"Cell Host Microbe"},{"issue":"2","key":"3948_CR17","doi-asserted-by":"publisher","first-page":"1160","DOI":"10.1128\/iai.69.2.1160-1171.2001","volume":"69","author":"DT Pride","year":"2001","unstructured":"Pride DT, Meinersmann RJ, Blaser MJ (2001) Allelic variation within Helicobacter pylori babA and babB. Infect Immun 69(2):1160\u20131171. https:\/\/doi.org\/10.1128\/iai.69.2.1160-1171.2001","journal-title":"Infect Immun"},{"issue":"11","key":"3948_CR18","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0187225","volume":"12","author":"S Ansari","year":"2017","unstructured":"Ansari S, Kabamba ET, Shrestha PK, Aftab H, Myint T, Tshering L, Sharma RP, Ni N, Aye TT, Subsomwong P, Uchida T, Ratanachu-Ek T, Vilaichone RK, Mahachai V, Matsumoto T, Akada J (2017) Helicobacter pylori bab characterization in clinical isolates from Bhutan, Myanmar, Nepal and Bangladesh. PLoS One 12(11):e0187225. https:\/\/doi.org\/10.1371\/journal.pone.0187225","journal-title":"PLoS One"},{"issue":"5349","key":"3948_CR19","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1126\/science.279.5349.373","volume":"279","author":"D Ilver","year":"1998","unstructured":"Ilver D, Arnqvis A, Ogren J, Frick IM, Kersulyte D, Incecik ET, Berg DE, Covacci A, Engstrand L (1998) Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging. Science 279(5349):373\u2013377. https:\/\/doi.org\/10.1126\/science.279.5349.373","journal-title":"Science"},{"issue":"3","key":"3948_CR20","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1006\/jmbi.2001.5311","volume":"316","author":"DT Pride","year":"2002","unstructured":"Pride DT, Blaser MJ (2002) Concerted evolution between duplicated genetic elements in Helicobacter pylori. J Mol Biol 316(3):640\u2013642. https:\/\/doi.org\/10.1006\/jmbi.2001.5311","journal-title":"J Mol Biol"},{"issue":"48","key":"3948_CR21","doi-asserted-by":"publisher","first-page":"16923","DOI":"10.1073\/pnas.0404817101","volume":"101","author":"A B\u00e4ckstr\u00f6m","year":"2004","unstructured":"B\u00e4ckstr\u00f6m A, Lundberg C, Kersulyte D, Berg DE, Bor\u00e9n T (2004) Metastability of Helicobacter pylori bab adhesin genes and dynamics in Lewis b antigen binding. Proc Natl Acad Sci U S A 101(48):16923\u201316928. https:\/\/doi.org\/10.1073\/pnas.0404817101","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6","key":"3948_CR22","doi-asserted-by":"publisher","first-page":"e02281","DOI":"10.1128\/mBio.02281-14","volume":"5","author":"S Nell","year":"2014","unstructured":"Nell S, Kennemann L, Schwarz S, Josenhans C (2014) Dynamics of Lewis b binding and sequence variation of the babA adhesin gene during chronic Helicobacter pylori infection in humans. mBio 5(6):e02281\u2013e02214","journal-title":"mBio"},{"key":"3948_CR23","doi-asserted-by":"publisher","first-page":"46499","DOI":"10.1038\/srep46499","volume":"7","author":"ME Kable","year":"2017","unstructured":"Kable ME, Hansen LM, Styer CM, Deck SL, Rakhimova O, Shevtsova A, Eaton KA, Martin ME, Gideonsson P, Bor\u00e9n T (2017) Host determinants of expression of the Helicobacter pylori BabA adhesin. Sci Rep 7:46499. https:\/\/doi.org\/10.1038\/srep46499","journal-title":"Sci Rep"},{"issue":"3","key":"3948_CR24","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1016\/j.chom.2017.02.013","volume":"21","author":"JA Bugaytsova","year":"2017","unstructured":"Bugaytsova JA, Bj\u00f6rnham O, Chernov YA, Gideonsson P, Henriksson S, Mendez M, Sj\u00f6str\u00f6m R, Mahdavi J, Shevtsova A, Ilver D, Moonens K, Quintana-Hayashi MP, Moskalenko R, Aisenbrey C, Bylund G, Schmidt A, \u00c5berg A, Br\u00e4nnstr\u00f6m K, K\u00f6niger V, Vikstr\u00f6m S, Rakhimova L, Hofer A, \u00d6gren J, Liu H, Goldman MD, Whitmire JM, \u00c5d\u00e9n J, Younson J, Kelly CG, Gilman RH, Chowdhury A, Mukhopadhyay AK, Nair GB, Papadakos KS, Martinez-Gonzalez B, Sgouras DN, Engstrand L, Unemo M, Danielsson D, Suerbaum S, Oscarson S, Morozova-Roche LA, Olofsson A, Gr\u00f6bner G, Holgersson J, Esberg A, Str\u00f6mberg N, Landstr\u00f6m M, Eldridge AM, Chromy BA, Hansen LM, Solnick JV, Lind\u00e9n SK, Haas R, Dubois A, Merrell DS, Schedin S, Remaut H, Arnqvist A, Berg DE (2017) Helicobacter pylori adapts to chronic infection and gastric disease via pH-responsive BabA-mediated adherence. Cell Host Microbe 21(3):376\u2013389. https:\/\/doi.org\/10.1016\/j.chom.2017.02.013","journal-title":"Cell Host Microbe"},{"issue":"7","key":"3948_CR25","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.1500315","volume":"1","author":"N Hage","year":"2015","unstructured":"Hage N, Howard T, Phillips C, Brassington C, Overman R, Debreczeni J, Gellert P, Stolnik S, Winkler GS (2015) Structural basis of Lewis(b) antigen binding by the Helicobacter pylori adhesin BabA. Sci Adv 1(7):e1500315. https:\/\/doi.org\/10.1126\/sciadv.1500315","journal-title":"Sci Adv"},{"issue":"9","key":"3948_CR26","doi-asserted-by":"publisher","first-page":"3782","DOI":"10.1128\/IAI.00364-09","volume":"77","author":"S Odenbreit","year":"2009","unstructured":"Odenbreit S, Swoboda K, Iris B, Stefan R, Rainer H (2009) Outer membrane protein expression profile in Helicobacter pylori clinical isolates. Infect Immun 77(9):3782\u20133790. https:\/\/doi.org\/10.1128\/IAI.00364-09","journal-title":"Infect Immun"},{"issue":"1","key":"3948_CR27","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1186\/s12929-018-0466-9","volume":"25","author":"WL Chang","year":"2018","unstructured":"Chang WL, Yeh YC, Sheu BS (2018) The impacts of H. pylori virulence factors on the development of gastroduodenal diseases. J Biomed Sci 25(1):68. https:\/\/doi.org\/10.1186\/s12929-018-0466-9","journal-title":"J Biomed Sci"},{"issue":"28","key":"3948_CR28","doi-asserted-by":"publisher","first-page":"25256","DOI":"10.1074\/jbc.M111.233601","volume":"286","author":"N Ishijima","year":"2011","unstructured":"Ishijima N, Suzuki M, Ashida H, Ichikawa Y, Kanegae Y, Saito I, Bor\u00e9n T, Haas R, Sasakawa C (2011) BabA-mediated adherence is a potentiator of the Helicobacter pylori type IV secretion system activity. J Biol Chem 286(28):25256\u201325264. https:\/\/doi.org\/10.1074\/jbc.M111.233601","journal-title":"J Biol Chem"},{"issue":"23","key":"3948_CR29","doi-asserted-by":"publisher","first-page":"15136","DOI":"10.1073\/pnas.182558799","volume":"99","author":"K Guillemin","year":"2002","unstructured":"Guillemin K, Salama NR, Tompkins LS (2002) Cag pathogenicity island-specific responses of gastric epithelial cells to Helicobacter pylori infection. Proc Natl Acad Sci U S A 99(23):15136\u201315141. https:\/\/doi.org\/10.1073\/pnas.182558799","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6","key":"3948_CR30","doi-asserted-by":"publisher","first-page":"1050","DOI":"10.1111\/j.1365-2958.2012.08073.x","volume":"84","author":"S Talarico","year":"2012","unstructured":"Talarico S, Whitefield SE, Fero J, Haas R (2012) Regulation of Helicobacter pylori adherence by gene conversion. Mol Microbiol 84(6):1050\u20131061. https:\/\/doi.org\/10.1111\/j.1365-2958.2012.08073.x","journal-title":"Mol Microbiol"},{"issue":"3","key":"3948_CR31","doi-asserted-by":"publisher","first-page":"174","DOI":"10.3855\/jidc.259","volume":"2","author":"Y Yamaoka","year":"2008","unstructured":"Yamaoka Y (2008) Increasing evidence of the role of Helicobacter pylori SabA in the pathogenesis of gastroduodenal disease. J Infect Dev Ctries 2(3):174. https:\/\/doi.org\/10.3855\/jidc.259","journal-title":"J Infect Dev Ctries"},{"issue":"1","key":"3948_CR32","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/j.femsle.2004.03.023","volume":"234","author":"P Michael","year":"2004","unstructured":"Michael P, Patricia D, Jennifer S, Beier D (2004) Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori. FEMS Microbiol Lett 234(1):51\u201361. https:\/\/doi.org\/10.1016\/j.femsle.2004.03.023","journal-title":"FEMS Microbiol Lett"},{"issue":"8","key":"3948_CR33","doi-asserted-by":"publisher","first-page":"2034","DOI":"10.1128\/jb.01703-08","volume":"192","author":"JT Loh","year":"2010","unstructured":"Loh JT, Gupta SS, Friedman DB, Krezel AM (2010) Analysis of protein expression regulated by the Helicobacter pylori ArsRS two-component signal transduction system. J Bacteriol 192(8):2034\u20132043. https:\/\/doi.org\/10.1128\/jb.01703-08","journal-title":"J Bacteriol"},{"issue":"10","key":"3948_CR34","doi-asserted-by":"publisher","first-page":"6332","DOI":"10.1074\/jbc.M113.513135","volume":"289","author":"SS Pang","year":"2014","unstructured":"Pang SS, Nguyen ST, Perry AJ, Day CJ, Panjikar S, Tiralongo J, Whisstock JC, T K (2014) The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori. J Biol Chem 289(10):6332\u20136340. https:\/\/doi.org\/10.1074\/jbc.M113.513135","journal-title":"J Biol Chem"},{"issue":"6","key":"3948_CR35","doi-asserted-by":"publisher","first-page":"2325","DOI":"10.1172\/jci34324","volume":"118","author":"NT Marcos","year":"2008","unstructured":"Marcos NT, Magalh\u00e3es A, Ferreira B, Oliveira MJ, Carvalho AS, Mendes N, Gilmartin T, Head SR, Figueiredo C, David L, Santos-Silva F (2008) Helicobacter pylori induces beta3GnT5 in human gastric cell lines, modulating expression of the SabA ligand sialyl-Lewis x. J Clin Invest 118(6):2325\u20132336. https:\/\/doi.org\/10.1172\/jci34324","journal-title":"J Clin Invest"},{"issue":"1","key":"3948_CR36","doi-asserted-by":"publisher","first-page":"738","DOI":"10.1080\/21505594.2018.1440171","volume":"9","author":"J Benktander","year":"2018","unstructured":"Benktander J, Barone A, Johansson MM (2018) Helicobacter pylori SabA binding gangliosides of human stomach. Virulence 9(1):738\u2013751. https:\/\/doi.org\/10.1080\/21505594.2018.1440171","journal-title":"Virulence"},{"issue":"5581","key":"3948_CR37","doi-asserted-by":"publisher","first-page":"573","DOI":"10.1126\/science.1069076","volume":"297","author":"J Mahdavi","year":"2002","unstructured":"Mahdavi J, Sond\u00e9n B, Hurtig M, Olfat FO, Forsberg L, Roche N, Angstrom J, Larsson T, Teneberg S, Karlsson KA, Altraja S, Wadstr\u00f6m T, Kersulyte D, Berg DE, Dubois A, Petersson C, Magnusson KE, Norberg T, Lindh F, Lundskog BB, Arnqvist A, Hammarstr\u00f6m L (2002) Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation. Science 297(5581):573\u2013578. https:\/\/doi.org\/10.1126\/science.1069076","journal-title":"Science"},{"issue":"2","key":"3948_CR38","doi-asserted-by":"publisher","first-page":"880","DOI":"10.1128\/iai.72.2.880-888.2004","volume":"72","author":"P Lehours","year":"2004","unstructured":"Lehours P, M\u00e9nard A, Dupouy S, Bergey B, Richy F, Zerbib F, Ruskon\u00e9-Fourmestraux A, Delchier JC (2004) Evaluation of the association of nine Helicobacter pylori virulence factors with strains involved in low-grade gastric mucosa-associated lymphoid tissue lymphoma. Infect Immun 72(2):880\u2013888. https:\/\/doi.org\/10.1128\/iai.72.2.880-888.2004","journal-title":"Infect Immun"},{"issue":"6","key":"3948_CR39","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1136\/gut.2005.083014","volume":"55","author":"Y Yamaoka","year":"2006","unstructured":"Yamaoka Y, Ojo O, Fujimoto S, Odenbreit S, Haas R, Gutierrez O, El-Zimaity HM, Reddy R, Arnqvist A (2006) Helicobacter pylori outer membrane proteins and gastroduodenal disease. Gut 55(6):775\u2013781. https:\/\/doi.org\/10.1136\/gut.2005.083014","journal-title":"Gut"},{"issue":"12","key":"3948_CR40","doi-asserted-by":"publisher","first-page":"2228","DOI":"10.1111\/j.1440-1746.2007.04831.x","volume":"22","author":"A Yanai","year":"2007","unstructured":"Yanai A, Maeda S, Hikiba Y, Shibata W, Ohmae T, Hirata Y, Ogura K, Yoshida H, Omata M (2007) Clinical relevance of Helicobacter pylori sabA genotype in Japanese clinical isolates. J Gastroenterol 22(12):2228\u20132232. https:\/\/doi.org\/10.1111\/j.1440-1746.2007.04831.x","journal-title":"J Gastroenterol"},{"issue":"13","key":"3948_CR41","doi-asserted-by":"publisher","first-page":"7533","DOI":"10.1073\/pnas.130079797","volume":"97","author":"Y Yamaoka","year":"2000","unstructured":"Yamaoka Y, Dong HK, Graham DYA (2000) A M(r) 34,000 proinflammatory outer membrane protein (oipA) of Helicobacter pylori. Proc Natl Acad Sci U S A 97(13):7533\u20137538. https:\/\/doi.org\/10.1073\/pnas.130079797","journal-title":"Proc Natl Acad Sci U S A"},{"key":"3948_CR42","doi-asserted-by":"publisher","unstructured":"Horridge DN, Begley AA, Kim J, Aravindan N, Fan K, Forsyth MH (2017) Outer inflammatory protein a (OipA) of Helicobacter pylori is regulated by host cell contact and mediates CagA translocation and interleukin-8 response only in the presence of a functional cag pathogenicity island type IV secretion system. Pathog Dis 75(8). https:\/\/doi.org\/10.1093\/femspd\/ftx113","DOI":"10.1093\/femspd\/ftx113"},{"key":"3948_CR43","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1016\/j.meegid.2018.02.017","volume":"60","author":"N Farzi","year":"2018","unstructured":"Farzi N, Yadegar A, Aghdaei HA, Yamaoka Y, Zali MR (2018) Genetic diversity and functional analysis of oipA gene in association with other virulence factors among Helicobacter pylori isolates from Iranian patients with different gastric diseases. Infect Genet Evol 60:26\u201334. https:\/\/doi.org\/10.1016\/j.meegid.2018.02.017","journal-title":"Infect Genet Evol"},{"issue":"2","key":"3948_CR44","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1053\/gast.2002.34781","volume":"123","author":"Y Yamaoka","year":"2002","unstructured":"Yamaoka Y, Kikuchi S, el-Zimaity HM, Gutierrez O, Osato MS, Graham DY (2002) Importance of Helicobacter pylori oipA in clinical presentation, gastric inflammation, and mucosal interleukin 8 production. Gastroenterology 123(2):414\u2013424. https:\/\/doi.org\/10.1053\/gast.2002.34781","journal-title":"Gastroenterology"},{"key":"3948_CR45","doi-asserted-by":"publisher","unstructured":"Al-Maleki AR, Loke MF, Lui SY, Ramli NSK, Khosravi Y, Ng CG, Venkatraman G, Goh KL, Ho B, Vadivelu J (2017) Helicobacter pylori outer inflammatory protein A (OipA) suppresses apoptosis of AGS gastric cells in vitro. Cell Microbiol 19(12). https:\/\/doi.org\/10.1111\/cmi.12771","DOI":"10.1111\/cmi.12771"},{"issue":"2","key":"3948_CR46","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1158\/0008-5472.Can-07-0824","volume":"68","author":"AT Franco","year":"2008","unstructured":"Franco AT, Johnston E, Krishna U, Yamaoka Y, Israel DA, Nagy TA, Wroblewski LE, Piazuelo MB, Correa P, Peek RM (2008) Regulation of gastric carcinogenesis by Helicobacter pylori virulence factors. Cancer Res 68(2):379\u2013387. https:\/\/doi.org\/10.1158\/0008-5472.Can-07-0824","journal-title":"Cancer Res"},{"key":"3948_CR47","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1099\/jmm.0.05229-0","volume":"52","author":"B Su","year":"2003","unstructured":"Su B, Ceponis PJM, Sherman PM (2003) Cytoskeletal rearrangements in gastric epithelial cells in response to Helicobacter pylori infection. J Med Microbiol 52:861\u2013867. https:\/\/doi.org\/10.1099\/jmm.0.05229-0","journal-title":"J Med Microbiol"},{"issue":"6","key":"3948_CR48","doi-asserted-by":"publisher","first-page":"3646","DOI":"10.1128\/iai.72.6.3646-3649.2004","volume":"72","author":"S Moese","year":"2004","unstructured":"Moese S, Selbach M, Kwok T, Brinkmann V, K\u00f6nig W, Meyer TF (2004) Helicobacter pylori induces AGS cell motility and elongation via independent signaling pathways. Infect Immun 72(6):3646\u20133649. https:\/\/doi.org\/10.1128\/iai.72.6.3646-3649.2004","journal-title":"Infect Immun"},{"issue":"4","key":"3948_CR49","doi-asserted-by":"publisher","first-page":"1008","DOI":"10.1111\/j.1462-5822.2007.01104.x","volume":"10","author":"FH Tabassam","year":"2008","unstructured":"Tabassam FH, Graham DY, Yamaoka Y (2008) OipA plays a role in Helicobacter pylori-induced focal adhesion kinase activation and cytoskeletal re-organization. Cell Microbiol 10(4):1008\u20131020. https:\/\/doi.org\/10.1111\/j.1462-5822.2007.01104.x","journal-title":"Cell Microbiol"},{"issue":"8","key":"3948_CR50","doi-asserted-by":"publisher","first-page":"1380","DOI":"10.1111\/j.1440-1746.2009.05876.x","volume":"24","author":"H Dabiri","year":"2009","unstructured":"Dabiri H, Maleknejad P, Yamaoka Y, Feizabadi MM, Jafari F, Rezadehbashi M, Nakhjavani FA, Mirsalehian A, Zali MR (2009) Distribution of Helicobacter pylori cagA, cagE, oipA and vacA in different major ethnic groups in Tehran, Iran. J Gastroenterol Hepatol 24(8):1380\u20131386. https:\/\/doi.org\/10.1111\/j.1440-1746.2009.05876.x","journal-title":"J Gastroenterol Hepatol"},{"key":"3948_CR51","doi-asserted-by":"publisher","first-page":"555","DOI":"10.1186\/1471-2334-13-555","volume":"13","author":"J Liu","year":"2013","unstructured":"Liu J, He C, Chen M, Wang Z, Xing C, Yuan Y (2013) Association of presence\/absence and on\/off patterns of Helicobacter pylori oipA gene with peptic ulcer disease and gastric cancer risks: a meta-analysis. BMC Infect Dis 13:555. https:\/\/doi.org\/10.1186\/1471-2334-13-555","journal-title":"BMC Infect Dis"},{"issue":"1","key":"3948_CR52","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1186\/s12885-018-5249-x","volume":"19","author":"LLBC Braga","year":"2019","unstructured":"Braga LLBC, Batista MHR, de Azevedo OGR, da Silva Costa KC, Gomes AD, Rocha GA, Queiroz DMM (2019) oipA \u201con\u201d status of Helicobacter pylori is associated with gastric cancer in North-Eastern Brazil. BMC Cancer 19(1):48. https:\/\/doi.org\/10.1186\/s12885-018-5249-x","journal-title":"BMC Cancer"},{"issue":"1","key":"3948_CR53","doi-asserted-by":"publisher","first-page":"326","DOI":"10.3906\/sag-1505-108","volume":"47","author":"M Mahboubi","year":"2017","unstructured":"Mahboubi M, Falsafi T, Sadeghizadeh M, Mahjoub F (2017) The role of outer inflammatory protein A (OipA) in vaccination of theC57BL\/6 mouse model infected by Helicobacter pylori. Turk J Med Sci 47(1):326\u2013333. https:\/\/doi.org\/10.3906\/sag-1505-108","journal-title":"Turk J Med Sci"},{"issue":"10","key":"3948_CR54","doi-asserted-by":"publisher","first-page":"2200","DOI":"10.1017\/s095026881600025x","volume":"144","author":"J Yakoob","year":"2016","unstructured":"Yakoob J, Abbas Z, Jafri W, Khan R, Salim SA, Awan S, Abid S, Hamid S, Ahmad Z (2016) Helicobacter pylori outer membrane protein and virulence marker differences in expatriate patients. Epidemiol Infect 144(10):2200\u20132208. https:\/\/doi.org\/10.1017\/s095026881600025x","journal-title":"Epidemiol Infect"},{"issue":"3","key":"3948_CR55","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1111\/j.1440-1746.2008.05762.x","volume":"24","author":"T Ohno","year":"2009","unstructured":"Ohno T, Sugimoto M, Nagashima A, Ogiwara H, Vilaichone RK, Mahachai V, Graham DY, Yamaoka Y (2009) Relationship between Helicobacter pylori hopQ genotype and clinical outcome in Asian and Western populations. J Gastroenterol Hepatol 24(3):462\u2013468. https:\/\/doi.org\/10.1111\/j.1440-1746.2008.05762.x","journal-title":"J Gastroenterol Hepatol"},{"issue":"11","key":"3948_CR56","doi-asserted-by":"publisher","first-page":"1896","DOI":"10.1111\/cmi.12158","volume":"15","author":"E Belogolova","year":"2013","unstructured":"Belogolova E, Bauer B, Pompaiah M, Asakura H, Brinkman V, Ertl C, Bartfeld S, Nechitaylo TY, Haas R, Machuy N, Salama N, Churin Y (2013) Helicobacter pylori outer membrane protein HopQ identified as a novel T4SS-associated virulence factor. Cell Microbiol 15(11):1896\u20131912. https:\/\/doi.org\/10.1111\/cmi.12158","journal-title":"Cell Microbiol"},{"issue":"1","key":"3948_CR57","doi-asserted-by":"publisher","DOI":"10.1111\/cmi.12965","volume":"21","author":"N Tegtmeyer","year":"2019","unstructured":"Tegtmeyer N, Harrer A, Schmitt V, Singer BB (2019) Expression of CEACAM1 or CEACAM5 in AZ-521 cells restores the type IV secretion deficiency for translocation of CagA by Helicobacter pylori. Cell Microbiol 21(1):e12965. https:\/\/doi.org\/10.1111\/cmi.12965","journal-title":"Cell Microbiol"},{"key":"3948_CR58","doi-asserted-by":"publisher","unstructured":"Moonens K, Hamway Y, Neddermann M, Reschke M, Tegtmeyer N, Kruse T, Kammerer R, Mej\u00edas-Luque R, Singer BB, Backert S, Gerhard M (2018) Helicobacter pylori adhesin HopQ disrupts dimerization in human CEACAMs. EMBO J 37(13). https:\/\/doi.org\/10.15252\/embj.201798665","DOI":"10.15252\/embj.201798665"},{"key":"3948_CR59","doi-asserted-by":"publisher","first-page":"16233","DOI":"10.1038\/nmicrobiol.2016.233","volume":"2","author":"V K\u00f6niger","year":"2016","unstructured":"K\u00f6niger V, Holsten L, Harrison U, Busch B, Loell E, Zhao Q, Bonsor DA, Roth A, Kengmo-Tchoupa A, Smith SI, Mueller S, Sundberg EJ, Zimmermann W, Fischer W, Hauck CR (2016) Erratum: Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA. Nat Microbiol 2:16233. https:\/\/doi.org\/10.1038\/nmicrobiol.2016.233","journal-title":"Nat Microbiol"},{"issue":"1","key":"3948_CR60","doi-asserted-by":"publisher","first-page":"8036","DOI":"10.1038\/s41598-017-08176-7","volume":"7","author":"O Teymournejad","year":"2017","unstructured":"Teymournejad O, Mobarez AM, Hassan ZM (2017) Binding of the Helicobacter pylori OipA causes apoptosis of host cells via modulation of Bax\/Bcl-2 levels. Sci Rep 7(1):8036. https:\/\/doi.org\/10.1038\/s41598-017-08176-7","journal-title":"Sci Rep"},{"issue":"1","key":"3948_CR61","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1111\/j.1440-1746.2009.06141.x","volume":"25","author":"BS Sheu","year":"2010","unstructured":"Sheu BS, Yang HB, Yeh YC (2010) Helicobacter pylori colonization of the human gastric epithelium: a bug\u2019s first step is a novel target for us. J Gastroenterol Hepatol 25(1):26\u201332. https:\/\/doi.org\/10.1111\/j.1440-1746.2009.06141.x","journal-title":"J Gastroenterol Hepatol"},{"issue":"16","key":"3948_CR62","doi-asserted-by":"publisher","first-page":"3325","DOI":"10.1093\/nar\/27.16.3325","volume":"27","author":"B Peck","year":"1999","unstructured":"Peck B, Ortkamp M, Diehl KD, Hundt E (1999) Conservation, localization and expression of HopZ, a protein involved in adhesion of Helicobacter pylori. Nucleic Acids Res 27(16):3325\u20133333. https:\/\/doi.org\/10.1093\/nar\/27.16.3325","journal-title":"Nucleic Acids Res"},{"issue":"12","key":"3948_CR63","doi-asserted-by":"publisher","first-page":"5033","DOI":"10.1073\/pnas.1018444108","volume":"108","author":"L Kennemann","year":"2011","unstructured":"Kennemann L, Didelot X, Aebischer T, Kuhn S, Drescher B, Droege M, Reinhardt R, Correa P, Meyer TF, Josenhans C, Falush D (2011) Helicobacter pylori genome evolution during human infection. Proc Natl Acad Sci U S A 108(12):5033\u20135038. https:\/\/doi.org\/10.1073\/pnas.1018444108","journal-title":"Proc Natl Acad Sci U S A"},{"key":"3948_CR64","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1078\/1438-4221-00205","volume":"292","author":"S Odenbreit","year":"2002","unstructured":"Odenbreit S, Kavermann H, P\u00fcls J, Haas R (2002) CagA tyrosine phosphorylation and interleukin-8 induction by Helicobacter pylori are independent from alpAB, HopZ and bab group outer membrane proteins. Int J Med Microbiol 292:257\u2013266. https:\/\/doi.org\/10.1078\/1438-4221-00205","journal-title":"Int J Med Microbiol"},{"issue":"2","key":"3948_CR65","doi-asserted-by":"publisher","DOI":"10.1111\/hel.12461","volume":"23","author":"SL Servetas","year":"2018","unstructured":"Servetas SL, Kim A, Su H, Cha JH (2018) Comparative analysis of the Hom family of outer membrane proteins in isolates from two geographically distinct regions: the United States and South Korea. Helicobacter 23(2):e12461. https:\/\/doi.org\/10.1111\/hel.12461","journal-title":"Helicobacter"},{"issue":"15","key":"3948_CR66","doi-asserted-by":"publisher","first-page":"3961","DOI":"10.1128\/jb.00395-10","volume":"192","author":"M Oleastro","year":"2010","unstructured":"Oleastro M, Cordeiro R, M\u00e9nard A, Gomes JP (2010) Allelic diversity among Helicobacter pylori outer membrane protein genes homB and homA generated by recombination. J Bacteriol 192(15):3961\u20133968. https:\/\/doi.org\/10.1128\/jb.00395-10","journal-title":"J Bacteriol"},{"issue":"12","key":"3948_CR67","doi-asserted-by":"publisher","first-page":"846","DOI":"10.1007\/s12275-016-6434-8","volume":"54","author":"A Kim","year":"2016","unstructured":"Kim A, Servetas SL, Kang J, Kim J, Jang S, Choi YH, Su H, Jeon YE, Hong YA, Yoo YJ, Merrell DS (2016) Helicobacter pylori outer membrane protein, HomC, shows geographic dependent polymorphism that is influenced by the Bab family. J Microbiol 54(12):846\u2013852. https:\/\/doi.org\/10.1007\/s12275-016-6434-8","journal-title":"J Microbiol"},{"issue":"7","key":"3948_CR68","doi-asserted-by":"publisher","first-page":"4064","DOI":"10.1128\/iai.00123-06","volume":"74","author":"M Oleastro","year":"2006","unstructured":"Oleastro M, Monteiro L, Lehours P, M\u00e9graud F (2006) Identification of markers for Helicobacter pylori strains isolated from children with peptic ulcer disease by suppressive subtractive hybridization. Infect Immun 74(7):4064\u20134074. https:\/\/doi.org\/10.1128\/iai.00123-06","journal-title":"Infect Immun"},{"issue":"1","key":"3948_CR69","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1186\/1757-4749-1-12","volume":"1","author":"M Oleastro","year":"2009","unstructured":"Oleastro M, Cordeiro R, Yamaoka Y, Queiroz D, M\u00e9graud F, Monteiro L (2009) Disease association with two Helicobacter pylori duplicate outer membrane protein genes, homB and homA. J Gut pathogens 1(1):12. https:\/\/doi.org\/10.1186\/1757-4749-1-12","journal-title":"J Gut pathogens"},{"issue":"10","key":"3948_CR70","doi-asserted-by":"publisher","first-page":"3241","DOI":"10.1128\/jcm.00293-09","volume":"47","author":"SW Jung","year":"2009","unstructured":"Jung SW, Sugimoto M, Graham DY (2009) homB status of Helicobacter pylori as a novel marker to distinguish gastric cancer from duodenal ulcer. J Biol Chem 47(10):3241\u20133245. https:\/\/doi.org\/10.1128\/jcm.00293-09","journal-title":"J Biol Chem"},{"issue":"3","key":"3948_CR71","doi-asserted-by":"publisher","first-page":"1082","DOI":"10.1128\/jcm.06293-11","volume":"50","author":"J Kang","year":"2012","unstructured":"Kang J, Jones KR, Jang S, Olsen CH, Yoo YJ, Merrell DS (2012) The geographic origin of Helicobacter pylori influences the association of the homB gene with gastric cancer. J Clin Microbiol 50(3):1082\u20131085. https:\/\/doi.org\/10.1128\/jcm.06293-11","journal-title":"J Clin Microbiol"},{"issue":"10002","key":"3948_CR72","doi-asserted-by":"publisher","first-page":"1457","DOI":"10.1016\/s0140-6736(15)60310-5","volume":"386","author":"M Zeng","year":"2015","unstructured":"Zeng M, Mao XH, Li JX, Tong WD, Wang B, Zhang YJ, Guo G, Zhao ZJ, Li L, Wu DL, Lu DS, Tan ZM, Liang HY, Wu C, Li DH, Luo P, Zeng H, Zhang WJ, Zhang JY, Guo BT, Zhu FC (2015) Efficacy, safety, and immunogenicity of an oral recombinant Helicobacter pylori vaccine in children in China: a randomised, double-blind, placebo-controlled, phase 3 trial. Lancet 386(10002):1457\u20131464. https:\/\/doi.org\/10.1016\/s0140-6736(15)60310-5","journal-title":"Lancet"},{"issue":"1","key":"3948_CR73","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1053\/j.gastro.2019.04.011","volume":"157","author":"CA Fallone","year":"2019","unstructured":"Fallone CA, Moss SF, Malfertheiner P (2019) Reconciliation of recent Helicobacter pylori treatment guidelines in a time of increasing resistance to antibiotics. Gastroenterology 157(1):44\u201353. https:\/\/doi.org\/10.1053\/j.gastro.2019.04.011","journal-title":"Gastroenterology"},{"key":"3948_CR74","doi-asserted-by":"publisher","unstructured":"Minhu C, Adrian L, Stuart H (1992) Immunisation against gastric helicobacter infection in a mouse\/Helicobacter felis model. Lancet. https:\/\/doi.org\/10.1016\/0140-6736(92)90720-N","DOI":"10.1016\/0140-6736(92)90720-N"},{"issue":"5","key":"3948_CR75","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1080\/1040841X.2017.1291578","volume":"43","author":"N Mirzaei","year":"2017","unstructured":"Mirzaei N, Poursina F, Moghim S, Rashidi N, Safaei HG (2017) The study of H. pylori putative candidate factors for single- and multi-component vaccine development. Crit Rev Microbiol 43(5):631\u2013650. https:\/\/doi.org\/10.1080\/1040841X.2017.1291578","journal-title":"Crit Rev Microbiol"},{"issue":"8","key":"3948_CR76","doi-asserted-by":"publisher","first-page":"3829","DOI":"10.4049\/jimmunol.1401633","volume":"194","author":"M Larena","year":"2015","unstructured":"Larena M, Holmgren J, Lebens M, Terrinoni M (2015) Cholera toxin, and the related nontoxic adjuvants mmCT and dmLT, promote human Th17 responses via cyclic AMP-protein kinase A and inflammasome-dependent IL-1 signaling. J Immunol 194(8):3829\u20133839. https:\/\/doi.org\/10.4049\/jimmunol.1401633","journal-title":"J Immunol"},{"issue":"34","key":"3948_CR77","doi-asserted-by":"publisher","first-page":"12294","DOI":"10.1073\/pnas.1400478111","volume":"111","author":"C Maisonneuve","year":"2014","unstructured":"Maisonneuve C, Bertholet S, Philpott DJ, De GE (2014) Unleashing the potential of NOD- and Toll-like agonists as vaccine adjuvants. Proc Natl Acad Sci U S A 111(34):12294\u201312299. https:\/\/doi.org\/10.1073\/pnas.1400478111","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"3948_CR78","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1080\/21645515.2014.1004026","volume":"11","author":"P He","year":"2015","unstructured":"He P, Zou Y, Hu Z (2015) Advances in aluminum hydroxide-based adjuvant research and its mechanism. Hum Vaccin Immunother 11(2):477\u2013488. https:\/\/doi.org\/10.1080\/21645515.2014.1004026","journal-title":"Hum Vaccin Immunother"},{"issue":"12","key":"3948_CR79","doi-asserted-by":"publisher","first-page":"21460","DOI":"10.1002\/jcp.28870","volume":"234","author":"M Keikha","year":"2019","unstructured":"Keikha M, Eslami M, Yousefi B, Ghasemian A (2019) Potential antigen candidates for subunit vaccine development against Helicobacter pylori infection. J Cell Physiol 234(12):21460\u201321470. https:\/\/doi.org\/10.1002\/jcp.28870","journal-title":"J Cell Physiol"},{"key":"3948_CR80","doi-asserted-by":"publisher","first-page":"2153","DOI":"10.3389\/fmicb.2018.02153","volume":"9","author":"A Ebbensgaard","year":"2018","unstructured":"Ebbensgaard A, Mordhorst H, Aarestrup FM, Hansen EB (2018) The role of outer membrane proteins and lipopolysaccharides for the sensitivity of Escherichia coli to antimicrobial peptides. Front Microbiol 9:2153. https:\/\/doi.org\/10.3389\/fmicb.2018.02153","journal-title":"Front Microbiol"},{"issue":"7","key":"3948_CR81","doi-asserted-by":"publisher","first-page":"3207","DOI":"10.1128\/iai.00279-10","volume":"78","author":"AS Barbosa","year":"2010","unstructured":"Barbosa AS, Monaris D, Silva LB, Morais ZM, Vasconcellos SA, Cianciarullo AM, Isaac L (2010) Functional characterization of LcpA, a surface-exposed protein of Leptospira spp. that binds the human complement regulator C4BP. Infect Immun 78(7):3207\u20133216. https:\/\/doi.org\/10.1128\/iai.00279-10","journal-title":"Infect Immun"},{"key":"3948_CR82","doi-asserted-by":"publisher","first-page":"1737","DOI":"10.3389\/fimmu.2018.01737","volume":"9","author":"C Liu","year":"2018","unstructured":"Liu C, Pan X, Xia B, Chen F, Jin Y, Bai F, Priebe G, Cheng Z, Jin S (2018) Construction of a protective vaccine against lipopolysaccharide-heterologous Pseudomonas aeruginosa strains based on expression profiling of outer membrane proteins during infection. Front Immunol 9:1737. https:\/\/doi.org\/10.3389\/fimmu.2018.01737","journal-title":"Front Immunol"},{"issue":"Spl. Edn. 2","key":"3948_CR83","doi-asserted-by":"publisher","first-page":"135","DOI":"10.13005\/bbra\/2020","volume":"12","author":"F Tohidi","year":"2015","unstructured":"Tohidi F, Teymournejad O, Taravati A, Ahmadi KJA (2015) Analysis of important H. pylori outer membrane proteins by detection of common sequences in exposed areas; in silico study. Biosci Biotechnol Res Asia 12(Spl. Edn. 2):135\u2013143. https:\/\/doi.org\/10.13005\/bbra\/2020","journal-title":"Biosci Biotechnol Res Asia"},{"issue":"3","key":"3948_CR84","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1016\/s0928-8244(03)00228-1","volume":"38","author":"I Ofek","year":"2003","unstructured":"Ofek I, Hasty DL, Sharon N (2003) Anti-adhesion therapy of bacterial diseases: prospects and problems. Med Microbiol Immunol 38(3):181\u2013191. https:\/\/doi.org\/10.1016\/s0928-8244(03)00228-1","journal-title":"Med Microbiol Immunol"},{"issue":"5","key":"3948_CR85","doi-asserted-by":"publisher","first-page":"808","DOI":"10.1016\/j.bbapap.2008.11.005","volume":"1794","author":"AH Delcour","year":"2009","unstructured":"Delcour AH (2009) Outer membrane permeability and antibiotic resistance. Biochim Biophys Acta 1794(5):808\u2013816. https:\/\/doi.org\/10.1016\/j.bbapap.2008.11.005","journal-title":"Biochim Biophys Acta"},{"issue":"46","key":"3948_CR86","doi-asserted-by":"publisher","first-page":"6054","DOI":"10.1016\/j.vaccine.2014.09.014","volume":"32","author":"J Chen","year":"2014","unstructured":"Chen J, Li N, She F (2014) Helicobacter pylori outer inflammatory protein DNA vaccine-loaded bacterial ghost enhances immune protective efficacy in C57BL\/6 mice. Vaccine 32(46):6054\u20136060. https:\/\/doi.org\/10.1016\/j.vaccine.2014.09.014","journal-title":"Vaccine"},{"key":"3948_CR87","doi-asserted-by":"publisher","unstructured":"George L, Goldberg JB (2012) Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pylori. Front Cell Infect Microbiol 2:\u201329. https:\/\/doi.org\/10.3389\/fcimb.2012.00029","DOI":"10.3389\/fcimb.2012.00029"},{"issue":"3","key":"3948_CR88","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1016\/s1286-4579(01)01377-6","volume":"3","author":"B Peck","year":"2001","unstructured":"Peck B, Ortkamp M, Nau U, Niederweis M, Hundt E (2001) Characterization of four members of a multigene family encoding outer membrane proteins of Helicobacter pylori and their potential for vaccination. Microbes Infect 3(3):171\u2013179. https:\/\/doi.org\/10.1016\/s1286-4579(01)01377-6","journal-title":"Microbes Infect"},{"issue":"5683","key":"3948_CR89","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1126\/science.1098801","volume":"305","author":"M Aspholm-Hurtig","year":"2004","unstructured":"Aspholm-Hurtig M, Dailide G, Lahmann M, Kalia A, Ilver D, Roche N, Vikstr\u00f6m S, Sj\u00f6str\u00f6m R, Lind\u00e9n S, B\u00e4ckstr\u00f6m A, Lundberg C, Arnqvist A, Mahdavi J, Nilsson UJ, Velapati\u00f1o B, Gilman RH, Gerhard M, Alarcon T, L\u00f3pez-Brea M, Nakazawa T, Fox JG, Correa P, Dominguez-Bello MG, Perez-Perez GI, Blaser MJ, Normark S, Carlstedt I, Oscarson S, Teneberg S, Berg DE (2004) Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin. Science 305(5683):519\u2013522. https:\/\/doi.org\/10.1126\/science.1098801","journal-title":"Science"},{"issue":"6","key":"3948_CR90","doi-asserted-by":"publisher","first-page":"1582","DOI":"10.1002\/pmic.200700808","volume":"9","author":"A Walz","year":"2009","unstructured":"Walz A, Odenbreit S, St\u00fchler K, Wattenberg A, Meyer HE, Mahdavi J, Bor\u00e9n T (2009) Identification of glycoprotein receptors within the human salivary proteome for the lectin-like BabA and SabA adhesins of Helicobacter pylori by fluorescence-based 2-D bacterial overlay. Proteomics 9(6):1582\u20131592. https:\/\/doi.org\/10.1002\/pmic.200700808","journal-title":"Proteomics"},{"issue":"5141","key":"3948_CR91","doi-asserted-by":"publisher","first-page":"1892","DOI":"10.1126\/science.8018146","volume":"262","author":"T Bor\u00e9n","year":"1993","unstructured":"Bor\u00e9n T, Falk P, Roth KA, Larson G (1993) Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens. Science 262(5141):1892\u20131895. https:\/\/doi.org\/10.1126\/science.8018146","journal-title":"Science"},{"issue":"22","key":"3948_CR92","doi-asserted-by":"publisher","first-page":"20140","DOI":"10.1074\/jbc.M301436200","volume":"278","author":"L Royle","year":"2003","unstructured":"Royle L, Roos A, Harvey DJ, Wormald MR, van Gijlswijk-Janssen D, Redwan e-RM, Wilson IA, Daha MR, Dwek RA (2003) Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems. J Biol Chem 278(22):20140\u201320153. https:\/\/doi.org\/10.1074\/jbc.M301436200","journal-title":"J Biol Chem"},{"issue":"8","key":"3948_CR93","doi-asserted-by":"publisher","first-page":"1046","DOI":"10.1093\/glycob\/cwq066","volume":"20","author":"S Issa","year":"2010","unstructured":"Issa S, Moran AP, Ustinov SN, Lin JH, Ligtenberg AJ (2010) O-linked oligosaccharides from salivary agglutinin: Helicobacter pylori binding sialyl-Lewis x and Lewis b are terminating moieties on hyperfucosylated oligo-N-acetyllactosamine. Glycobiology 20(8):1046\u20131057. https:\/\/doi.org\/10.1093\/glycob\/cwq066","journal-title":"Glycobiology"},{"key":"3948_CR94","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1042\/bj20040402","volume":"384","author":"S Lind\u00e9n","year":"2004","unstructured":"Lind\u00e9n S, Mahdavi J, Hedenbro J, Bor\u00e9n T, Carlstedt I (2004) Effects of pH on Helicobacter pylori binding to human gastric mucins: identification of binding to non-MUC5AC mucins. Biochem J 384:263\u2013270. https:\/\/doi.org\/10.1042\/bj20040402","journal-title":"Biochem J"},{"issue":"8","key":"3948_CR95","doi-asserted-by":"publisher","first-page":"1077","DOI":"10.1093\/glycob\/cws076","volume":"22","author":"DT Kenny","year":"2012","unstructured":"Kenny DT, Skoog EC, Lind\u00e9n SK, Struwe WB, Rudd PM (2012) Presence of terminal N-acetylgalactosamine\u03b21-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: involvement in Helicobacter pylori colonization? Glycobiology 22(8):1077\u20131085. https:\/\/doi.org\/10.1093\/glycob\/cws076","journal-title":"Glycobiology"},{"issue":"10","key":"3948_CR96","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000617","volume":"5","author":"SK Lind\u00e9n","year":"2009","unstructured":"Lind\u00e9n SK, Sheng YH, Every AL, Miles KM, Skoog EC, Florin TH, Sutton P (2009) MUC1 limits Helicobacter pylori infection both by steric hindrance and by acting as a releasable decoy. PLoS Pathog 5(10):e1000617. https:\/\/doi.org\/10.1371\/journal.ppat.1000617","journal-title":"PLoS Pathog"},{"issue":"2","key":"3948_CR97","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1080\/pdp.22.2.117.129","volume":"22","author":"M Cohen","year":"2003","unstructured":"Cohen M, Drut R, Cueto RE (2003) SIALYL-Tn antigen distribution in Helicobacter pylori chronic gastritis in children: an immunohistochemical study. Pediatr Pathol Mol Med 22(2):117\u2013129. https:\/\/doi.org\/10.1080\/pdp.22.2.117.129","journal-title":"Pediatr Pathol Mol Med"},{"issue":"7","key":"3948_CR98","doi-asserted-by":"publisher","first-page":"700","DOI":"10.1093\/glycob\/cwi049","volume":"15","author":"A Walz","year":"2005","unstructured":"Walz A, Odenbreit S, Mahdavi J, Bor\u00e9n T (2005) Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays. Glycobiology 15(7):700\u2013708. https:\/\/doi.org\/10.1093\/glycob\/cwi049","journal-title":"Glycobiology"},{"issue":"10","key":"3948_CR99","doi-asserted-by":"publisher","first-page":"e110","DOI":"10.1371\/journal.ppat.0020110","volume":"2","author":"M Aspholm","year":"2006","unstructured":"Aspholm M, Olfat FO, Nord\u00e9n J, Sond\u00e9n B, Lundberg C, Sj\u00f6str\u00f6m R, Altraja S, Odenbreit S, Haas R, Wadstr\u00f6m T, Engstrand L, Semino-Mora C, Liu H, Dubois A, Teneberg S, Arnqvist A (2006) SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. PLoS Pathog 2(10):e110. https:\/\/doi.org\/10.1371\/journal.ppat.0020110","journal-title":"PLoS Pathog"},{"issue":"15","key":"3948_CR100","doi-asserted-by":"publisher","first-page":"15390","DOI":"10.1074\/jbc.M412725200","volume":"280","author":"M Unemo","year":"2005","unstructured":"Unemo M, Aspholm-Hurtig M, Ilver D, Bergstr\u00f6m J, Bor\u00e9n T, Danielsson D (2005) The sialic acid binding SabA adhesin of Helicobacter pylori is essential for nonopsonic activation of human neutrophils. J Biol Chem 280(15):15390\u201315397. https:\/\/doi.org\/10.1074\/jbc.M412725200","journal-title":"J Biol Chem"},{"key":"3948_CR101","doi-asserted-by":"publisher","unstructured":"Matsuo Y, Kido Y, Yamaoka Y (2017) Helicobacter pylori outer membrane protein-related pathogenesis. Toxins 9(3). https:\/\/doi.org\/10.3390\/toxins9030101","DOI":"10.3390\/toxins9030101"}],"container-title":["European Journal of Clinical Microbiology &amp; Infectious Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10096-020-03948-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10096-020-03948-y\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10096-020-03948-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,6,16]],"date-time":"2021-06-16T20:18:24Z","timestamp":1623874704000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10096-020-03948-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6,17]]},"references-count":101,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2020,10]]}},"alternative-id":["3948"],"URL":"https:\/\/doi.org\/10.1007\/s10096-020-03948-y","relation":{},"ISSN":["0934-9723","1435-4373"],"issn-type":[{"value":"0934-9723","type":"print"},{"value":"1435-4373","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,6,17]]},"assertion":[{"value":"31 March 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 June 2020","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 June 2020","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"The authors declare that they have no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"There are no ethical issues.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"There is no informed consent required for this review article.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Informed consent"}},{"value":"This content has been made available to all.","name":"free","label":"Free to read"}]}}