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Antibiotics, including amoxicillin, clarithromycin, furazolidone, levofloxacin, metronidazole, and tetracycline, are commonly used and considered the major treatment regimens for H. pylori eradication, which is, however, becoming less effective by the increasing prevalence of H pylori resistance. Thus, it is urgent to understand the molecular mechanisms of H. pylori pathogenesis and develop alternative therapeutic strategies. In this review, we focus on the virulence factors for H. pylori colonization and survival within host gastric mucosa and the host antimicrobial responses against H. pylori infection. 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Microbiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s10096-018-3414-4","article-title":"Diagnostic methods for helicobacter pylori infection: Ideals, options, and limitations","volume":"38","author":"Sabbagh","year":"2019","journal-title":"Eur. J. Clin. Microbiol. Infect. Dis."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ijfoodmicro.2010.01.016","article-title":"Transmission pathway of helicobacter pylori: Does food play a role in rural and urban areas?","volume":"138","author":"Vale","year":"2010","journal-title":"Int. J. Food Microbiol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3892\/ijo.2012.1701","article-title":"Pylori infection and gastric cancer: State of the art (review)","volume":"42","author":"Conteduca","year":"2013","journal-title":"Int. J. Oncol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1111\/1574-6976.12027","article-title":"Survival in hostile territory: The microbiota of the stomach","volume":"37","author":"Yang","year":"2013","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.3390\/biology2031110","article-title":"The role of helicobacter pylori outer membrane proteins in adherence and pathogenesis","volume":"2","author":"Oleastro","year":"2013","journal-title":"Biology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1002\/jcb.24389","article-title":"Role of the helicobacter pylori-induced inflammatory response in the development of gastric cancer","volume":"114","author":"Lamb","year":"2013","journal-title":"J. Cell Biochem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"159","DOI":"10.3389\/fcimb.2016.00159","article-title":"Adhesion and invasion of gastric mucosa epithelial cells by helicobacter pylori","volume":"6","author":"Huang","year":"2016","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.3748\/wjg.v17.i11.1383","article-title":"Molecular cross-talk between helicobacter pylori and human gastric mucosa","volume":"17","author":"Ricci","year":"2011","journal-title":"World J. Gastroenterol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"12753","DOI":"10.3748\/wjg.v20.i36.12753","article-title":"Immune evasion strategies used by helicobacter pylori","volume":"20","author":"Lina","year":"2014","journal-title":"World J. Gastroenterol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"668632","DOI":"10.3389\/fcimb.2021.668632","article-title":"Antimicrobial peptides: A new hope in biomedical and pharmaceutical fields","volume":"11","author":"Moretta","year":"2021","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1111\/j.1462-5822.2009.01421.x","article-title":"The innate immune molecule, nod1, regulates direct killing of helicobacter pylori by antimicrobial peptides","volume":"12","author":"Grubman","year":"2010","journal-title":"Cell Microbiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.4161\/auto.21007","article-title":"Crohn disease atg16l1 polymorphism increases susceptibility to infection with helicobacter pylori in humans","volume":"8","author":"Raju","year":"2012","journal-title":"Autophagy"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1093\/femsre\/fuw025","article-title":"Oxidative and nitrosative stress defences of helicobacter and campylobacter species that counteract mammalian immunity","volume":"40","author":"Flint","year":"2016","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/s41575-021-00449-x","article-title":"Helicobacter pylori infection and antibiotic resistance\u2014from biology to clinical implications","volume":"18","author":"Yamaoka","year":"2021","journal-title":"Nat. Rev. Gastroenterol. Hepatol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/1478-811X-9-28","article-title":"Molecular mechanisms of gastric epithelial cell adhesion and injection of caga by helicobacter pylori","volume":"9","author":"Backert","year":"2011","journal-title":"Cell Commun. Signal"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"656439","DOI":"10.3389\/fmolb.2021.656439","article-title":"Adhesion of helicobacter species to the human gastric mucosa: A deep look into glycans role","volume":"8","author":"Matos","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e1500315","DOI":"10.1126\/sciadv.1500315","article-title":"Structural basis of lewis(b) antigen binding by the helicobacter pylori adhesin baba","volume":"1","author":"Hage","year":"2015","journal-title":"Sci. Adv."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"4158","DOI":"10.3748\/wjg.v23.i23.4158","article-title":"Helicobacter pylori baba in adaptation for gastric colonization","volume":"23","author":"Ansari","year":"2017","journal-title":"World J. Gastroenterol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1093\/glycob\/cws076","article-title":"Presence of terminal n-acetylgalactosaminebeta1-4n-acetylglucosamine residues on o-linked oligosaccharides from gastric muc5ac: Involvement in helicobacter pylori colonization?","volume":"22","author":"Kenny","year":"2012","journal-title":"Glycobiology"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1093\/glycob\/cwi049","article-title":"Identification and characterization of binding properties of helicobacter pylori by glycoconjugate arrays","volume":"15","author":"Walz","year":"2005","journal-title":"Glycobiology"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"25256","DOI":"10.1074\/jbc.M111.233601","article-title":"Baba-mediated adherence is a potentiator of the helicobacter pylori type iv secretion system activity","volume":"286","author":"Ishijima","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1186\/1478-811X-11-77","article-title":"The functional interplay of helicobacter pylori factors with gastric epithelial cells induces a multi-step process in pathogenesis","volume":"11","author":"Posselt","year":"2013","journal-title":"Cell Commun. Signal"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1080\/21505594.2018.1440171","article-title":"Helicobacter pylori saba binding gangliosides of human stomach","volume":"9","author":"Benktander","year":"2018","journal-title":"Virulence"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1007\/s004280050269","article-title":"Helicobacter pylori infection produces reversible glycosylation changes to gastric mucins","volume":"433","author":"Ota","year":"1998","journal-title":"Virchows Arch."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Doohan, D., Rezkitha, Y.A.A., Waskito, L.A., Yamaoka, Y., and Miftahussurur, M. (2021). Helicobacter pylori baba-saba key roles in the adherence phase: The synergic mechanism for successful colonization and disease development. Toxins, 13.","DOI":"10.3390\/toxins13070485"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1126\/science.1069076","article-title":"Helicobacter pylori saba adhesin in persistent infection and chronic inflammation","volume":"297","author":"Mahdavi","year":"2002","journal-title":"Science"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1136\/gut.2005.083014","article-title":"Helicobacter pylori outer membrane proteins and gastroduodenal disease","volume":"55","author":"Yamaoka","year":"2006","journal-title":"Gut"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"ftx113","DOI":"10.1093\/femspd\/ftx113","article-title":"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","volume":"75","author":"Horridge","year":"2017","journal-title":"Pathog. Dis."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"12767","DOI":"10.3748\/wjg.v20.i36.12767","article-title":"Effect of helicobacter pylori on gastric epithelial cells","volume":"20","author":"Alzahrani","year":"2014","journal-title":"World J. Gastroenterol."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Braga, L., Batista, M.H.R., de Azevedo, O.G.R., Costa, K.C.d., Gomes, A.D., Rocha, G.A., and Queiroz, D.M.M. (2019). Oipa \u201con\u201d status of helicobacter pylori is associated with gastric cancer in north-eastern brazil. BMC Cancer, 19.","DOI":"10.1186\/s12885-018-5249-x"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1111\/j.1462-5822.2007.01104.x","article-title":"Oipa plays a role in helicobacter pylori-induced focal adhesion kinase activation and cytoskeletal re-organization","volume":"10","author":"Tabassam","year":"2008","journal-title":"Cell Microbiol."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Ansari, S., and Yamaoka, Y. (2020). Helicobacter pylori virulence factor cytotoxin-associated gene a (caga)-mediated gastric pathogenicity. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21197430"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/j.tim.2020.02.004","article-title":"The helicobacter pylori cag type iv secretion system","volume":"28","author":"Cover","year":"2020","journal-title":"Trends Microbiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1218","DOI":"10.1086\/597416","article-title":"Role of helicobacter pylori caga molecular variations in induction of host phenotypes with carcinogenic potential","volume":"199","author":"Schneider","year":"2009","journal-title":"J. Infect. Dis."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1186\/s12929-018-0466-9","article-title":"The impacts of h. Pylori virulence factors on the development of gastroduodenal diseases","volume":"25","author":"Chang","year":"2018","journal-title":"J. Biomed. Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"196","DOI":"10.2183\/pjab.93.013","article-title":"Structure and function of helicobacter pylori caga, the first-identified bacterial protein involved in human cancer","volume":"93","author":"Hatakeyama","year":"2017","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/s41423-019-0339-5","article-title":"Molecular anatomy and pathogenic actions of helicobacter pylori caga that underpin gastric carcinogenesis","volume":"17","author":"Knight","year":"2020","journal-title":"Cell Mol. Immunol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"e01869-15","DOI":"10.1128\/mBio.01869-15","article-title":"Helicobacter pylori diversity and gastric cancer risk","volume":"7","author":"Cover","year":"2016","journal-title":"mBio"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/j.1523-5378.2010.00759.x","article-title":"The versatility of helicobacter pylori caga effector protein functions: The master key hypothesis","volume":"15","author":"Backert","year":"2010","journal-title":"Helicobacter"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1186\/s13046-018-0962-5","article-title":"Helicobacter pylori caga promotes epithelial mesenchymal transition in gastric carcinogenesis via triggering oncogenic yap pathway","volume":"37","author":"Li","year":"2018","journal-title":"J. Exp. Clin. Cancer Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1080\/19490976.2020.1774311","article-title":"Inhibition of autophagy aggravates DNA damage response and gastric tumorigenesis via rad51 ubiquitination in response to h. Pylori infection","volume":"11","author":"Xie","year":"2020","journal-title":"Gut Microbes"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Ansari, S., and Yamaoka, Y. (2019). Helicobacter pylori virulence factors exploiting gastric colonization and its pathogenicity. Toxins, 11.","DOI":"10.3390\/toxins11110677"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Ricci, V. (2016). Relationship between vaca toxin and host cell autophagy in helicobacter pylori infection of the human stomach: A few answers, many questions. Toxins, 8.","DOI":"10.3390\/toxins8070203"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/S0014-5793(98)00788-1","article-title":"Vacuolation induced by cytotoxin from helicobacter pylori is mediated by the egf receptor in hela cells","volume":"431","author":"Seto","year":"1998","journal-title":"FEBS Lett."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"19183","DOI":"10.1074\/jbc.M300117200","article-title":"Protein-tyrosine phosphatase alpha, rptp alpha, is a helicobacter pylori vaca receptor","volume":"278","author":"Yahiro","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"36693","DOI":"10.1074\/jbc.274.51.36693","article-title":"Activation of helicobacter pylori vaca toxin by alkaline or acid conditions increases its binding to a 250-kda receptor protein-tyrosine phosphatase beta","volume":"274","author":"Yahiro","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"31104","DOI":"10.1074\/jbc.M112.387498","article-title":"Low-density lipoprotein receptor-related protein-1 (lrp1) mediates autophagy and apoptosis caused by helicobacter pylori vaca","volume":"287","author":"Yahiro","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"92","DOI":"10.3389\/fcimb.2012.00092","article-title":"Vacuolating cytotoxin a (vaca), a key toxin for helicobacter pylori pathogenesis","volume":"2","author":"Palframan","year":"2012","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"11250","DOI":"10.1074\/jbc.M509404200","article-title":"Helicobacter pylori vacuolating cytotoxin induces activation of the proapoptotic proteins bax and bak, leading to cytochrome c release and cell death, independent of vacuolation","volume":"281","author":"Yamasaki","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.tim.2013.09.004","article-title":"Modulation of autophagy by helicobacter pylori and its role in gastric carcinogenesis","volume":"21","author":"Greenfield","year":"2013","journal-title":"Trends Microbiol."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Trang, T.T.H., Binh, T.T., and Yamaoka, Y. (2016). Relationship between vaca types and development of gastroduodenal diseases. Toxins, 8.","DOI":"10.3390\/toxins8060182"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Aftab, H., Miftahussurur, M., Subsomwong, P., Ahmed, F., Khan, A.K.A., Matsumoto, T., Suzuki, R., and Yamaoka, Y. (2017). Two populations of less-virulent helicobacter pylori genotypes in bangladesh. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0182947"},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Sahara, S., Sugimoto, M., Vilaichone, R.K., Mahachai, V., Miyajima, H., Furuta, T., and Yamaoka, Y. (2012). Role of helicobacter pylori caga epiya motif and vaca genotypes for the development of gastrointestinal diseases in southeast asian countries: A meta-analysis. BMC Infect. Dis., 12.","DOI":"10.1186\/1471-2334-12-223"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Drayton, M., Deisinger, J.P., Ludwig, K.C., Raheem, N., Muller, A., Schneider, T., and Straus, S.K. (2021). Host defense peptides: Dual antimicrobial and immunomodulatory action. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222011172"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"582779","DOI":"10.3389\/fmicb.2020.582779","article-title":"Antimicrobial peptides: Classification, design, application and research progress in multiple fields","volume":"11","author":"Huan","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"e12555","DOI":"10.1111\/hel.12555","article-title":"Review of antimicrobial peptides with anti-helicobacter pylori activity","volume":"24","author":"Neshani","year":"2019","journal-title":"Helicobacter"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"545","DOI":"10.3390\/ph7050545","article-title":"Human antimicrobial peptides and proteins","volume":"7","author":"Wang","year":"2014","journal-title":"Pharmaceuticals"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"10957","DOI":"10.1007\/s11033-012-1997-x","article-title":"Cathelicidins: Family of antimicrobial peptides. A review","volume":"39","author":"Kosciuczuk","year":"2012","journal-title":"Mol. Biol. Rep."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1902","DOI":"10.3389\/fmicb.2020.01902","article-title":"Cathelicidin host defense peptides and inflammatory signaling: Striking a balance","volume":"11","author":"Alford","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1613","DOI":"10.1053\/j.gastro.2003.08.028","article-title":"Expression of ll-37 by human gastric epithelial cells as a potential host defense mechanism against helicobacter pylori","volume":"125","author":"Hase","year":"2003","journal-title":"Gastroenterology"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"10094","DOI":"10.1002\/jcp.29826","article-title":"Helicobacter pylori promote inflammation and host defense through the caga-dependent activation of mtorc1","volume":"235","author":"Feng","year":"2020","journal-title":"J. Cell Physiol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.4049\/jimmunol.1500021","article-title":"Critical role of antimicrobial peptide cathelicidin for controlling helicobacter pylori survival and infection","volume":"196","author":"Zhang","year":"2016","journal-title":"J. Immunol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1038\/gt.2012.92","article-title":"Cathelicidin protects against helicobacter pylori colonization and the associated gastritis in mice","volume":"20","author":"Zhang","year":"2013","journal-title":"Gene Ther."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.3390\/ph6121543","article-title":"Antimicrobial peptides","volume":"6","author":"Bahar","year":"2013","journal-title":"Pharmaceuticals"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.peptides.2014.09.021","article-title":"Inhibition and destruction of pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides","volume":"62","author":"Dosler","year":"2014","journal-title":"Peptides"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Kumar, P., Kizhakkedathu, J.N., and Straus, S.K. (2018). Antimicrobial peptides: Diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules, 8.","DOI":"10.3390\/biom8010004"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1038\/nchembio.1393","article-title":"Immune modulation by multifaceted cationic host defense (antimicrobial) peptides","volume":"9","author":"Hilchie","year":"2013","journal-title":"Nat. Chem. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"104930","DOI":"10.1016\/j.micpath.2021.104930","article-title":"Promising role of defensins peptides as therapeutics to combat against viral infection","volume":"155","author":"Solanki","year":"2021","journal-title":"Microb. Pathog."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"764","DOI":"10.3389\/fimmu.2020.00764","article-title":"Defensins: A double-edged sword in host immunity","volume":"11","author":"Xu","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Pero, R., Coretti, L., Nigro, E., Lembo, F., Laneri, S., Lombardo, B., Daniele, A., and Scudiero, O. (2017). Beta-defensins in the fight against helicobacter pylori. Molecules, 22.","DOI":"10.3390\/molecules22030424"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1007\/s00011-008-8100-z","article-title":"Helicobacter pylori induces the release of alpha-defensin by human granulocytes","volume":"58","author":"Kocsis","year":"2009","journal-title":"Inflamm. Res."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1916","DOI":"10.1111\/j.1572-0241.2004.40334.x","article-title":"Elevated concentrations of alpha-defensins in gastric juice of patients with helicobacter pylori infection","volume":"99","author":"Isomoto","year":"2004","journal-title":"Am. J. Gastroenterol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"5412","DOI":"10.1128\/IAI.68.9.5412-5415.2000","article-title":"Regulation of human beta-defensins by gastric epithelial cells in response to infection with helicobacter pylori or stimulation with interleukin-1","volume":"68","author":"Cole","year":"2000","journal-title":"Infect. Immun."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1136\/gut.51.3.356","article-title":"Modulation of host antimicrobial peptide (beta-defensins 1 and 2) expression during gastritis","volume":"51","author":"Fedeli","year":"2002","journal-title":"Gut"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2183","DOI":"10.4049\/jimmunol.1900351","article-title":"Helicobacter pylori exploits the nlrc4 inflammasome to dampen host defenses","volume":"203","author":"Semper","year":"2019","journal-title":"J. Immunol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"ftv128","DOI":"10.1093\/femspd\/ftv128","article-title":"Novel epidermal growth factor receptor pathway mediates release of human beta-defensin 3 from helicobacter pylori-infected gastric epithelial cells","volume":"74","author":"Muhammad","year":"2016","journal-title":"Pathog. Dis."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1111\/j.1365-2362.2008.02071.x","article-title":"Expression of beta-defensin 4 is increased in human gastritis","volume":"39","author":"Otte","year":"2009","journal-title":"Eur. J. Clin. Investig."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"128","DOI":"10.3389\/fcimb.2019.00128","article-title":"Application of antimicrobial peptides of the innate immune system in combination with conventional antibiotics-a novel way to combat antibiotic resistance?","volume":"9","author":"Zharkova","year":"2019","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1038\/nri3532","article-title":"Autophagy in infection, inflammation and immunity","volume":"13","author":"Deretic","year":"2013","journal-title":"Nat. Rev. Immunol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.1111\/j.1462-5822.2007.00921.x","article-title":"Helicobacter pylori is invasive and it may be a facultative intracellular organism","volume":"9","author":"Dubois","year":"2007","journal-title":"Cell Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1046\/j.1523-5378.2000.00023.x","article-title":"Helicobacter pylori entry into human gastric epithelial cells: A potential determinant of virulence, persistence, and treatment failures","volume":"5","author":"Bjorkholm","year":"2000","journal-title":"Helicobacter"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"639","DOI":"10.4161\/auto.23782","article-title":"The impact of autophagic processes on the intracellular fate of helicobacter pylori: More tricks from an enigmatic pathogen?","volume":"9","author":"Deen","year":"2013","journal-title":"Autophagy"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1042\/bj0600604","article-title":"Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue","volume":"60","author":"Pressman","year":"1955","journal-title":"Biochem. J."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"138","DOI":"10.3389\/fcell.2020.00138","article-title":"Autophagy and stem cells: Self-eating for self-renewal","volume":"8","author":"Chang","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/s41580-018-0003-4","article-title":"Mechanism and medical implications of mammalian autophagy","volume":"19","author":"Dikic","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"540","DOI":"10.4161\/auto.5.4.8167","article-title":"When helicobacter pylori invades and replicates in the cells","volume":"5","author":"Wang","year":"2009","journal-title":"Autophagy"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1046\/j.1523-5378.1999.98690.x","article-title":"Invasiveness of helicobacter pylori into human gastric mucosa","volume":"4","author":"Ko","year":"1999","journal-title":"Helicobacter"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2108","DOI":"10.1128\/IAI.70.4.2108-2120.2002","article-title":"Specific entry of helicobacter pylori into cultured gastric epithelial cells via a zipper-like mechanism","volume":"70","author":"Kwok","year":"2002","journal-title":"Infect. Immun."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.semcdb.2019.07.014","article-title":"Autophagy in intracellular bacterial infection","volume":"101","author":"Hu","year":"2020","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"370","DOI":"10.4161\/auto.5.3.7663","article-title":"Effect of helicobacter pylori\u2019s vacuolating cytotoxin on the autophagy pathway in gastric epithelial cells","volume":"5","author":"Terebiznik","year":"2009","journal-title":"Autophagy"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.chom.2014.04.001","article-title":"The immune receptor nod1 and kinase rip2 interact with bacterial peptidoglycan on early endosomes to promote autophagy and inflammatory signaling","volume":"15","author":"Irving","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/cdd.2008.130","article-title":"Eating the enemy within: Autophagy in infectious diseases","volume":"16","author":"Orvedahl","year":"2009","journal-title":"Cell Death Differ."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1053\/j.gastro.2012.01.043","article-title":"Vacuolating cytotoxin and variants in atg16l1 that disrupt autophagy promote helicobacter pylori infection in humans","volume":"142","author":"Raju","year":"2012","journal-title":"Gastroenterology"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1038\/s41564-019-0441-6","article-title":"Vaca generates a protective intracellular reservoir for helicobacter pylori that is eliminated by activation of the lysosomal calcium channel trpml1","volume":"4","author":"Capurro","year":"2019","journal-title":"Nat. Microbiol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1038\/nrmicro1004","article-title":"Antimicrobial reactive oxygen and nitrogen species: Concepts and controversies","volume":"2","author":"Fang","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1179\/174329211X12968219310756","article-title":"Redox biology and gastric carcinogenesis: The role of helicobacter pylori","volume":"16","author":"Handa","year":"2011","journal-title":"Redox Rep."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/s00430-011-0227-9","article-title":"Helicobacter pylori regulates inos promoter by histone modifications in human gastric epithelial cells","volume":"201","author":"Angrisano","year":"2012","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"4250","DOI":"10.1038\/s41388-019-0702-0","article-title":"NF-kappab-induced nox1 activation promotes gastric tumorigenesis through the expansion of sox2-positive epithelial cells","volume":"38","author":"Echizen","year":"2019","journal-title":"Oncogene"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"C450","DOI":"10.1152\/ajpcell.00319.2004","article-title":"Helicobacter pylori lipopolysaccharide activates rac1 and transcription of nadph oxidase nox1 and its organizer noxo1 in guinea pig gastric mucosal cells","volume":"288","author":"Kawahara","year":"2005","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1111\/j.1365-2958.2011.07612.x","article-title":"How does the oxidative burst of macrophages kill bacteria? Still an open question","volume":"80","author":"Slauch","year":"2011","journal-title":"Mol. Microbiol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.freeradbiomed.2012.05.008","article-title":"What really happens in the neutrophil phagosome?","volume":"53","author":"Hurst","year":"2012","journal-title":"Free Radic. Biol. Med."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1111\/imr.12378","article-title":"Ncf1 polymorphism reveals oxidative regulation of autoimmune chronic inflammation","volume":"269","author":"Holmdahl","year":"2016","journal-title":"Immunol. Rev."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1046\/j.1365-2958.2000.02114.x","article-title":"Helicobacter pylori induces but survives the extracellular release of oxygen radicals from professional phagocytes using its catalase activity","volume":"38","author":"Ramarao","year":"2000","journal-title":"Mol. Microbiol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"4034","DOI":"10.1128\/IAI.69.6.4034-4040.2001","article-title":"Superoxide dismutase-deficient mutants of helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization","volume":"69","author":"Seyler","year":"2001","journal-title":"Infect. Immun."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.it.2015.01.003","article-title":"Nitric oxide synthase in innate and adaptive immunity: An update","volume":"36","author":"Bogdan","year":"2015","journal-title":"Trends Immunol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"5839","DOI":"10.1073\/pnas.1804932115","article-title":"Oxygen radicals, nitric oxide, and peroxynitrite: Redox pathways in molecular medicine","volume":"115","author":"Radi","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"13844","DOI":"10.1073\/pnas.241443798","article-title":"Helicobacter pylori arginase inhibits nitric oxide production by eukaryotic cells: A strategy for bacterial survival","volume":"98","author":"Gobert","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"2572","DOI":"10.4049\/jimmunol.0902436","article-title":"Arginase ii restricts host defense to helicobacter pylori by attenuating inducible nitric oxide synthase translation in macrophages","volume":"184","author":"Lewis","year":"2010","journal-title":"J. Immunol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1159\/000519413","article-title":"The ideal helicobacter pylori treatment for the present and the future","volume":"103","author":"Suzuki","year":"2022","journal-title":"Digestion"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/5584_2019_367","article-title":"Current and future treatment of helicobacter pylori infections","volume":"1149","author":"Matsumoto","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"S56","DOI":"10.1136\/gut.43.2008.S56","article-title":"The life and death of helicobacter pylori","volume":"43","author":"Scott","year":"1998","journal-title":"Gut"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1038\/ajg.2016.563","article-title":"Acg clinical guideline: Treatment of helicobacter pylori infection","volume":"112","author":"Chey","year":"2017","journal-title":"Am. J. Gastroenterol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/j.mayocp.2016.11.017","article-title":"Helicobacter pylori: The past, present, and future in management","volume":"92","author":"Kamboj","year":"2017","journal-title":"Mayo Clin. Proc."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Ji, J., and Yang, H. (2020). Using probiotics as supplementation for helicobacter pylori antibiotic therapy. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21031136"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"10644","DOI":"10.3748\/wjg.v21.i37.10644","article-title":"Are probiotics useful in helicobacter pylori eradication?","volume":"21","author":"Homan","year":"2015","journal-title":"World J. Gastroenterol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"96409","DOI":"10.18632\/oncotarget.21633","article-title":"Probiotics in 14-day triple therapy for asian pediatric patients with helicobacter pylori infection: A network meta-analysis","volume":"8","author":"Wen","year":"2017","journal-title":"Oncotarget"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"3150","DOI":"10.3748\/wjg.v22.i11.3150","article-title":"Vaccine against helicobacter pylori: Inevitable approach","volume":"22","author":"Abadi","year":"2016","journal-title":"World J. Gastroenterol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/S0025-6196(11)60838-0","article-title":"Helicobacter pylori vaccine: From past to future","volume":"83","author":"Agarwal","year":"2008","journal-title":"Mayo Clin. Proc."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1136\/gut.2003.022111","article-title":"H pylori antibiotic resistance: Prevalence, importance, and advances in testing","volume":"53","author":"Megraud","year":"2004","journal-title":"Gut"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"2870","DOI":"10.3748\/wjg.v23.i16.2870","article-title":"Strategies used by helicobacter pylori to establish persistent infection","volume":"23","author":"Abadi","year":"2017","journal-title":"World J. Gastroenterol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"e1719","DOI":"10.1093\/cid\/ciaa839","article-title":"Apparent intracellular helicobacter pylori detected by immunohistochemistry: The missing link in eradication failure","volume":"73","author":"Beer","year":"2021","journal-title":"Clin. Infect. Dis."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/s15010-018-1240-3","article-title":"Correction to: A review on anti-adhesion therapies of bacterial diseases","volume":"47","author":"Asadi","year":"2019","journal-title":"Infection"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1080\/10408398.2020.1846157","article-title":"Sialic acid-based strategies for the prevention and treatment of helicobacter pylori infection: Emerging trends in food industry","volume":"62","author":"Sun","year":"2022","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"11404","DOI":"10.1002\/anie.201906280","article-title":"Inhibition of pathogen adhesion by bacterial outer membrane-coated nanoparticles","volume":"58","author":"Zhang","year":"2019","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"4888","DOI":"10.2174\/1381612821666150820104028","article-title":"Polysaccharides as bacterial antiadhesive agents and \u201csmart\u201d constituents for improved drug delivery systems against helicobacter pylori infection","volume":"21","author":"Menchicchi","year":"2015","journal-title":"Curr. Pharm. Des."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/hel.12177","article-title":"Review: Prospects for the use of extracts and polysaccharides from marine algae to prevent and treat the diseases caused by helicobacter pylori","volume":"20","author":"Besednova","year":"2015","journal-title":"Helicobacter"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.copbio.2011.10.009","article-title":"Cranberry components for the therapy of infectious disease","volume":"23","author":"Shmuely","year":"2012","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"566730","DOI":"10.3389\/fcimb.2020.566730","article-title":"Vitamin d3 inhibits helicobacter pylori infection by activating the vitd3\/vdr-camp pathway in mice","volume":"10","author":"Zhou","year":"2020","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1016\/j.molimm.2004.05.005","article-title":"Histone-deacetylase inhibitors induce the cathelicidin ll-37 in gastrointestinal cells","volume":"41","author":"Schauber","year":"2004","journal-title":"Mol. Immunol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"44","DOI":"10.3390\/antibiotics4010044","article-title":"Augmentation of cationic antimicrobial peptide production with histone deacetylase inhibitors as a novel epigenetic therapy for bacterial infections","volume":"4","author":"Yedery","year":"2015","journal-title":"Antibiotics"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.semcdb.2020.01.007","article-title":"Cellular evasion strategies of helicobacter pylori in regulating its intracellular fate","volume":"101","author":"Sit","year":"2020","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"e12324","DOI":"10.1111\/hel.12324","article-title":"The internalization of helicobacter pylori plays a role in the failure of h. Pylori eradication","volume":"22","author":"Wang","year":"2017","journal-title":"Helicobacter"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1080\/15548627.2018.1557835","article-title":"Vitamin d3 activates the autolysosomal degradation function against helicobacter pylori through the pdia3 receptor in gastric epithelial cells","volume":"15","author":"Hu","year":"2019","journal-title":"Autophagy"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/j.jcmgh.2017.02.002","article-title":"Oxidative stress resulting from helicobacter pylori infection contributes to gastric carcinogenesis","volume":"3","author":"Butcher","year":"2017","journal-title":"Cell Mol. Gastroenterol. Hepatol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1038\/s41467-021-22286-x","article-title":"In vivo activation of ph-responsive oxidase-like graphitic nanozymes for selective killing of helicobacter pylori","volume":"12","author":"Zhang","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"6863","DOI":"10.1093\/nar\/gkab440","article-title":"Hp1021 is a redox switch protein identified in helicobacter pylori","volume":"49","author":"Szczepanowski","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1128\/CMR.00011-10","article-title":"Helicobacter pylori and gastric cancer: Factors that modulate disease risk","volume":"23","author":"Wroblewski","year":"2010","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.2217\/fmb.09.87","article-title":"The vitamin d-antimicrobial peptide pathway and its role in protection against infection","volume":"4","author":"Gombart","year":"2009","journal-title":"Future Microbiol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"eaay8085","DOI":"10.1126\/science.aay8085","article-title":"Mammalian lipid droplets are innate immune hubs integrating cell metabolism and host defense","volume":"370","author":"Bosch","year":"2020","journal-title":"Science"},{"key":"ref_141","first-page":"1","article-title":"Autophagy-activating strategies to promote innate defense against mycobacteria","volume":"51","author":"Kim","year":"2019","journal-title":"Exp. Mol. Med."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/18\/10941\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:34:10Z","timestamp":1760142850000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/18\/10941"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,19]]},"references-count":141,"journal-issue":{"issue":"18","published-online":{"date-parts":[[2022,9]]}},"alternative-id":["ijms231810941"],"URL":"https:\/\/doi.org\/10.3390\/ijms231810941","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,19]]}}}