幽门螺杆菌黏附素BabA的致病性
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摘要
幽门螺杆菌在人群中感染非常普遍。全世界约有三分之二人口感染了幽门螺杆菌。长期慢性幽门螺杆菌感染能诱发炎症,如慢性胃炎和溃疡,甚至恶性肿瘤(如黏膜胃癌和相关淋巴组织淋巴瘤)。吸附在胃黏膜上是幽门螺旋杆菌定植宿主和诱发炎症的第一步,在此过程中,细菌很多外膜蛋白发挥了关键作用。本文将重点论述幽门螺杆菌外膜蛋白中的血型结合黏附素(blood-group-antigen-binding adhesin, BabA),并从宿主受体分子、黏附区域晶体结构和酸适应性等方面阐述其在幽门螺杆菌致病过程中的作用。
Helicobacter pylori(H. pylori) is a common acquired gastric pathogen and infects almost twothirds of world's population. Long-term chronic infection can lead to gastritis and duodenal ulcers including gastric cancer or mucosa-associated lymphoid tissue(MALT) lymphoma. Adhesion to the mucosal epithelium is the first step to colonize in host and induce gastric inflammation. A large number of outer membrane proteins(OMPs) were involved in this process including blood-group-antigen-binding adhesin(BabA). This review summarizes interacted partner, the crystallized structure of adherence domain and pH-sensitive adaption of BabA, besides that how BabA's structure influence H. pylori pathogenesis was also illustrated.
Helicobacter pylori(H. pylori) is a common acquired gastric pathogen and infects almost twothirds of world's population. Long-term chronic infection can lead to gastritis and duodenal ulcers including gastric cancer or mucosa-associated lymphoid tissue(MALT) lymphoma. Adhesion to the mucosal epithelium is the first step to colonize in host and induce gastric inflammation. A large number of outer membrane proteins(OMPs) were involved in this process including blood-group-antigen-binding adhesin(BabA). This review summarizes interacted partner, the crystallized structure of adherence domain and pH-sensitive adaption of BabA, besides that how BabA's structure influence H. pylori pathogenesis was also illustrated.
引文
[1]Ronnie H, Bradley AC. Infectious Diseases Related to Travel, Helicobacter pylori[EB/OL]. Atlanta, USA:Centers for Disease Control and Prevention,(2017-6-12)[2019-4-15]. https://wwwnc.cdc.gov/travel/yellowbook/2018/infectious-diseases-related-to-travel/helicobacter-pylori.
[2]Matsuo Y, Kido Y, Yamaoka Y. Helicobacter pylori outer membrane protein-related pathogenesis. Toxins(Basel),2017, 9(3):101-110
[3]Kumar S, Dhiman M. Inflammasome activation and regulation during Helicobacter pylori pathogenesis. Microb Pathog, 2018, 125:468-474
[4]Rad R, Gerhard M, Lang R, et al. The Helicobacter pylori blood group antigen-binding adhesin facilitates bacterial colonization and augments a nonspecific immune response. J Immunol, 2002, 168(6):3033-3041
[5]Krzyzek P, Gosciniak G. Oral Helicobacter pylori:Interactions with host and microbial flora of the oral cavity. Dent Med Probl, 2018, 55(1):75-82
[6]Ilver D, Arnqvist A, Ogren J, et al. Helicobacter pylori adhesinbindingfucosylatedhisto-bloodgroupantigens revealed by retagging. Science, 1998, 279(5349):373-377
[7]Sweeney EG, Guillemin K. H. pylori's BabA embraces change. Cell Host Microbe, 2016, 19(1):5-7
[8]Styer CM, Hansen LM, Cooke CL, et al. Expression of the BabA adhesin during experimental infection with Helicobacter pylori. Infect Immun, 2010, 78(4):1593-1600
[9]Kable ME, Hansen LM, Styer CM, et al. Host determinantsofexpressionoftheHelicobacterpyloriBabA adhesin. Sci Rep, 2017, 7:46499
[10]Asl SF, Pourvahedi M, Mojtahedi A, et al. Analysis of babA, cagE and cagA genes in Helicobacter pylori from upper gastric patients in the north of Iran. Infect Disord Drug Targets, 2018, 18(1):doi:10.2174/1871526518666180515113218
[11]Benktander J, Angstrom J, Breimer ME, et al. RedefinitionofthecarbohydratebindingspecificityofHelicobacter pylori BabA adhesin. J Biol Chem, 2012, 287(38):31712-31724
[12]Hatakeyama M. A sour relationship between BabA and Lewis b. Cell Host Microbe, 2017, 21(3):318-320
[13]Stanley P CRSCtDGIVA, Cummings RD, Esko JD, et al.,editors. Essentials of Glycobiology. 2nd ed. Cold Spring Harbor(NY):Cold Spring Harbor Laboratory Press,2009. Chapter 13.
[14]Aspholm-Hurtig M, Dailide G, Lahmann M, et al.FunctionaladaptationofBabA,theH.pylori ABO bloodgroupantigenbindingadhesin.Science,2004,305(5683):519-522
[15]Skoog EC, Padra M, Aberg A, et al. BabA dependent binding of Helicobacter pylori to human gastric mucins cause aggregation that inhibits proliferation and is regulated via ArsS. Sci Rep, 2017, 7:40656
[16]Gerhard M, Lehn N, Neumayer N, et al. Clinical relevance of the Helicobacter pylori gene for blood-group antigen-binding adhesin. Proc Natl Acad Sci USA, 1999,96(22):12778-12783
[17]Moonens K, Gideonsson P, Subedi S, et al. Structural insights into polymorphic ABO glycan binding by Helicobacter pylori. Cell Host Microbe, 2016, 19(1):55-66
[18]Schreiber S, Konradt M, Groll C, et al. The spatial orientation of Helicobacter pylori in the gastric mucus. Proc Natl Acad Sci USA, 2004, 101(14):5024-5029
[19]Bugaytsova JA, Bjornham O, Chernov YA, et al. Helicobacter pylori adapts to chronic infection and gastric disease via pH-responsive BabA-mediated adherence. Cell Host Microbe, 2017, 21(3):376-389
[20]Quintana-Hayashi MP, Rocha R, Padra M, et al. BabAmediatedadherenceofpediatriculcerogenicH.pylori strains to gastric mucins at neutral and acidic pH. Virulence, 2018, 9(1):1699-1717
[21]Jencks DS, Adam JD, Borum ML, et al. Overview of current concepts in gastric intestinal metaplasia and gastric cancer. Gastroenterol Hepatol(N Y), 2018, 14(2):92-101
[22]Correa P. Gastric cancer:overview. Gastroenterol Clin North Am, 2013, 42(2):211-217
[2]Matsuo Y, Kido Y, Yamaoka Y. Helicobacter pylori outer membrane protein-related pathogenesis. Toxins(Basel),2017, 9(3):101-110
[3]Kumar S, Dhiman M. Inflammasome activation and regulation during Helicobacter pylori pathogenesis. Microb Pathog, 2018, 125:468-474
[4]Rad R, Gerhard M, Lang R, et al. The Helicobacter pylori blood group antigen-binding adhesin facilitates bacterial colonization and augments a nonspecific immune response. J Immunol, 2002, 168(6):3033-3041
[5]Krzyzek P, Gosciniak G. Oral Helicobacter pylori:Interactions with host and microbial flora of the oral cavity. Dent Med Probl, 2018, 55(1):75-82
[6]Ilver D, Arnqvist A, Ogren J, et al. Helicobacter pylori adhesinbindingfucosylatedhisto-bloodgroupantigens revealed by retagging. Science, 1998, 279(5349):373-377
[7]Sweeney EG, Guillemin K. H. pylori's BabA embraces change. Cell Host Microbe, 2016, 19(1):5-7
[8]Styer CM, Hansen LM, Cooke CL, et al. Expression of the BabA adhesin during experimental infection with Helicobacter pylori. Infect Immun, 2010, 78(4):1593-1600
[9]Kable ME, Hansen LM, Styer CM, et al. Host determinantsofexpressionoftheHelicobacterpyloriBabA adhesin. Sci Rep, 2017, 7:46499
[10]Asl SF, Pourvahedi M, Mojtahedi A, et al. Analysis of babA, cagE and cagA genes in Helicobacter pylori from upper gastric patients in the north of Iran. Infect Disord Drug Targets, 2018, 18(1):doi:10.2174/1871526518666180515113218
[11]Benktander J, Angstrom J, Breimer ME, et al. RedefinitionofthecarbohydratebindingspecificityofHelicobacter pylori BabA adhesin. J Biol Chem, 2012, 287(38):31712-31724
[12]Hatakeyama M. A sour relationship between BabA and Lewis b. Cell Host Microbe, 2017, 21(3):318-320
[13]Stanley P CRSCtDGIVA, Cummings RD, Esko JD, et al.,editors. Essentials of Glycobiology. 2nd ed. Cold Spring Harbor(NY):Cold Spring Harbor Laboratory Press,2009. Chapter 13.
[14]Aspholm-Hurtig M, Dailide G, Lahmann M, et al.FunctionaladaptationofBabA,theH.pylori ABO bloodgroupantigenbindingadhesin.Science,2004,305(5683):519-522
[15]Skoog EC, Padra M, Aberg A, et al. BabA dependent binding of Helicobacter pylori to human gastric mucins cause aggregation that inhibits proliferation and is regulated via ArsS. Sci Rep, 2017, 7:40656
[16]Gerhard M, Lehn N, Neumayer N, et al. Clinical relevance of the Helicobacter pylori gene for blood-group antigen-binding adhesin. Proc Natl Acad Sci USA, 1999,96(22):12778-12783
[17]Moonens K, Gideonsson P, Subedi S, et al. Structural insights into polymorphic ABO glycan binding by Helicobacter pylori. Cell Host Microbe, 2016, 19(1):55-66
[18]Schreiber S, Konradt M, Groll C, et al. The spatial orientation of Helicobacter pylori in the gastric mucus. Proc Natl Acad Sci USA, 2004, 101(14):5024-5029
[19]Bugaytsova JA, Bjornham O, Chernov YA, et al. Helicobacter pylori adapts to chronic infection and gastric disease via pH-responsive BabA-mediated adherence. Cell Host Microbe, 2017, 21(3):376-389
[20]Quintana-Hayashi MP, Rocha R, Padra M, et al. BabAmediatedadherenceofpediatriculcerogenicH.pylori strains to gastric mucins at neutral and acidic pH. Virulence, 2018, 9(1):1699-1717
[21]Jencks DS, Adam JD, Borum ML, et al. Overview of current concepts in gastric intestinal metaplasia and gastric cancer. Gastroenterol Hepatol(N Y), 2018, 14(2):92-101
[22]Correa P. Gastric cancer:overview. Gastroenterol Clin North Am, 2013, 42(2):211-217