close
Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2017 Mar 11;9(3):101.
doi: 10.3390/toxins9030101.

Helicobacter pylori Outer Membrane Protein-Related Pathogenesis

Yuichi Matsuo  1 , Yasutoshi Kido  2 , Yoshio Yamaoka  3   4
Affiliations
Review

Helicobacter pylori Outer Membrane Protein-Related Pathogenesis

Yuichi Matsuo et al. Toxins (Basel). .

Abstract

Helicobacter pylori colonizes the human stomach and induces inflammation, and in some cases persistent infection can result in gastric cancer. Attachment to the gastric mucosa is the first step in establishing bacterial colonization, and outer membrane proteins (OMPs) play a pivotal role in binding to human cells. Some OMP interaction molecules are known in H. pylori, and their associated host cell responses have been gradually clarified. Many studies have demonstrated that OMPs are essential to CagA translocation into gastric cells via the Type IV secretion system of H. pylori. This review summarizes the mechanisms through which H. pylori utilizes OMPs to colonize the human stomach and how OMPs cooperate with the Type IV secretion system.

Keywords: Helicobacter pylori; Type IV secretion system; outer membrane protein; pathogenesis.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic of outer membrane protein-mediated pathogenesis. (A) BabA interacts with Lea antigen and enhances CagA translocation via the Type 4 secretion system (T4SS). HopQ interacts with CEACAMs, and is essential for CagA translocation. BabA and HopQ might interact with the T4SS in the membrane region of H. pylori, although this is unclear. (B) Absence of sLex antigen expression in the healthy stomach. H. pylori infection induces β3GnT5 expression in gastric epithelial cells and biosynthesis of the sLex antigen; sLex localizes to the membrane region of gastric epithelial cells. As a result, H. pylori can colonize by utilizing SabA, which interacts with the sLex antigen. Although the detailed mechanism is unclear, TNF and the T4SS are suggested to induce β3GnT5 expression. (C) OipA is suggested to induce phosphorylation of EGFR, leading to activation of focal adhesion kinase (FAK) and Akt-related signaling. Activated FAK induces actin stress fiber remodeling via the MAPK and Erk1/2 signaling pathway. In addition, phosphorylation of Akt can activate FoxO transcription factors and induce IL-8 production. The binding partner of OipA and whether OipA can cooperate with the T4SS are unclear.
See this image and copyright information in PMC

References

    1. McConnell M.J., Actis L., Pachón J. Acinetobacter baumannii: Human infections; factors contributing to pathogenesis and animal models. FEMS Microbiol. Rev. 2013;37:130–155. doi: 10.1111/j.1574-6976.2012.00344.x. - DOI - PubMed
    1. Wu X., Chavez J.D., Schweppe D.K., Zheng C., Weisbrod C.R., Eng J.K., Murali A., Lee S.A., Ramage E., Gallagher L.A., et al. In vivo protein interaction network analysis reveals porin-localized antibiotic inactivation in Acinetobacter baumannii strain AB5075. Nat. Commun. 2016;11:13414. doi: 10.1038/ncomms13414. - DOI - PMC - PubMed
    1. Posselt G., Backert S., Wessler S. The functional interplay of Helicobacter pylori factors with gastric epithelial cells induces a multi-step process in pathogenesis. Cell Commun. Signal. 2013;7:77. doi: 10.1186/1478-811X-11-77. - DOI - PMC - PubMed
    1. Terradot L., Waksman G. Architecture of the Helicobacter Cag-type IV secretion system. FEBS J. 2011;278:1213–1222. doi: 10.1111/j.1742-4658.2011.08037.x. - DOI - PubMed
    1. Backert S., Fronzes R., Waksman G. VirB2 and VirB5 proteins: Specialized adhesins in bacterial type-IV secretion systems? Trends Microbiol. 2008;16:409–413. doi: 10.1016/j.tim.2008.07.001. - DOI - PubMed

MeSH terms

Substances

LinkOut - more resources