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Review
.2017 Mar 11;9(3):101.
doi: 10.3390/toxins9030101.

Helicobacter pylori Outer Membrane Protein-Related Pathogenesis

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 inH. 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 ofH. pylori. This review summarizes the mechanisms through whichH. 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.

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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 ofH. 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.
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