Abstract
HpaA as an outer membrane protein of Helicobacter pylori (H. pylori) plays a significant role in the adhesion to the human stomach, but the functional relation between HpaA and gastric epithelial cells is still not clear. To screen the interaction between HpaA and cellular proteins in gastric epithelial cells, the HpaA protein from H. pylori 26695 fused with a tag (6× His) was expressed and purified successfully, the secondary structure was estimated by the Circular Dichroism (CD) spectrum, and the purified recombinant protein was used to perform the pull-down assays with gastric cancer cell lines (AGS and SGC-7901) lysates, respectively. The pull-down proteins were identified by high-performance liquid chromatography tandem mass spectrometry system (HPLC-MS/MS). A total of 9 and 13 proteins related were analyzed from AGS and SGC-7901 cell lysates, respectively. ANXA2 was considered as putative HpaA functional partner discovered from lysates of both cell lines with high score and coverage. It is hypothesized that HpaA may be involved in the biological process of regulation of transcription and nucleic acid metabolism during the adhesion of H. pylori to human gastric epithelial cells, and HpaA-binding proteins also be used as targets for the development of antiadhesion drugs against H. pylori.
Highlights
Helicobacter pylori (H. pylori) infection is a common and prevalent bacterial infection in the world
The adhesion of H. pylori to the gastric epithelium was mediated by the expression of adhesins and the receptor system [2,3,4], among which H. pylori adhesin (HpaA) as an outer membrane protein with approximately 29 kDa detected on the surface and flagellar sheath of H. pylori plays an important role in bacterial adhesion [5,6,7,8]
About the HpaA-binding proteins identified from AGS cells, we found a network composed of cleavage stimulation factor subunit 2 tau variant (CSTF2T), SNW domain-containing protein 1 (SNW1), and FUS in STRING database (Figure 3(c))
Summary
Helicobacter pylori (H. pylori) infection is a common and prevalent bacterial infection in the world. H. pylori adhesion and colonization are essential for the persistence of bacterial infection. HpaA was originally described by Evans et al [9] as a putative neuraminyllactose-binding hemagglutinin (NLBH) and could bind to various glycosylation components on the surface of gastric epithelial cells. Many studies tried to prove the function of HpaA in H. pylori adhesion, but results were controversial. Carlsohn et al [7] proposed that HpaA was essential for the colonization of H. pylori in mice. The earlier study proposed that bacterial binding to gastric cells was not affected by the inactivated hpaA gene [11]. The function and mechanism of the BioMed Research International action of HpaA mediating bacterial colonization in gastric epithelial cells were not clear due to the lack of related studies on molecular levels
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