Cholesteryl α-D-glucoside 6-acyltransferase enhances the adhesion of Helicobacter pylori to gastric epithelium

ABSTRACT: Cellular locations of (Cholesteryl α-D-glucoside 6-acyltransferase) CGAT To study the cellular location of CGAT, based on our pervious experiments, the CGAT activity was observed in the outer membrane vesicles (OMVs), rather than in the culture medium, suggesting that CGAT resided in the outer membrane can be enclosed in the OMVs and secreted to the extracellular space. We then performed proteomic analysis for OMVs. Based on proteomic analysis, we found CGAT was present in the OMVs isolated from the strains of H. pylori 26695 and ΔCGT-knock-out, instead of ΔCGAT-knock-out strain.

INSTRUMENT(S):

ORGANISM(S): Helicobacter Pylori 26695

SUBMITTER: Hau-Ming Jan  

LAB HEAD: Chun-Hung Lin

PROVIDER: PXD017518 | Pride | 2020-03-19

REPOSITORIES: Pride