Dataset Information

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): LTQ Orbitrap Velos

ORGANISM(S): Helicobacter Pylori 26695

SUBMITTER: Hau-Ming Jan

LAB HEAD: Chun-Hung Lin

PROVIDER: PXD017518 | Pride | 2020-03-19

REPOSITORIES: Pride

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

Jan Hau-Ming HM Chen Yi-Chi YC Yang Tsai-Chen TC Ong Lih-Lih LL Chang Chia-Chen CC Muthusamy Sasikala S Abera Andualem Bahiru AB Wu Ming-Shiang MS Gervay-Hague Jacquelyn J Mong Kwok-Kong Tony KT Lin Chun-Hung CH

Communications biology 20200313 1

Helicobacter pylori, the most common etiologic agent of gastric diseases including gastric cancer, is auxotrophic for cholesterol and has to hijack it from gastric epithelia. Upon uptake, the bacteria convert cholesterol to cholesteryl 6'-O-acyl-α-D-glucopyranoside (CAG) to promote lipid raft clustering in the host cell membranes. However, how CAG appears in the host to exert the pathogenesis still remains ambiguous. Herein we identified hp0499 to be the gene of cholesteryl α-D-glucopyranoside a ...[more]

PMID: 32170208

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			Action	DRS
	26695OMV.mzid.gz	Mzid
	26695OMV.pride.mztab.gz	Mztab
	26695_OMV_160907.raw	Raw
	F064153.mgf	Mgf
	F064153.pride.mgf.gz	Mgf