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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Project description:. The transition of the opportunistic pathogen Pseudomonas aeruginosa from free-living bacteria into surface-associated biofilm communities represents a viable target for the prevention and treatment of chronic infectious disease. We have established a proteomics platform that identified 2443 and 1142 high-confidence proteins in P. aeruginosa whole cells and outer membrane vesicles (OMVs), respectively, at three time points during biofilm development. Analysis of cellular systems, specifically the phenazine biosynthetic pathway, demonstrates that whole cell protein abundance correlates to end product (i.e., pyocyanin) concentrations in biofilm but not planktonic cultures. Furthermore, increased cellular protein abundance in this pathway results in quantifiable pyocyanin in early biofilm OMVs, and OMVs from both growth modes isolated at later time points. Overall, our data indicate that the OMVs being released from the surface of the biofilm whole cells have unique proteomes in comparison to their planktonic counterparts. The relative abundance of OMV proteins from various subcellular sources showed considerable differences between the two growth modes over time, supporting the existence and preferential activation of multiple OMV biogenesis mechanisms under different conditions. The consistent detection of cytoplasmic proteins in the OMV subproteome suggests that these proteins may contribute a small but functionally relevant component to biofilm OMVs. Direct comparisons of outer membrane protein abundance levels between OMVs and whole cells shows ratios that vary greatly from 1:1, and supports previous studies that advocate specific inclusion, or “packaging”, of proteins into OMVs. The detailed analysis of packaged protein groups indicates biogenesis mechanisms that involve untethered, rather than absent, peptidoglycan-binding proteins. Collectively, individual protein and biological system analyses of biofilm OMVs show that drug-binding cytoplasmic proteins and porins are shuttled from the whole cell into the OMVs, potentially contributing to the antibiotic resistance of P. aeruginosa whole cells within biofilms.

Dataset Information

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

Publications

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

Similar Datasets

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