Vibiro Vulnificus Hemolysin Associates with Gangliosides

Overview

Journal BMC Microbiol

Publisher Biomed Central

Specialty Microbiology

Date 2020 Apr 2

PMID 32228455

Citations 2

Authors

Takashige Kashimoto

Hiroyuki Sugiyama

Keigo Kawamidori

Kohei Yamazaki

Takehiro Kado

Kaho Matsuda

Toshio Kodama

Takao Mukai

Shunji Ueno

Affiliations

Soon will be listed here.

Abstract

Background: Vibrio vulnificus hemolysin (VVH) is a pore-forming toxin secreted by Vibrio vulnificus. Cellular cholesterol was believed to be the receptor for VVH, because cholesterol could bind to VVH and preincubation with cholesterol inhibited cytotoxicity. It has been reported that specific glycans such as N-acetyl-D-galactosamine and N-acetyl-D-lactosamine bind to VVH, however, it has not been known whether these glycans could inhibit the cytotoxicity of VVH without oligomer formation. Thus, to date, binding mechanisms of VVH to cellular membrane, including specific receptors have not been elucidated.

Results: We show here that VVH associates with ganglioside GM1a, Fucosyl-GM1, GD1a, GT1c, and GD1b by glycan array. Among them, GM1a could pulldown VVH. Moreover, the GD1a inhibited the cytotoxicity of VVH without the formation of oligomers.

Conclusion: This is the first report of a molecule able to inhibit the binding of VVH to target cells without oligomerization of VVH.

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