Phospholipid binding residues of eukaryotic membrane-remodelling F-BAR domain proteins are conserved in Helicobacter pylori CagA.

ABSTRACT:

Background

Cytotoxin associated gene product A (CagA) is an oncogenic protein secreted by the gastric bacterium Helicobacter pylori. Internalization of CagA by human epithelial cells occurs by an unknown mechanism that requires interaction with the host membrane lipid phosphatidylserine.

Findings

Local homology at the level of amino acid sequence and secondary structure has been identified between the membrane-tethering region of CagA and the lipid-binding Fes-CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domains of eukaryotic proteins. The F-BAR proteins are major components of the endocytic machinery. In addition to the membrane-binding F-BAR domains, they contain other domains that interact with actin-regulatory networks and mediate interplay between membrane dynamics and cyt

SUBMITTER: Roujeinikova A 

PROVIDER: S-EPMC4141123 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature