6gw5

Publication Abstract from PubMed

The human stomach pathogen Helicobacter pylori attaches to healthy and inflamed gastric tissue through members of a paralogous family of "Helicobacter outer membrane proteins" (Hops), including adhesins BabA, SabA, HopQ, LabA and HopZ. Hops share a conserved 25 kDa C-terminal region that is thought to form an autotransporter-like transmembrane domain. Instead, our results show that Hops contain a non-continuous transmembrane domain, composed of seven predicted beta-strands at the C-terminus and one at the N-terminus. Folding and outer membrane localization of the C-terminal beta-domain critically depends on a predicted transmembrane beta-strand within the first 16 N-terminal residues. The N-terminus is shown to reside in the periplasm, and our crystal and small angle X-ray scattering structures for the SabA extracellular domain reveal a conserved coiled-coil stem domain that connects to transmembrane beta-strand 1 and 2. Taken together, our data show that Hop adhesins represent a novel outer membrane protein topology encompassing an OmpA-like 8-stranded beta-barrel that is interrupted by a 15 to 108 kDa domain inserted inside the first extracellular loop. The insertion of large, folded domains in an extracellular loop is unprecedented in bacterial outer membrane proteins and is expected to have important consequences on how these proteins reach the cell surface. This article is protected by copyright. All rights reserved.

Hop-family Helicobacter outer membrane adhesins form a novel class of Type 5-like secretion proteins with an interrupted beta-barrel domain.,Coppens F, Castaldo G, Debraekeleer A, Subedi S, Moonens K, Lo A, Remaut H Mol Microbiol. 2018 Jul 11. doi: 10.1111/mmi.14075. PMID:29995350^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.