Citation
Webb, Chaille T. and Chandrapala, Dilini and Oslan, Siti Nurbaya and Bamert, Rebecca S. and Grinter, Rhys D. and Dunstan, Rhys A. and Gorrell, Rebecca J. and Song, Jiangning and Strugnell, Richard A. and Lithgow, Trevor and Kwok, Terry
(2017)
Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori.
MicrobiologyOpen, 6 (6).
pp. 1-17.
ISSN 2045-8827
Abstract
Helicobacter pylori is a gram-negative bacterial pathogen that chronically inhabits the human stomach. To survive and maintain advantage, it has evolved unique host-pathogen interactions mediated by Helicobacter-specific proteins in the bacterial outer membrane. These outer membrane proteins (OMPs) are anchored to the cell surface via a C-terminal β-barrel domain, which requires their assembly by the β-barrel assembly machinery (BAM). Here we have assessed the complexity of the OMP C-terminal β-barrel domains employed by H. pylori, and characterized the H. pyloriBAM complex. Around 50 Helicobacter-specific OMPs were assessed with predictive structural algorithms. The data suggest that H. pylori utilizes a unique β-barrel architecture that might constitute H. pylori-specific Type V secretions system. The structural and functional diversity in these proteins is encompassed by their extramembrane domains. Bioinformatic and biochemical characterization suggests that the low β-barrel-complexity requires only minimalist assembly machinery. The H. pylori proteins BamA and BamD associate to form a BAM complex, with features of BamA enabling an oligomerization that might represent a mechanism by which a minimalist BAM complex forms a larger, sophisticated machinery capable of servicing the outer membrane proteome of H. pylori.
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