Journal article

Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori

Chaille T Webb, Dilini Chandrapala, Siti Nurbaya Oslan, Rebecca S Bamert, Rhys D Grinter, Rhys A Dunstan, Rebecca J Gorrell, Jiangning Song, Richard A Strugnell, Trevor Lithgow, Terry Kwok

MICROBIOLOGYOPEN | WILEY | Published : 2017

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. pyl..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council (ARC) Laureate Fellowship award


Awarded by NHMRC Program Grant


Awarded by Ministry of Higher Education Malaysia


Awarded by National Health and Medical Research Council of Australia


Funding Acknowledgements

Australian Research Council (ARC) Laureate Fellowship award, Grant/Award Number: FL30100038; NHMRC Program Grant, Grant/Award Number: 1092262; Ministry of Higher Education Malaysia, Grant/Award Number: 1092262; Welcome Trust Fellow