Projects per year
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.
Original language | English |
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Article number | e00513 |
Number of pages | 17 |
Journal | MicrobiologyOpen |
Volume | 6 |
Issue number | 6 |
DOIs | |
Publication status | Published - 1 Dec 2017 |
Keywords
- BAM complex
- beta-barrel
- Helicobacter
- outer membrane
- surface protein
Projects
- 1 Finished
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NHMRC Program in Cellular Microbiology
Lithgow, T. (Primary Chief Investigator (PCI)), Dougan, G. (Chief Investigator (CI)) & Strugnell, R. A. (Chief Investigator (CI))
NHMRC - National Health and Medical Research Council (Australia)
1/01/16 → 31/12/20
Project: Research