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 |
|---|---|
| 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
Cite this
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Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori. / Webb, Chaille T.; Chandrapala, Dilini; Oslan, Siti Nurbaya; Bamert, Rebecca S.; Grinter, Rhys D.; Dunstan, Rhys A.; Gorrell, Rebecca J.; Song, Jiangning; Strugnell, Richard A; Lithgow, Trevor ; Kwok, Terry.
In: MicrobiologyOpen, Vol. 6, No. 6, e00513, 01.12.2017.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori
AU - Webb, Chaille T.
AU - Chandrapala, Dilini
AU - Oslan, Siti Nurbaya
AU - Bamert, Rebecca S.
AU - Grinter, Rhys D.
AU - Dunstan, Rhys A.
AU - Gorrell, Rebecca J.
AU - Song, Jiangning
AU - Strugnell, Richard A
AU - Lithgow, Trevor
AU - Kwok, Terry
PY - 2017/12/1
Y1 - 2017/12/1
N2 - 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.
AB - 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.
KW - BAM complex
KW - beta-barrel
KW - Helicobacter
KW - outer membrane
KW - surface protein
UR - http://www.scopus.com/inward/record.url?scp=85031777046&partnerID=8YFLogxK
U2 - 10.1002/mbo3.513
DO - 10.1002/mbo3.513
M3 - Article
VL - 6
JO - MicrobiologyOpen
JF - MicrobiologyOpen
SN - 2045-8827
IS - 6
M1 - e00513
ER -