Structural basis for the hijacking of endosomal sorting nexin proteins by Chlamydia trachomatis

Paul, Blessy, Kim, Hyun Sung, Kerr, Markus C., Huston, Wilhelmina M., Teasdale, Rohan D. and Collins, Brett M. (2017) Structural basis for the hijacking of endosomal sorting nexin proteins by Chlamydia trachomatis. eLife, 6 e22311: 1-23. doi:10.7554/eLife.22311


 
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Author Paul, Blessy
Kim, Hyun Sung
Kerr, Markus C.
Huston, Wilhelmina M.
Teasdale, Rohan D.
Collins, Brett M.
Title Structural basis for the hijacking of endosomal sorting nexin proteins by Chlamydia trachomatis
Formatted title
Structural basis for the hijacking of endosomal sorting nexin proteins by Chlamydia trachomatis
Journal name eLife   Check publisher's open access policy
ISSN 2050-084X
Publication date 2017-02-22
Year available 2017
Sub-type Article (original research)
DOI 10.7554/eLife.22311
Open Access Status DOI
Volume 6
Issue e22311
Start page 1
End page 23
Total pages 23
Place of publication Cambridge, United Kingdom
Publisher eLife Sciences Publications
Language eng
Subject 2800 Neuroscience
1300 Biochemistry, Genetics and Molecular Biology
2400 Immunology and Microbiology
Abstract During infection chlamydial pathogens form an intracellular membrane-bound replicative niche termed the inclusion, which is enriched with bacterial transmembrane proteins called Incs. Incs bind and manipulate host cell proteins to promote inclusion expansion and provide camouflage against innate immune responses. Sorting nexin (SNX) proteins that normally function in endosomal membrane trafficking are a major class of inclusion-associated host proteins, and are recruited by IncE/CT116. Crystal structures of the SNX5 phox-homology (PX) domain in complex with IncE define the precise molecular basis for these interactions. The binding site is unique to SNX5 and related family members SNX6 and SNX32. Intriguingly the site is also conserved in SNX5 homologues throughout evolution, suggesting that IncE captures SNX5-related proteins by mimicking a native host protein interaction. These findings thus provide the first mechanistic insights both into how chlamydial Incs hijack host proteins, and how SNX5-related PX domains function as scaffolds in protein complex assembly.
Keyword Inclusion Membrane-Proteins
Retrograde Trafficking
Inc Proteins
Infection
Interacts
Retromer
Genome
Domain
Replication
Persistence
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID 606788
APP1041929
APP1058734
APP1061574
DE120102321
DP0985029
DP150100364
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 5 times in Thomson Reuters Web of Science Article | Citations
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