Imperial College London
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Dr Tiago Costa

Faculty of Natural Sciences, Department of Life Sciences

Senior Lecturer in Bacterial Pathogenesis
 
 
 
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Contact

 

+44 (0)20 7594 3696t.costa Website

 
 
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Location

 

5.02Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Gurung:2018:10.3389/fcimb.2018.00080,
author = {Gurung, JM and Amer, AAA and Francis, MK and Costa, TRD and Chen, S and Zavialov, AV and Francis, MS},
doi = {10.3389/fcimb.2018.00080},
journal = {Frontiers in Cellular and Infection Microbiology},
pages = {1--1},
title = {Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis Type III secretion},
url = {http://dx.doi.org/10.3389/fcimb.2018.00080},
volume = {8},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Type III secretion systems harbored by several Gram-negative bacteria are often used to deliver host-modulating effectors into infected eukaryotic cells. About 20 core proteins are needed for assembly of a secretion apparatus. Several of these proteins are genetically and functionally conserved in type III secretion systems of bacteria associated with invertebrate or vertebrate hosts. In the Ysc family of type III secretion systems are two poorly characterized protein families, the YscX family and the YscY family. In the plasmid-encoded Ysc-Yop type III secretion system of human pathogenic Yersinia species, YscX is a secreted substrate while YscY is its non-secreted cognate chaperone. Critically, neither an yscX nor yscY null mutant of Yersinia is capable of type III secretion. In this study, we show that the genetic equivalents of these proteins produced as components of other type III secretion systems of Pseudomonas aeruginosa (PscX and PscY), Aeromonas species (AscX and AscY), Vibrio species (VscX and VscY), and Photorhabdus luminescens (SctX and SctY) all possess an ability to interact with its native cognate partner and also establish cross-reciprocal binding to non-cognate partners as judged by a yeast two-hybrid assay. Moreover, a yeast three-hybrid assay also revealed that these heterodimeric complexes could maintain an interaction with YscV family members, a core membrane component of all type III secretion systems. Despite maintaining these molecular interactions, only expression of the native yscX in the near full-length yscX deletion and native yscY in the near full-length yscY deletion were able to complement for their general substrate secretion defects. Hence, YscX and YscY must have co-evolved to confer an important function specifically critical for Yersinia type III secretion.
AU  - Gurung,JM
AU  - Amer,AAA
AU  - Francis,MK
AU  - Costa,TRD
AU  - Chen,S
AU  - Zavialov,AV
AU  - Francis,MS
DO  - 10.3389/fcimb.2018.00080
EP  - 1
PY  - 2018///
SN  - 2235-2988
SP  - 1
TI  - Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis Type III secretion
T2  - Frontiers in Cellular and Infection Microbiology
UR  - http://dx.doi.org/10.3389/fcimb.2018.00080
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000427608900001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://www.frontiersin.org/articles/10.3389/fcimb.2018.00080/full
UR  - http://hdl.handle.net/10044/1/85848
VL  - 8
ER  -
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