Please use this identifier to cite or link to this item: https://doi.org/10.1099/mic.0.021865-0
Title: Investigation of EscA as a chaperone for the Edwardsiella tarda type III secretion system putative translocon component EseC
Authors: Wang, B.
Mo, Z.L.
Mao, Y.X.
Zou, Y.X.
Xiao, P.
Li, J.
Yang, J.Y.
Ye, X.H.
Leung, K.Y. 
Zhang, P.J.
Issue Date: 2009
Citation: Wang, B., Mo, Z.L., Mao, Y.X., Zou, Y.X., Xiao, P., Li, J., Yang, J.Y., Ye, X.H., Leung, K.Y., Zhang, P.J. (2009). Investigation of EscA as a chaperone for the Edwardsiella tarda type III secretion system putative translocon component EseC. Microbiology 155 (4) : 1260-1271. ScholarBank@NUS Repository. https://doi.org/10.1099/mic.0.021865-0
Abstract: Edwardsiella tarda is an important Gram-negative enteric pathogen affecting both animals and humans. It possesses a type III secretion system (T3SS) essential for pathogenesis. EseB, EseC and EseD have been shown to form a translocon complex after secretion, while EscC functions as a T3SS chaperone for EseB and EseD. In this paper we identify EscA, a protein required for accumulation and proper secretion of another translocon component, EseC. The escA gene is located upstream of eseC and the EscA protein has the characteristics of T3SS chaperones. Cell fractionation experiments indicated that EscA is located in the cytoplasm and on the cytoplasmic membrane. Mutation with in-frame deletion of escA greatly decreased the secretion of EseC, while complementation of escA restored the wild-type secretion phenotype. The stabilization and accumulation of EseC in the cytoplasm were also affected in the absence of EscA. Mutation of escA did not affect the transcription of eseC but reduced the accumulation level of EseC as measured by using an EseC-LacZ fusion protein in Ed. tarda. Co-purification and co-immunoprecipitation studies demonstrated a specific interaction between EscA and EseC. Further analysis showed that residues 31-137 of EseC are required for EseC-EscA interaction. Mutation of EseC residues 31-137 reduced the secretion and accumulation of EseC in Ed. tarda. Finally, infection experiments showed that mutations of EscA and residues 31-137 of EseC increased the LD50 by approximately 10-fold in blue gourami fish. These results indicated that EscA functions as a specific chaperone for EseC and contributes to the virulence of Ed. tarda. © 2009 SGM.
Source Title: Microbiology
URI: http://scholarbank.nus.edu.sg/handle/10635/100970
ISSN: 13500872
DOI: 10.1099/mic.0.021865-0
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

18
checked on Oct 18, 2018

WEB OF SCIENCETM
Citations

19
checked on Oct 2, 2018

Page view(s)

35
checked on Oct 19, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.