The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA

BMC Microbiology

Research Article

David T Mulder¹  Sarah E Allison¹  Ana Victoria C Pilar¹  Brian K Coombes¹  Colin A Cooper² 

[1] Michael G. DeGroote Institute for Infectious Disease Research, L8N 3Z5, Hamilton, Ontario, Canada;Department of Biochemistry and Biomedical Sciences, McMaster University, Health Sciences Centre Room 4H17, L8S 4K1, Hamilton, Ontario, Canada;Michael G. DeGroote Institute for Infectious Disease Research, L8N 3Z5, Hamilton, Ontario, Canada;Department of Biochemistry and Biomedical Sciences, McMaster University, Health Sciences Centre Room 4H17, L8S 4K1, Hamilton, Ontario, Canada;Department of Molecular and Cellular Biology, University of Guelph, 488 Gordon Street, Science Complex, Room 4202, N1G 2W1, Guelph, Ontario, Canada;

关键词: Salmonella;    Pathogenesis;    Chaperone;    Translocon;    T3SS;   

DOI  :  10.1186/1471-2180-13-221

 received in 2013-06-04, accepted in 2013-10-01,  发布年份 2013

来源: Springer

【 摘 要 】

BackgroundSalmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever. This bacterium uses two type three secretion systems (T3SSs) to translocate protein effectors into host cells to manipulate cellular function. Salmonella pathogenicity island (SPI)-2 encodes a T3SS required for intracellular survival of the pathogen. Genes in SPI-2 include apparatus components, secreted effectors and chaperones that bind to secreted cargo to coordinate their release from the bacterial cell. Although the effector repertoire secreted by the SPI-2 T3SS is large, only three virulence-associated chaperones have been characterized.ResultsHere we report that SscA is the chaperone for the SseC translocon component. We show that SscA and SseC interact in bacterial cells and that deletion of sscA results in a loss of SseC secretion, which compromises intracellular replication and leads to a loss of competitive fitness in mice.ConclusionsThis work completes the characterization of the chaperone complement within SPI-2 and identifies SscA as the chaperone for the SseC translocon.

【 授权许可】

Unknown   
© Cooper et al.; licensee BioMed Central Ltd. 2013. This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.