한빛사논문
Soomin Choi1,5, Eunna Choi1,5, Yong-Joon Cho2,5, Daesil Nam3, Jangwoo Lee4 & Eun-Jin Lee1,*
1 Department of Life Sciences, College of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea. 2 Korea Polar Research Institute, Incheon 21990, South Korea. 3 Division of Microbiology, Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 16419, South Korea. 4 Department of Genetic Engineering and Graduate School of Biotechnology, College of Life Sciences, Kyung Hee University, Yongin 17104, South Korea. 5These authors contributed equally: Soomin Choi, Eunna Choi, Yong-Joon Cho.
*Correspondence and requests for materials should be addressed to E.-J.L.
Abstract
The MgtC virulence protein from the intracellular pathogen Salmonella enterica is required for its intramacrophage survival and virulence in mice and this requirement of MgtC is conserved in several intracellular pathogens including Mycobacterium tuberculosis. Despite its critical role in survival within macrophages, only a few molecular targets of the MgtC protein have been identified. Here, we report that MgtC targets PhoR histidine kinase and activates phosphate transport independently of the available phosphate concentration. A single amino acid substitution in PhoR prevents its binding to MgtC, thus abrogating MgtC-mediated phosphate transport. Surprisingly, the removal of MgtC’s effect on the ability to transport phosphate renders Salmonella hypervirulent and decreases a non-replicating population inside macrophages, indicating that MgtC-mediated phosphate transport is required for normal Salmonella pathogenesis. This provides an example of a virulence protein directly activating a pathogen’s phosphate transport inside host.
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