High-temperature protein G is an essential virulence factor of Leptospira interrogans

Amy McKarral King, Gabriela Pretre, Thanatchaporn Bartpho, Rasana Sermswan, Claudia Toma, Toshihiko Suzuki, Azad Eshghi, Mathieu Picardeau, Ben Adler, Gerald Laurence Murray

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30 Citations (Scopus)

Abstract

Leptospira interrogans is a global zoonotic pathogen and is the causative agent of leptospirosis, an endemic disease of humans and animals worldwide. There is limited understanding of leptospiral pathogenesis; therefore, further elucidation of the mechanisms involved would aid in vaccine development and the prevention of infection. HtpG (high-temperature protein G) is the bacterial homolog to the highly conserved molecular chaperone Hsp90 and is important in the stress responses of many bacteria. The specific role of HtpG, especially in bacterial pathogenesis, remains largely unknown. Through the use of an L. interrogans htpG transposon insertion mutant, this study demonstrates that L. interrogans HtpG is essential for virulence in the hamster model of acute leptospirosis. Complementation of the htpG mutant completely restored virulence. Surprisingly, the htpG mutant did not appear to show sensitivity to heat or oxidative stress, phenotypes common in htpG mutants in other bacterial species. Furthermore, the mutant did not show increased sensitivity to serum complement, reduced survival within macrophages, or altered protein or lipopolysaccharide expression. The underlying cause for attenuation thus remains unknown, but HtpG is a novel leptospiral virulence factor and one of only a very small number identified to date.
Original languageEnglish
Pages (from-to)1123 - 1131
Number of pages9
JournalInfection and Immunity
Volume82
Issue number3
DOIs
Publication statusPublished - 2014

Cite this

King, A. M., Pretre, G., Bartpho, T., Sermswan, R., Toma, C., Suzuki, T., Eshghi, A., Picardeau, M., Adler, B., & Murray, G. L. (2014). High-temperature protein G is an essential virulence factor of Leptospira interrogans. Infection and Immunity, 82(3), 1123 - 1131. https://doi.org/10.1128/IAI.01546-13