1887

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Volume 62, Issue 7

Protective role of small heat-shock protein in heterologous hosts, and , grown under stress Free

Abstract

The aim of this study is to examine the role of a small heat-shock protein (sHsp18) from in the survival of heterologous recombinant hosts carrying the gene encoding this protein under different environmental conditions that are normally encountered by during its infection of the human host. Using an system where expression is controlled by its native promoter, we show that expression of is induced under low oxygen tension, nutrient depletion and oxidative stress, all of which reflect the natural internal environment of the granulomas where the pathogen resides for long periods. We demonstrate the chaperone activity of sHsp18 through its ability to confer survival advantage to recombinant at heat-shock temperatures. Additional evidence for the protective role of sHsp18 was obtained when harbouring a copy of was found to multiply better in human macrophages. Furthermore, the autokinase activity of sHsp18 protein demonstrated for what is believed to be the first time in this study implies that some of the functions of sHsp18 might be controlled by the phosphorylation state of this protein. Results from this study suggest that might be one of the factors that facilitate the survival and persistence of under stress and autophosphorylation of sHsp18 protein could be a mechanism used by this protein to sense changes in the external environment.

  • Received:
  • Accepted:
  • Published Online:
© 2013 SGM
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2013-07-01
2024-04-20
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Protective role of Mycobacterium leprae small heat-shock protein in heterologous hosts, Escherichia coli and Mycobacterium smegmatis, grown under stress
J. Med. Microbiol. 62, 959 (2013); https://doi.org/10.1099/jmm.0.057851-0
/content/journal/jmm/10.1099/jmm.0.057851-0
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