ArticleBMC microbiology2008
Functional characterization of a small heat shock protein from Mycobacterium leprae.
Article in BMC microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Mycobacterium leprae small heat shock protein-18 complements Lon protease in Escherichia coli.BMC microbiology · 2026Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Role of ATP-Small Heat Shock Protein Interaction in Human Diseases.Frontiers in molecular biosciences · 2022Review
- Small but mighty: a functional look at bacterial sHSPs.Cell stress & chaperones · 2020Review
- Characterization of rice small heat shock proteins targeted to different cellular organelles.Cell stress & chaperones · 2015Article
- Interaction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and function.PLoS neglected tropical diseases · 2015Article
- Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18.PloS one · 2015Article
- Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens.Microbiology (Reading, England) · 2009Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSmall heat shock proteins are ubiquitous family of stress proteins, having a role in virulence and survival of the pathogen. M. leprae, the causative agent of leprosy is an uncultivable organism in defined media, hence the biology and function of proteins were examined by cloning M. leprae genes in heterologous hosts. The study on sHsp18 was carried out as the knowledge about the functions of this major immunodominant antigen of M. leprae is scanty.
resultsThe gene encoding Mycobacterium leprae small heat shock protein (sHsp18) was amplified from biopsy material of leprosy patients, and cloned and expressed in E. coli. The localization and in vitro characterization of the protein are detailed in this report. Data show that major portion of the protein is localized in the outer membrane of E. coli. The purified sHsp18 functions as an efficient chaperone as shown by their ability to prevent thermal inactivation of restriction enzymes SmaI and NdeI. Physical interaction of the chaperone with target protein is also demonstrated. Size exclusion chromatography of purified protein shows that the protein can form multimeric complexes under in vitro conditions as is demonstrated for several small heat shock proteins.
conclusionThe small heat shock protein sHsp18 of M. leprae is a chaperone and shows several properties associated with other small heat shock proteins. Membrane association and in vitro chaperone function of sHsp18 shows that the protein may play a role in the virulence and survival of M. leprae in infected host.
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