Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite
| Autor: | A Hörauf, Andreas Hübel, Joachim Clos, Sylvia Krobitsch |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Hot Temperature
Mutant Protozoan Proteins Virulence Leishmaniasis Cutaneous Mice Heat shock protein Animals Leishmania major Amastigote Molecular Biology Cells Cultured Heat-Shock Proteins Regulation of gene expression Recombination Genetic Mice Inbred BALB C biology Gene targeting Cell Biology Endopeptidase Clp biology.organism_classification Molecular biology Cell biology Gene Expression Regulation Gene Targeting Macrophages Peritoneal CLPB Research Article |
| Popis: | In Leishmania major a 100-kDa heat shock protein, Hsp100, is abundant in the intracellular amastigote stage which persists in the mammalian host. A replacement of both clpB alleles which encode Hsp100 does not affect promastigote viability under standard culture conditions but impairs thermotolerance in vitro. In experimental infections of BALB/c inbred mice, the lack of Hsp100 in the gene replacement mutants results in a markedly delayed lesion development compared with that in infections with wild-type L. major. Overexpression of exogenous clpB gene copies can partly restore virulence to the gene replacement mutants. Genetic-selection experiments also reveal a strong pressure for Hsp100 expression in the mammalian stage. This requirement for Hsp100 was also observed in in vitro infection experiments with mouse peritoneal macrophages. These experiments indicated a role for Hsp100 during the development from the promastigote to the amastigote stage. Our results suggest an important role for this parasite heat shock protein during the initial stages of a mammalian infection. |
| Databáze: | OpenAIRE |
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