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100 kD热休克蛋白在杜氏利什曼原虫中的新作用。

A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani.

作者信息

Krobitsch S, Clos J

机构信息

Leishmania Unit, Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.

出版信息

Cell Stress Chaperones. 1999 Sep;4(3):191-8. doi: 10.1379/1466-1268(1999)004<0191:anrfkh>2.3.co;2.

Abstract

Heat shock proteins of the 100 kD family have been known to confer general stress tolerance in yeast and plants. Several protozoan parasites possess genes for Hsp100 proteins. In Leishmania species the protein is expressed under heat stress and during the mammalian stage, the amastigote. We show here that replacement of the clpB gene which encodes Hsp100 does not affect thermotolerance or general viability in Leishmania donovani insect stages (promastigotes) nor in axenically cultured mammalian stages (amastigotes). However, its expression is required for normal development of the parasite inside mammalian host cells. Hsp100 appears to function as an antagonist of amastigote-to-promastigote differentiation and a promoter of full amastigote development.

摘要

已知100 kD家族的热休克蛋白可赋予酵母和植物普遍的胁迫耐受性。几种原生动物寄生虫拥有Hsp100蛋白的基因。在利什曼原虫属物种中,该蛋白在热应激下以及在哺乳动物阶段(无鞭毛体)表达。我们在此表明,编码Hsp100的clpB基因的替换并不影响杜氏利什曼原虫昆虫阶段(前鞭毛体)或无菌培养的哺乳动物阶段(无鞭毛体)的耐热性或总体生存能力。然而,其表达是寄生虫在哺乳动物宿主细胞内正常发育所必需的。Hsp100似乎起到无鞭毛体向前鞭毛体分化的拮抗剂和完全无鞭毛体发育的促进剂的作用。

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