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刚地弓形虫的热休克蛋白

Heat shock proteins of Toxoplasma gondii.

作者信息

Lyons R E, Johnson A M

机构信息

Molecular Parasitology Unit, Faculty of Science, University of Technology, Sydney, Gore Hill, NSW, Australia.

出版信息

Parasite Immunol. 1995 Jul;17(7):353-9. doi: 10.1111/j.1365-3024.1995.tb00902.x.

Abstract

We have investigated heat shock protein (HSP) expression in mouse-virulent and -avirulent strains of Toxoplasma gondii by performing Western blot analysis using a monoclonal antibody against HSP65 of Mycobacterium bovis and a polyclonal antiserum against HSP70 of Plasmodium falciparum as primary antibodies. We initially observed that murine macrophages express HSP65 when infected with either virulent or avirulent strains, a result which contradicts previous reports. Differential HSP expression consistent which virulence was observed between strains, with high levels of a 70kDa HSP (HSP70) only detected in virulent strains in vivo. This protein was not observed in virulent strains in the immunocompromised mouse or in vitro, suggesting induction by immunological stress. This protein was only poorly expressed in avirulent strains. A 65kDa protein was observed in all strains in vivo and in vitro, suggesting a shared epitope with HSP70. These results are consistent with the hypothesis that the induced expression of HSP70 in virulent strains of T. gondii by immunological stresses may provide protection for these strains against cell damage associated with invasion of the host, allowing the virulent strains to persist as tachyzoites without the requirement for the encystation observed in avirulent strains.

摘要

我们通过使用抗牛分枝杆菌HSP65的单克隆抗体和抗恶性疟原虫HSP70的多克隆抗血清作为一抗进行蛋白质印迹分析,研究了小鼠强毒株和无毒株弓形虫中的热休克蛋白(HSP)表达情况。我们最初观察到,当用强毒株或无毒株感染时,鼠巨噬细胞会表达HSP65,这一结果与先前的报道相矛盾。在不同毒株之间观察到与毒力一致的HSP表达差异,仅在体内的强毒株中检测到高水平的70kDa HSP(HSP70)。在免疫受损小鼠体内的强毒株或体外培养的强毒株中均未观察到这种蛋白,提示其由免疫应激诱导产生。这种蛋白在无毒株中仅微弱表达。在体内和体外的所有毒株中均观察到一种65kDa的蛋白,提示其与HSP70有共同表位。这些结果与以下假设一致:免疫应激诱导弓形虫强毒株中HSP70的表达,可能为这些毒株提供保护,使其免受与宿主入侵相关的细胞损伤,从而使强毒株能够以速殖子形式持续存在,而无需像无毒株那样形成包囊。

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