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来自猬迭宫绦虫的应激蛋白释放是一种布雷菲德菌素A可抑制的过程:应激蛋白主动输出的证据。

Release of stress proteins from Mesocestoides corti is a brefeldin A-inhibitable process: evidence for active export of stress proteins.

作者信息

Ernani F P, Teale J M

机构信息

Department of Microbiology, University of Texas Health Science Center, San Antonio 78284-7758.

出版信息

Infect Immun. 1993 Jun;61(6):2596-601. doi: 10.1128/iai.61.6.2596-2601.1993.

Abstract

Substantial evidence indicates that molecules released by infectious organisms affect virulence and influence immunity to infection. The characterization of extracellular molecules and their mechanism of release is therefore critical to understanding host-parasite relationships. The cestode parasite Mesocestoides corti is known to release at the larval stage several molecules including the heat shock proteins hsp70 and hsp60. In this report, it is shown that several molecules released by M. corti, including 70- and 60-kDa proteins, are induced by a temperature shift from room temperature to 37 degrees C. Such a shift is comparable to the thermal stress of parasites transmitted from insect vector to vertebrate host. By drug inhibition studies and Western blot (immunoblot) analyses, it is shown that M. corti hsp70 and hsp60 as well as other released molecules are actively exported. The active release of stress proteins by parasites has not been described and may play a critical role in the disease process.

摘要

大量证据表明,感染性生物体释放的分子会影响毒力并影响对感染的免疫力。因此,细胞外分子的特性及其释放机制对于理解宿主与寄生虫的关系至关重要。已知绦虫寄生虫中殖孔绦虫在幼虫阶段会释放几种分子,包括热休克蛋白hsp70和hsp60。在本报告中,研究表明,中殖孔绦虫释放的几种分子,包括70 kDa和60 kDa的蛋白质,是由温度从室温转变为37摄氏度诱导产生的。这种转变类似于从昆虫媒介传播到脊椎动物宿主的寄生虫所经历的热应激。通过药物抑制研究和蛋白质印迹(免疫印迹)分析,结果表明中殖孔绦虫的hsp70和hsp60以及其他释放的分子是被主动输出的。寄生虫主动释放应激蛋白的情况尚未见报道,可能在疾病过程中起关键作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e7ef/280889/20c828875dfc/iai00018-0340-a.jpg

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