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一种疟疾裂殖子表面蛋白(MSP1)——结构、加工与功能

A malaria merozoite surface protein (MSP1)-structure, processing and function.

作者信息

Holder A A, Blackman M J, Burghaus P A, Chappel J A, Ling I T, McCallum-Deighton N, Shai S

机构信息

National Institute for Medical Research, Division of Parasitology, London, U.K.

出版信息

Mem Inst Oswaldo Cruz. 1992;87 Suppl 3:37-42. doi: 10.1590/s0074-02761992000700004.

Abstract

Merozoite surface protein-1 (MSP-1, also referred to as P195, PMMSA or MSA 1) is one of the most studied of all malaria proteins. The protein is found in all malaria species investigated and structural studies on the gene indicate that parts of the molecule are well-conserved. Studies on Plasmodium falciparum have shown that the protein is in a processed form on the merozoite surface, a result of proteolytic cleavage of the large precursor molecule. Recent studies have identified some of these cleavage sites. During invasion of the new red cell most of the MSP1 molecule is shed from the parasite surface except for a small C-terminal fragment which can be detected in ring stages. Analysis of the structure of this fragment suggests that it contains two growth factor-like domains that may have a functional role.

摘要

裂殖子表面蛋白-1(MSP-1,也称为P195、PMMSA或MSA 1)是所有疟疾蛋白中研究最多的蛋白之一。在所有已研究的疟原虫物种中均发现了该蛋白,对该基因的结构研究表明,分子的某些部分高度保守。对恶性疟原虫的研究表明,该蛋白在裂殖子表面呈加工后的形式,这是大的前体分子经蛋白水解切割后的结果。最近的研究已确定了其中一些切割位点。在入侵新的红细胞过程中,大多数MSP1分子从寄生虫表面脱落,除了在环状体期可检测到的一个小的C末端片段。对该片段结构的分析表明,它含有两个可能具有功能作用的生长因子样结构域。

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