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人类盘尾丝虫病中的宿主-寄生虫相互作用:一种新型人类钙粒蛋白的鉴定与序列分析

Host-parasite interaction in human onchocerciasis: identification and sequence analysis of a novel human calgranulin.

作者信息

Marti T, Erttmann K D, Gallin M Y

机构信息

Department of Molecular Biology, Bernhard Nocht Insitute for Tropical Medicine, Hamburg, Germany.

出版信息

Biochem Biophys Res Commun. 1996 Apr 16;221(2):454-8. doi: 10.1006/bbrc.1996.0616.

Abstract

A novel S100 ca2+-binding protein, termed calgranulin-related protein (CGRP), was purified to homogeneity from extracts of adult Onchocerca volvulus, a human tissue-dwelling parasite. Its complete amino acid sequence was determined using microanalytical techniques. The primary structure of CGRP consists of 91 residues and displays identity with the recently reported partial sequence of an S100 protein present in human neutrophils. The human origin of CGRP is supported by the occurrence in O. volvulus extracts of additional human neutrophil proteins, including migration inhibitory factor-related protein 8 and defensins. The results suggest that these proteins interact with the worm surface following their release by activated neutrophils in the course of inflammatory reactions caused by O. volvulus infection.

摘要

一种名为钙粒蛋白相关蛋白(CGRP)的新型S100钙结合蛋白,从人体组织寄生寄生虫——成年盘尾丝虫的提取物中纯化至同质。使用微量分析技术确定了其完整的氨基酸序列。CGRP的一级结构由91个残基组成,与最近报道的人类中性粒细胞中存在的一种S100蛋白的部分序列具有同一性。盘尾丝虫提取物中存在包括迁移抑制因子相关蛋白8和防御素在内的其他人类中性粒细胞蛋白,支持了CGRP的人类起源。结果表明,这些蛋白在盘尾丝虫感染引起的炎症反应过程中被活化的中性粒细胞释放后,与虫体表面相互作用。

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