溶组织内阿米巴半乳糖/ N - 乙酰半乳糖胺凝集素的结构与功能

Structure and function of the Entamoeba histolytica Gal/GalNAc lectin.

作者信息

Mann Barbara J

机构信息

Department of Internal Medicine and Microbiology, University of Virginia, Charlottesville 22908, USA.

出版信息

Int Rev Cytol. 2002;216:59-80. doi: 10.1016/s0074-7696(02)16003-7.

DOI:10.1016/s0074-7696(02)16003-7

PMID:12049210

Abstract

Gal/GalNAc lectin is a novel multifunctional virulence factor of the human parasite Entamoeba histolytica. The native protein is a 260-kDa heterodimer consisting of a type 1 membrane protein disulfide bonded to a lipid-anchored protein. Each subunit has several isoforms that may form functionally different heterodimers, analogous to the integrin family of proteins. Recently a second 150-kDa Gal/GalNAc lectin has been identified in E. histolytica that associates with the 260-kDa lectin. The functions of the 260-kDa lectin have been characterized using specific monoclonal antibodies. This lectin plays roles in many of the critical aspects of this parasite's pathogenicity including adherence, cytolysis, invasion, resistance to lysis by complement, and also perhaps encystment. Current knowledge regarding both the structure and function of this unique multifunctional virulence factor are discussed.

摘要

半乳糖/ N - 乙酰半乳糖胺凝集素是人类寄生虫溶组织内阿米巴的一种新型多功能毒力因子。天然蛋白是一种260 kDa的异二聚体，由一个通过二硫键与脂质锚定蛋白相连的1型膜蛋白组成。每个亚基都有几种亚型，它们可能形成功能不同的异二聚体，类似于整合素蛋白家族。最近，在溶组织内阿米巴中发现了第二种150 kDa的半乳糖/ N - 乙酰半乳糖胺凝集素，它与260 kDa的凝集素相关联。已使用特异性单克隆抗体对260 kDa凝集素的功能进行了表征。这种凝集素在该寄生虫致病性的许多关键方面发挥作用，包括黏附、细胞溶解、侵袭、对补体裂解的抗性，也许还包括包囊形成。本文讨论了关于这种独特的多功能毒力因子的结构和功能的当前知识。