摘要
钙网蛋白(calreticulin, CRT)结构由凝集素结构域和臂结构域两部分组成,可以通过与不同蛋白互作,如C1q、ERp57、MHCⅠ类分子等,参与寄生虫免疫逃避、蛋白质折叠、抑制蛋白质聚集、抗原递呈以及凋亡细胞的吞噬等重要生命过程。目前,已有多种哺乳动物(人源和鼠源)和寄生虫(克氏锥虫和溶组织内阿米巴)钙网蛋白的部分结构域得到解析。本综述通过分析钙网蛋白相应功能的结构基础,为今后以钙网蛋白为靶点防治寄生虫病与蛋白质折叠相关疾病提供理论基础。
Calreticulin, consisting of lectin domain and arm domain, is involved in important life processes such as parasitic immune evasion, protein folding, inhibition of protein aggregation, antigen presentation and phagocytosis of apoptotic cells through interaction with multiple proteins including C1q, ERp57 and MHC I. So far, some domains of mammalian(Human and Mouse) and parasitic(Trypanosoma cruzi and Entamoeba histolytica) calreticulin have been determined. By elaborating the structural basis for corresponding functions of calreticulin, we provided new ideas for the prevention and treatment for diseases targeting calreticulin including parasitosis and protein folding-related diseases in the future.
作者
余文
贾智惠
诸欣平
YU WEN;JIA Zhi-hui;ZHU Xin-ping(Department of Medical Microbiology and Parasitology,School of Basic Medical Sciences,Capital Medical University,Beijing 100069,China)
出处
《中国病原生物学杂志》
CSCD
北大核心
2023年第1期117-120,125,共5页
Journal of Pathogen Biology
基金
北京市自然科学基金项目(No.7214213)。
