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作 者:韩明远[1] 沈青春[1] 邹兴启[1] 宁宜宝[1]
出 处:《中国兽药杂志》2009年第1期37-42,共6页Chinese Journal of Veterinary Drug
摘 要:病毒蛋白糖基化较为常见,但糖基化的类型各不相同。病毒的糖基化蛋白具有识别宿主细胞,介导病毒囊膜与宿主细胞融合以及引起病毒免疫逃避现象等多种生物学特性。人类免疫缺陷病毒的GP41与猪呼吸与繁殖综合征病毒GP5蛋白上存在诱骗表位,诱骗表位抑制临近中和表位的识别。GP5蛋白膜外区上非中和表位A表位会降低临近中和表位B表位的免疫原性,使针对B表位中和抗体延缓产生。除了两个表位位置临近外,寡糖链对B表位的遮蔽或许是造成该现象的主要因素。本文就糖基化的类型,病毒糖基化蛋白的生物学特性以及与糖基化作用相关的猪繁殖与呼吸综合征病毒GP5蛋白诱骗表位进行了介绍以期阐明糖基化作用与免疫应答现象之间的联系。Many virus proteins are glycosylated, but the patterns of glycosylation are variable. Virus glycoprotein possesses many biological properties including recognition of host cell, mediating the fusion between cell membrane and virus envelope and immune evasion. Both the GP41 of human immunodeficiency virus and the GP5 of porcine reproductive and respiratory syndrome virus have decoy epitope which can suppress the recognition of nearby neutralizing epitopes. The nonneutralizing epitope A located in the ectodomain of PRRSV GP5 can decrease the immunogenicity of the nearby neutralizing epitope B and delay the induction of neutralizing antibody against epitope B. Besides their location, glyean - shielding on epitope B is perhaps the main factor for decoy. In order to illuminate the relationship between glycosylation and immune responses, this article provides an overview about the pattern of glycosylation, the biological properties of virus glycoprotein and the decoy epitope on GP5 of PRRSV related to the glycosylation.
关 键 词:糖基化作用 病毒糖基化蛋白 PRRSV GP5 诱骗表位
分 类 号:S852.4[农业科学—基础兽医学]
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