POSTASSEMBLY CLEAVAGE OF A RETROVIRAL GLYCOPROTEIN CYTOPLASMIC DOMAIN REMOVES A NECESSARY INCORPORATION SIGNAL AND ACTIVATES FUSION ACTIVITY
POSTASSEMBLY CLEAVAGE OF A RETROVIRAL GLYCOPROTEIN CYTOPLASMIC DOMAIN REMOVES A NECESSARY INCORPORATION SIGNAL AND ACTIVATES FUSION ACTIVITY
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DOI：
10.1128/jvi.68.7.4620-4627.1994
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发表时间：
1994-07-01
影响因子：
5.4
通讯作者：
HUNTER, E
中科院分区：
文献类型：
--
作者：
BRODY, BA;RHEE, SS;HUNTER, E
D型逆转录病毒Mason-Pfizer猴病毒的跨膜（TM）糖蛋白的胞质结构域内的病毒蛋白酶介导的切割从蛋白质的羧基末端去除约16个氨基酸。为了确定这种切割在病毒生命周期中的功能意义，我们将提前终止密码子引入TM编码结构域，从而产生截短的糖蛋白。逐步截断的胞质结构域确定的羧基末端的第三个作为所需的糖蛋白复合物的有效掺入到出芽的病毒粒子，并大大增加了融合能力的TM糖蛋白。这些结果，以及基质蛋白突变抑制TM切割的能力，意味着这部分糖蛋白在出芽过程中与衣壳蛋白特异性相互作用，抑制糖蛋白融合功能，直到病毒成熟。
Viral protease-mediated cleavage within the cytoplasmic domain of the transmembrane (TM) glycoprotein of the type D retrovirus, Mason-Pfizer monkey virus, removes approximately 16 amino acids from the carboxy terminus of the protein. To determine the functional significance of this cleavage in the virus life cycle, we introduced premature stop codons into the TM coding domain, resulting in the production of truncated glycoproteins. Progressive truncation of the cytoplasmic domain identified the carboxy-terminal third as being required for efficient incorporation of the glycoprotein complex into budding virions and profoundly increased the fusogenic capability of the TM glycoprotein. These results, together with the ability of matrix protein mutations to suppress TM cleavage, imply that this portion of the glycoprotein interacts specifically with the capsid proteins during budding, suppressing glycoprotein fusion function until virus maturation has occurred.