The Bipartite Sequence Motif in the N and C Termini of gp85 of Subgroup J Avian Leukosis Virus Plays a Crucial Role in Receptor Binding and Viral Entry
Yao Zhang, Mengmeng Yu, Lixiao Xing, Peng Liu, Yuntong Chen, Fangfang Chang, Suyan Wang, Yuanling Bao, Muhammad Farooque, Xinyi Li, Xiaolu Guan, Yongzhen Liu, Aijing Liu, Xiaole Qi, Qing Pan, Yanping Zhang, Li Gao, Kai Li, Changjun Liu, Hongyu Cui, Xiaomei Wang, Yulong Gao
Abstract
Infection of a cell by retroviruses requires the attachment and fusion of the host and viral membranes. The specific adsorption of envelope (Env) surface proteins to cell receptors is a key step in triggering infections and has been the target of antiviral drug screening. ALV-J is an economically important avian pathogen that belongs to the genus Alpharetrovirus and has a wider host range than other ALV subgroups. Our results showed that the amino acids 38 to 131 of the N terminus and 159 to 283 of the C terminus of ALV-J gp85 controlled the efficiency of gp85 binding to chNHE1 and were critical for viral infection. In addition, the glycosylation sites (N6 and N11) and cysteines (C3 and C9) of gp85 played a crucial role in the receptor binding and viral entry. These findings might help elucidate the mechanism of the entry of ALV-J into host cells and provide antiviral targets for the control of ALV-J.