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

Author:

Zhang Yao1,Yu Mengmeng1,Xing Lixiao1,Liu Peng1,Chen Yuntong1,Chang Fangfang1,Wang Suyan1,Bao Yuanling1,Farooque Muhammad1,Li Xinyi1,Guan Xiaolu1,Liu Yongzhen1,Liu Aijing1,Qi Xiaole1,Pan Qing1,Zhang Yanping1,Gao Li1,Li Kai1,Liu Changjun1,Cui Hongyu1,Wang Xiaomei1,Gao Yulong1ORCID

Affiliation:

1. Avian Immunosuppressive Diseases Division, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, Harbin, People’s Republic of China

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.

Funder

National Natural Science Foundation of China

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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