Role of O-linked glycosylation modification on internalization and replication of avian leukosis virus subgroup J
Moru Xu, Menglu Xu, He Zhu, Kun Qian, Hongxia Shao, Jinlin Huang, Jianqiang Ye, Aijian Qin
TL;DR
This study shows how O-linked glycosylation affects the internalization and replication of ALV-J, an avian virus, and identifies key sites that could help develop anti-viral strategies.
Contribution
The first identification of O-linked glycosylation sites (T32 and T271) in ALV-J Env and their role in viral internalization and replication.
Findings
ALV-J replication is enhanced by GalNAc and core 1 β3-Gal-T in DF-1 cells.
Mutations in T32 or T271 reduce ALV-J infection by impairing internalization.
T32A and T271A mutations significantly lower ALV-J replication and viral shedding in vivo.
Abstract
Upon infection, viruses reprogram the host metabolic system to hijack metabolic resources for proliferation. Avian leukosis virus subgroup J (ALV-J), an avian oncogenic virus, poses significant challenges to the poultry industry. ALV-J infection upgrades monosaccharide N-acetylgalactosamine (GalNAc) and galactosyltransferase (core 1 β3-Gal-T) in DF-1 cells, both of which are crucial for O-linked glycosylation. Addition of GalNAc or overexpression of core 1 β3-Gal-T in DF-1 cells can promote ALV-J replication. ALV-J envelope protein (Env) undergoes complex post-translational modifications. Two O-linked glycosylation sites (T32 and T271) located in the head region of the ALV-J Env have been identified for the first time using liquid chromatography–mass spectrometry (LC–MS). The results of coimmunoprecipitation and flow cytometry indicate that mutations in T32 or T271 diminish ALV-J…
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Taxonomy
TopicsT-cell and Retrovirus Studies · Herpesvirus Infections and Treatments · Glycosylation and Glycoproteins Research