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<p>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 infection by affecting viral internalization, rather than attachment. The viral internalization efficiency was partially restored under a low pH environment. Incorporation of T32A and T271A into ALV-J led to significantly reduced replication capacity in vivo and viral shedding of the recombinant virus. These findings are valuable for our understanding of the roles of glycans in the ALV-J infection cycle, as well as for providing potential anti-ALV-J strategies.</p>

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Role of O-linked glycosylation modification on internalization and replication of avian leukosis virus subgroup J

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年2月16日

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  • Moru Xu,
  • Menglu Xu,
  • He Zhu,
  • Kun Qian,
  • Hongxia Shao,
  • Jinlin Huang,
  • Jianqiang Ye,
  • Aijian Qin

摘要

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 infection by affecting viral internalization, rather than attachment. The viral internalization efficiency was partially restored under a low pH environment. Incorporation of T32A and T271A into ALV-J led to significantly reduced replication capacity in vivo and viral shedding of the recombinant virus. These findings are valuable for our understanding of the roles of glycans in the ALV-J infection cycle, as well as for providing potential anti-ALV-J strategies.