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<p>Avian leukosis virus subgroup A (ALV-A) invades cells through the specific recognition of the cellular receptor Tva by its encoded surface glycoprotein gp85. Certain Fowl glioma-inducing virus (FGV) strains and their variants belong to ALV-A, but their gp85 proteins differ substantially from classical ALV-A strains. To identify the key residues in the gp85 of FGV-like ALV-A strain 2023ZW001 that determine Tva-binding affinity and infectivity, a strategy of substituting the corresponding gp85 residues between ALV-A 2023ZW001 and ALV-E ev-1 (which uses Tvb as its receptor) was adopted. A series of chimeric gp85 proteins for receptor binding assays were expressed, and multiple recombinant retroviral vectors RCASBP(ZW/ev-1)-EGFP/mCherry were constructed to transfect DF-1 cells for replication capacity analysis. The results showed that host range region 1 (hr1), host range region 2 (hr2), and variable region 3 (vr3) play a decisive role in mediating viral infection. Among these regions, residues 140–146 in hr1 and residues 267–273 in vr3 are the indispensable regions for 2023ZW001 to bind the receptor and mediate viral infection. Residues Y142, I143, and T146 in hr1; residues Q206, S215, and R228 in hr2; and as residues G267 and M268 in vr3 are the key sites determining Tva receptor binding and infectivity. This study indicated that hr1 and hr2 of the FGV-like ALV-A strain contain the major receptor interaction determinants, while vr3 also plays a key role in receptor-binding affinity and infectivity.</p>

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Residues Y142, I143, T146, Q206, S215, R228, G267, and M268 in the surface glycoprotein of FGV-like subgroup A avian leukosis virus are the key sites determining Tva receptor binding and infectivity

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年7月11日

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  • Jinqun Li,
  • Qi Li,
  • Yilin Yuan,
  • Biyue Dai,
  • Kangping Lu,
  • Hongyan Pan,
  • Ming Liao,
  • Weisheng Cao

摘要

Avian leukosis virus subgroup A (ALV-A) invades cells through the specific recognition of the cellular receptor Tva by its encoded surface glycoprotein gp85. Certain Fowl glioma-inducing virus (FGV) strains and their variants belong to ALV-A, but their gp85 proteins differ substantially from classical ALV-A strains. To identify the key residues in the gp85 of FGV-like ALV-A strain 2023ZW001 that determine Tva-binding affinity and infectivity, a strategy of substituting the corresponding gp85 residues between ALV-A 2023ZW001 and ALV-E ev-1 (which uses Tvb as its receptor) was adopted. A series of chimeric gp85 proteins for receptor binding assays were expressed, and multiple recombinant retroviral vectors RCASBP(ZW/ev-1)-EGFP/mCherry were constructed to transfect DF-1 cells for replication capacity analysis. The results showed that host range region 1 (hr1), host range region 2 (hr2), and variable region 3 (vr3) play a decisive role in mediating viral infection. Among these regions, residues 140–146 in hr1 and residues 267–273 in vr3 are the indispensable regions for 2023ZW001 to bind the receptor and mediate viral infection. Residues Y142, I143, and T146 in hr1; residues Q206, S215, and R228 in hr2; and as residues G267 and M268 in vr3 are the key sites determining Tva receptor binding and infectivity. This study indicated that hr1 and hr2 of the FGV-like ALV-A strain contain the major receptor interaction determinants, while vr3 also plays a key role in receptor-binding affinity and infectivity.