Residues L55 and W69 of Tva Mediate Entry of Subgroup A Avian Leukosis Virus

Chen, Yuntong; Wang, Suyan; Yu, Mengmeng; Liu, Peng; Meng, Lingzhai; Guo, Ru; Feng, Xiaoyan; Liu, Aijing; Qi, Xiaole; Li, Kai; Gao, Li; Pan, Qing; Zhang, Yanping; Liu, Changjun; Cui, Hongyu; Wang, Xiaomei; Gao, Yulong

doi:10.1128/jvi.00678-22

Cited by 3 publications

(1 citation statement)

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“…This expanded the binding interface of gp85 with TM-chECL1 and resulted in a decrease in the binding free energies (by 300 kJ/mol). This phenomenon has also been observed in the binding of ALV-A [ 52 ] and SARS-CoV-2 [ 53 ] to their respective receptors. Thus, it is plausible that the N123I mutation could increase the binding capacity of gp85 to the chNHE1 receptor by strengthening the structure of the stability of the gp85 protein, expanding the docking surface, and reducing binding free energies.…”

Section: Discussionmentioning

confidence: 60%

N123I mutation in the ALV-J receptor-binding domain region enhances viral replication ability by increasing the binding affinity with chNHE1

Yu,

Zhang,

Zhang

et al. 2024

PLoS Pathog

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The subgroup J avian leukosis virus (ALV-J), a retrovirus, uses its gp85 protein to bind to the receptor, the chicken sodium hydrogen exchanger isoform 1 (chNHE1), facilitating viral invasion. ALV-J is the main epidemic subgroup and shows noteworthy mutations within the receptor-binding domain (RBD) region of gp85, especially in ALV-J layer strains in China. However, the implications of these mutations on viral replication and transmission remain elusive. In this study, the ALV-J layer strain JL08CH3-1 exhibited a more robust replication ability than the prototype strain HPRS103, which is related to variations in the gp85 protein. Notably, the gp85 of JL08CH3-1 demonstrated a heightened binding capacity to chNHE1 compared to HPRS103-gp85 binding. Furthermore, we showed that the specific N123I mutation within gp85 contributed to the enhanced binding capacity of the gp85 protein to chNHE1. Structural analysis indicated that the N123I mutation primarily enhanced the stability of gp85, expanded the interaction interface, and increased the number of hydrogen bonds at the interaction interface to increase the binding capacity between gp85 and chNHE1. We found that the N123I mutation not only improved the viral replication ability of ALV-J but also promoted viral shedding in vivo. These comprehensive data underscore the notion that the N123I mutation increases receptor binding and intensifies viral replication.

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Section: Discussionmentioning

confidence: 60%