Asset Details
Do you wish to reserve the book?
Single Amino Acid Residue W33 of tva Receptor Is Critical for Viral Entry and High-Affinity Binding of Avian Leukosis Virus Subgroup K
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Single Amino Acid Residue W33 of tva Receptor Is Critical for Viral Entry and High-Affinity Binding of Avian Leukosis Virus Subgroup K
Do you wish to request the book?
Single Amino Acid Residue W33 of tva Receptor Is Critical for Viral Entry and High-Affinity Binding of Avian Leukosis Virus Subgroup K
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Single Amino Acid Residue W33 of tva Receptor Is Critical for Viral Entry and High-Affinity Binding of Avian Leukosis Virus Subgroup K
2025
Overview
Avian leukosis virus (ALV), the prototypical alpharetrovirus, causes tumorigenesis, immunosuppression, and wasting disease in poultry. The ALV genus is classified into ten subgroups, which differ in their host range, cell tropism, and receptor usage. The subgroups A, B, K, and J cause significant economic losses worldwide. The most recently discovered subgroup, ALV-K, which is now widespread in China, has been shown to use the tva cell receptor and share it with ALV-A. However, the specific amino acid residues crucial for ALV-K host cell entry remain unknown. Using precise tva expression and chimeric tva receptors, we further elucidated the significance of the cysteine-rich domain in mediating interactions with both ALV-A and ALV-K. Through a comprehensive analysis of mutated tva receptor variants, we pinpointed tryptophan at position 33 (W33) as a pivotal amino acid residue essential for ALV-K virus binding and entry. Of note is the finding that the substitution of W33 induced resistance to ALV-K while preserving sensitivity to ALV-A. This study not only represents an advance in the understanding of the specificity of the tva receptor for ALV-K, but also offers a biotechnological strategy for the prevention of ALV-K infections in poultry.
Publisher
MDPI AG,MDPI
Subject
