KIF5B-mediated internalization of FMDV promotes virus infection.

Virol Sin

State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730000, China; Gansu Province Research Center for Basic Disciplines of Pathogen Biology, Lanzhou 730046, China. Electronic address:

Published: June 2024

AI Article Synopsis

  • Foot-and-mouth disease (FMD) is caused by the FMD virus (FMDV) and is economically significant, but the internalization process of the virus after infection is not well understood.
  • The study identifies kinesin family member 5B (KIF5B) as crucial for FMDV internalization, confirming its interaction with the virus's structural protein VP1 and emphasizing a specific domain in KIF5B that facilitates this interaction.
  • KIF5B enhances FMDV replication and aids in the virus's transport within the host cells by regulating clathrin uncoating and viral particle movement, suggesting it as a potential target for antiviral drug development.

Article Abstract

Foot-and-mouth disease (FMD) is a highly contagious and economically important disease, which is caused by the FMD virus (FMDV). Although the cell receptor for FMDV has been identified, the specific mechanism of FMDV internalization after infection remains unknown. In this study, we found that kinesin family member 5B (KIF5B) plays a vital role during FMDV internalization. Moreover, we confirmed the interaction between KIF5B and FMDV structural protein VP1 by co-immunoprecipitation (Co-IP) and co-localization in FMDV-infected cells. In particular, the stalk [amino acids (aa) 413-678] domain of KIF5B was indispensable for KIF5B-VP1 interaction. Moreover, overexpression of KIF5B dramatically enhanced FMDV replication; consistently, knockdown or knockout of KIF5B suppressed FMDV replication. Furthermore, we also demonstrated that KIF5B promotes the internalization of FMDV via regulating clathrin uncoating. KIF5B also promotes the transmission of viral particles to early and late endosomes during the early stages of infection. In conclusion, our results demonstrate that KIF5B promotes the internalization of FMDV via regulating clathrin uncoating and intracellular transport. This study may provide a new therapeutic target for developing FMDV antiviral drugs.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11279799PMC
http://dx.doi.org/10.1016/j.virs.2024.03.005DOI Listing

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