Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example
Issued Date
2022-07-01
Resource Type
eISSN
19994915
Scopus ID
2-s2.0-85135112600
Pubmed ID
35891508
Journal Title
Viruses
Volume
14
Issue
7
Rights Holder(s)
SCOPUS
Bibliographic Citation
Viruses Vol.14 No.7 (2022)
Suggested Citation
Lin C.Y., Urbina A.N., Wang W.H., Thitithanyanont A., Wang S.F. Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example. Viruses Vol.14 No.7 (2022). doi:10.3390/v14071528 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/85745
Title
Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example
Author(s)
Other Contributor(s)
Abstract
Viral assembly and budding are the final steps and key determinants of the virus life cycle and are regulated by virus–host interaction. Several viruses are known to use their late assembly (L) domains to hijack host machinery and cellular adaptors to be used for the requirement of virus replication. The L domains are highly conserved short sequences whose mutation or deletion may lead to the accumulation of immature virions at the plasma membrane. The L domains were firstly identified within retroviral Gag polyprotein and later detected in structural proteins of many other enveloped RNA viruses. Here, we used HIV-1 as an example to describe how the HIV-1 virus hijacks ESCRT membrane fission machinery to facilitate virion assembly and release. We also introduce galectin-3, a chimera type of the galectin family that is up-regulated by HIV-1 during infection and further used to promote HIV-1 assembly and budding via the stabilization of Alix–Gag interaction. It is worth further dissecting the details and finetuning the regulatory mechanism, as well as identifying novel candidates involved in this final step of replication cycle.