Next Article in Journal
SARS-CoV-2 Genomic Characteristics and Clinical Impact of SARS-CoV-2 Viral Diversity in Critically Ill COVID-19 Patients: A Prospective Multicenter Cohort Study
Next Article in Special Issue
Synthesis, Assembly and Processing of Viral Proteins
Previous Article in Journal
An Updated Review on SARS-CoV-2 Infection in Animals
 
 
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Editorial

Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example

by
Chih-Yen Lin
1,2,†,
Aspiro Nayim Urbina
2,†,
Wen-Hung Wang
2,3,
Arunee Thitithanyanont
4 and
Sheng-Fan Wang
1,2,5,*
1
Department of Medical Laboratory Science and Biotechnology, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
2
Center for Tropical Medicine and Infectious Disease, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
3
Division of Infectious Disease, Department of Internal Medicine, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
4
Department of Microbiology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
5
Department of Medical Research, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Viruses 2022, 14(7), 1528; https://doi.org/10.3390/v14071528
Submission received: 5 June 2022 / Revised: 2 July 2022 / Accepted: 6 July 2022 / Published: 13 July 2022
(This article belongs to the Special Issue Synthesis, Assembly and Processing of Viral Proteins)

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.
Keywords: assembly; budding; HIV-1; ESCRT; late domain; Alix; galectin-3 assembly; budding; HIV-1; ESCRT; late domain; Alix; galectin-3

Share and Cite

MDPI and ACS Style

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 2022, 14, 1528. https://doi.org/10.3390/v14071528

AMA Style

Lin C-Y, Urbina AN, 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. 2022; 14(7):1528. https://doi.org/10.3390/v14071528

Chicago/Turabian Style

Lin, Chih-Yen, Aspiro Nayim Urbina, Wen-Hung Wang, Arunee Thitithanyanont, and Sheng-Fan Wang. 2022. "Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example" Viruses 14, no. 7: 1528. https://doi.org/10.3390/v14071528

APA Style

Lin, C.-Y., Urbina, A. N., Wang, W.-H., Thitithanyanont, A., & Wang, S.-F. (2022). Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example. Viruses, 14(7), 1528. https://doi.org/10.3390/v14071528

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop