The HIV-1 Viral Protease Is Activated during Assembly and Budding Prior to Particle Release-Reference-Cited by-同舟云学术

The HIV-1 Viral Protease Is Activated during Assembly and Budding Prior to Particle Release

Published:2022-05-11 Issue:9 Volume:96 Page:
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Tabler Caroline O.¹²,Wegman Sarah J.¹,Chen Jiji³,Shroff Hari³⁴,Alhusaini Najwa¹,Tilton John C.¹^ORCID

Affiliation:

1. Center for Proteomics and Bioinformatics, Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio, USA

2. Department of Pathology, School of Medicine, Case Western Reserve University, Cleveland, Ohio, USA

3. Advanced Imaging and Microscopy Resource, National Institutes of Health, Bethesda, Maryland, USA

4. Laboratory of High Resolution Optical Imaging, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, Maryland, USA

Abstract

HIV-1 protease inhibitors have been a mainstay of antiretroviral therapy for more than 2 decades. Although antiretroviral therapy is effective at controlling HIV-1 replication, persistent reservoirs of latently infected cells quickly reestablish replication if therapy is halted.

Funder

HHS | NIH | National Institute of Allergy and Infectious Diseases

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jvi.02198-21

Reference59 articles.

1. Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease

2. Terminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 Protease

3. Cleavage of Human Immunodeficiency Virus Type 1 Proteinase from the N-Terminally Adjacent p6* Protein Is Essential for Efficient Gag Polyprotein Processing and Viral Infectivity

4. Importance of Protease Cleavage Sites within and Flanking Human Immunodeficiency Virus Type 1 Transframe Protein p6* for Spatiotemporal Regulation of Protease Activation

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