HIV Gag polyprotein: processing and early viral particle assembly
Abstract
Over the past several decades, extensive research into the Gag polyprotein, the main structural protein of HIV-1 and all other retroviruses, has changed the way that we describe Gag's role within viral lifecycles. Initially thought of as a simple scaffold protein forming the viral core, Gag has demonstrated the ability to specifically recognize genomic RNA and both viral and host proteins as it traffics to the cell membrane. There, Gag forms higher ordered structures required for the correct assembly, budding, and maturation of new infectious particles.
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Concomitant with or after budding, activation of the viral protease leads to cleavage of Gag at specific positions, inducing major structural rearrangements of the individual Gag domains and a dramatic change in virus morphology.
“Concomitant with or after budding, activation of the viral protease leads to cleavage of Gag at specific positions, inducing major structural rearrangements of the individual Gag domains and a dramatic change in virus morphology”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [2]
Proteolytic cleavages catalysed by the viral protease lead to a spectacular structural rearrangement of the viral particle into a mature form that is competent to fuse with and infect a new cell.
“Subsequently, a series of proteolytic cleavages catalysed by the viral protease leads to a spectacular structural rearrangement of the viral particle into a mature form that is competent to fuse with and infect a new cell.”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [2]
Gag is indispensable for packaging of gRNA into the forming virus particle.
“The role of Gag is indispensable for the packaging of gRNA into the forming virus particle (Freed 1998, Bell and Lever 2013).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Bell and Lever 2013
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References 104 · Cited by 222
- Authors
- Bell, N. M., & Lever, A. M. L.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Lever, Andrew M.L.
- ORCID
- Lever, Andrew M.L.
- Venue
- Trends in Microbiology
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 21
- Issue
- 3
- Pages
- 136-144
- ISSN
- 0966-842X (ISSN-L)
- OpenAlex
- W1969836275
- Cited by
- 222
- References
- 104
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 9 · 2023: 20 · 2022: 17 · 2021: 11 · 2020: 27 · 2019: 19 · 2018: 24 · 2017: 11 · 2016: 19 · 2015: 17 · 2014: 14 · 2013: 11 · 2012: 1
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- HIV-1 Gag polyprotein, Gag processing, viral assembly, retroviral structural proteins, viral budding, virus maturation, viral life cycle
- MeSH terms
- Protein Binding, HIV-1, Gene Products, gag, Virus Assembly
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