Cited by 717HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

HIV-1 Gag proteins: diverse functions in the virus life cycle

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Freed, Eric O.·1998·Virology

Abstract

The Gag proteins of HIV-1, like those of other retroviruses, are necessary and sufficient for the assembly of virus-like particles. The roles played by HIV-1 Gag proteins during the life cycle are numerous and complex, involving not only assembly but also virion maturation after particle release and early postentry steps in virus replication. As the individual Gag domains carry out their diverse functions, they must engage in interactions with themselves, other Gag proteins, other viral proteins, lipid, nucleic acid (DNA and RNA), and host cell proteins. This review briefly summarizes our current understanding of how HIV-1 Gag proteins function in the virus life cycle.

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Crossref · 10.1006/viro.1998.9398

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  • The MA domain remains associated with the inner face of the viral membrane and plays a crucial role in directing Gag or the viral core to the plasma membrane and incorporating the envelope during virus assembly.

    “The MA domain remains associated with the inner face of the viral membrane and plays a crucial role in directing Gag or the viral core to the plasma membrane and incorporating the envelope during virus assembly”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Freed 1998

    The “Membrane binding and Gag targeting” section says MA directs Gag binding and assembly at the plasma membrane, and the “Env glycoprotein incorporation” section reports that MA mutations can block Env incorporation (page numbers unavailable). The copy does not say MA directs the viral core to the plasma membrane. It also qualifies the claim that MA remains membrane-associated: a subset may dissociate from the lipid bilayer and associate with the core. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • 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).”

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Research works printed but not linked: 1

  1. Myers, G., Wain-Hobson, S., Korber, B., Smith, R. F., Pavlakas, G. N. (Eds.) (1993). ``Human Retroviruses and AIDS: A Compilation and Analysis of Nucleic Acid and Amino Acid Sequences.'' Los Alamos National Laboratory, Los Alamos, NM.

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Authors
Freed, E. O.
Affiliations
National Institutes of Health (US)
Corresponding author
Freed, Eric O.
Venue
Virology
Publisher
Elsevier BV
Published
1998-11
Volume
251
Issue
1
Pages
1-15
ISSN
0042-6822 (ISSN-L)
OpenAlex
W1993452562
Cited by
717
References
163
Citations by year
2026: 6 · 2025: 13 · 2024: 9 · 2023: 8 · 2022: 7 · 2021: 15 · 2020: 14 · 2019: 13 · 2018: 19 · 2017: 16 · 2016: 18 · 2015: 33 · 2014: 22 · 2013: 25 · 2012: 37
FWCI
6.52
Type
journal article
Language
en
Open access
Locations
  • Virology (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 protein, viral assembly, virus-like particles, virion maturation, protein-protein interaction, host-virus interaction
MeSH terms
Amino Acid Sequence, Capsid, Molecular Sequence Data, Transcription, Genetic, Viral Proteins, HIV Antigens, HIV-1, Gene Products, gag, Gene Products, env, Virus Assembly, Nucleocapsid, Anti-HIV Agents, gag Gene Products, Human Immunodeficiency Virus

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