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HIV-1 assembly, release and maturation

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Freed, Eric O.·2015·Nature Reviews Microbiology
DOI 10.1038/nrmicro3490PMC PMC6936268
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Abstract

Major advances have occurred in recent years in our understanding of HIV-1 assembly, release and maturation, as work in this field has been propelled forwards by developments in imaging technology, structural biology, and cell and molecular biology. This increase in basic knowledge is being applied to the development of novel inhibitors designed to target various aspects of virus assembly and maturation. This Review highlights recent progress in elucidating the late stages of the HIV-1 replication cycle and the related interplay between virology, cell and molecular biology, and drug discovery.

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  • The primary region responsible for Gag multimerization is the C-terminal part of the CA domain.

    “The primary region responsible for Gag multimerization is the C-terminal part of the CA domain”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Freed 2015

    The ‘Gag protein: structure and function’ section says the C-terminal CA domain contains a dimer interface that plays an important part in Gag multimerization. The ‘Gag assembly’ section calls CA as a whole the main viral determinant, but the copy does not identify its C-terminal part as the primary region. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • Basic residues within the NC domain play a crucial role in Gag multimerization, which is mediated by the interaction domain (I-domain).

    “basic residues within the NC domain are believed to play a crucial role in Gag multimerization, which is mediated by the interaction domain (I-domain)”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Freed 2015

    In “RNA encapsidation” (page not supplied), the paper says basic residues increase NC’s affinity for RNA and that NC–RNA interactions help drive Gag multimerization. It does not identify an interaction domain (I-domain) as the mediator or directly assign the crucial multimerization role to those residues. “Gag assembly” instead identifies CA as the main viral determinant driving multimerization. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Once a retrovirus completes its assembly, it buds off as an immature, noninfectious virion containing viral components as large polyproteins, primarily Gag and Gag-Pol (such as MLV and HIV-1) assembling at the plasma membrane, and Gag, Gag-Pro, and Gag-Pro-Pol (such as MPMV and MMTV), preassembling in the cytoplasm.

    “Once a retrovirus completes its assembly, it buds off as an immature, noninfectious virion containing viral components as large polyproteins, primarily Gag and Gag–Pol (such as MLV and HIV-1) assembling at the plasma membrane (Fig. 5), and Gag, Gag–Pro, and Gag–Pro–Pol (such as MPMV and MMTV), preassembling in the cytoplasm”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Freed 2015

    Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.

    Experimental — accuracy not yet measured

  • L domains are short, 4-6 amino acid domains that act like cellular adaptor proteins, ensuring membrane scission and virion separation from host cell membranes.

    “These short, 4–6 amino acid domains act like cellular adaptor proteins, ensuring membrane scission and virion separation from the host cell membranes”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Freed 2015

    In “Gag protein: structure and function” (page unavailable), the paper calls p6 an adaptor for host ESCRT machinery. In “Virion release” (page unavailable), it identifies late domains as short motifs that drive virus release by engaging cellular proteins, while attributing membrane scission to ESCRT machinery. The listed motifs are four amino acids long; our copy does not establish the claimed 4–6-amino-acid range. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • Initially inactive, the retroviral PR undergoes autocatalytic activation upon budding, triggering a cascade of cleavage events that cleaves the Gag precursor polyprotein into the three main structural proteins, MA, CA, and NC.

    “Initially inactive, the retroviral PR undergoes an autocatalytic activation upon budding, triggering a cascade of cleavage events that cleaves the Gag precursor polyprotein into the three main structural proteins, MA, CA, and NC”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Freed 2015

    The ‘Virus maturation’ section says that HIV-1 protease cleaves Gag during release in an ordered, stepwise cascade, and ‘Gag protein: structure and function’ identifies MA, CA and NC among the mature products. Our copy does not say that protease is initially inactive or undergoes autocatalytic activation upon budding; it also names p6 as another mature Gag product. No page numbers are available in the indexed passages. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Cites

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Authors
Freed, E. O.
Affiliations
National Cancer Institute (US)
Corresponding author
Freed, Eric O.
ORCID
Freed, Eric O.
Venue
Nature Reviews Microbiology
Publisher
Springer Science and Business Media LLC
Published
2015-06-29
Volume
13
Issue
8
Pages
484-496
ISSN
  • 1740-1526 (ISSN-L)
  • 1740-1534
DOI
10.1038/nrmicro3490
PMC
PMC6936268
OpenAlex
W1823429634
Cited by
654
References
13
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FWCI
8.19
Type
journal article
Language
en
Open access
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature Reviews Microbiology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Cancer Institute (ZIABC010776, ZIABC010775, ZIABC010778)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords
HIV-1, viral assembly, virus release, virus maturation, Gag protein, HIV-1 replication, maturation inhibitors
MeSH terms
Humans, Viral Proteins, Virus Replication, HIV-1, Gene Expression Regulation, Viral, Virus Assembly, Virus Release

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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