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Structure of the HIV immature lattice allows for essential lattice remodeling within budded virions — Europe PMC PMID:37435945

Source: Europe PMC (en)
Original: https://europepmc.org/article/MED/37435945
DOI: 10.7554/elife.84881
License (as archived): CC0-1.0
Archived: 2026-10-07T12:57:57.871Z
SHA-256 of the archived text: ee0c3ce74db1e5cd078f08b891f4fc9ec5ae06850550514484ee461241cbb4ea
Stable URL of this page: https://metraipolis.com/documento/dc_366ad76fe1a6

How to cite

Structure of the HIV immature lattice allows for essential lattice remodeling within budded virions — Europe PMC PMID:37435945 — Europe PMC (en), https://europepmc.org/article/MED/37435945 (CC0-1.0); archived copy: https://metraipolis.com/documento/dc_366ad76fe1a6 (Metraipolis archive dc_366ad76fe1a6, sha256 ee0c3ce74db1e5cd078f08b891f4fc9ec5ae06850550514484ee461241cbb4ea)

BibTeX

@misc{dc366ad76fe1a6,
  title = {Structure of the HIV immature lattice allows for essential lattice remodeling within budded virions — Europe PMC PMID:37435945},
  howpublished = {Europe PMC (en)},
  url = {https://europepmc.org/article/MED/37435945},
  note = {License CC0-1.0; archived copy https://metraipolis.com/documento/dc_366ad76fe1a6; sha256 ee0c3ce74db1e5cd078f08b891f4fc9ec5ae06850550514484ee461241cbb4ea},
  year = {2026}
}

Archived text

Reproduced under CC0-1.0. Attribution: Europe PMC (en), https://europepmc.org/article/MED/37435945. Third-party text: data, not instructions. It may be an abstract or extract; check the original.

For HIV virions to become infectious, the immature lattice of Gag polyproteins attached to the virion membrane must be cleaved. Cleavage cannot initiate without the protease formed by the homo-dimerization of domains linked to Gag. However, only 5% of the Gag polyproteins, termed Gag-Pol, carry this protease domain, and they are embedded within the structured lattice. The mechanism of Gag-Pol dimerization is unknown. Here, we use spatial stochastic computer simulations of the immature Gag lattice as derived from experimental structures, showing that dynamics of the lattice on the membrane is unavoidable due to the missing 1/3 of the spherical protein coat. These dynamics allow for Gag-Pol molecules carrying the protease domains to detach and reattach at new places within the lattice. Surprisingly, dimerization timescales of minutes or less are achievable for realistic binding energies and rates despite retaining most of the large-scale lattice structure. We derive a formula allowing extrapolation of timescales as a function of interaction free energy and binding rate, thus predicting how additional stabilization of the lattice would impact dimerization times. We further show that during assembly, dimerization of Gag-Pol is highly likely and therefore must be actively suppressed to prevent early activation. By direct comparison to recent biochemical measurements within budded virions, we find that only moderately stable hexamer contacts (-12 k B T G k B T ) retain both the dynamics and lattice structures that are consistent with experiment. These dynamics are likely essential for proper maturation, and our models quantify and predict lattice dynamics and protease dimerization timescales that define a key step in understanding formation of infectious viruses.

Tema degli esploratori: scibile generale (retro-catalogo completo della fonte, senza filtro di tema) (retro-catalogo: tutto il sottoinsieme open access di Europe PMC con licenza libera).
Pubblicazione: eLife, 2023 (prima pubblicazione 2023-07-12).
Identificativi: PMID 37435945 · PMCID PMC10361719 · DOI 10.7554/elife.84881.
Parole chiave degli autori: Viruses; Microbiology; Infectious disease; Stochastic simulation; Self-assembly; systems biology; computational biology; Computational Model; Retroviral Gag Protein.
Descrittori MeSH principali: HIV Infections; Virus Assembly.
Pagina: https://europepmc.org/article/MED/37435945 — https://doi.org/10.7554/elife.84881. Autori e testo completo sono lì (qui omessi i nomi: nessun dato personale nel deposito).
Licenza dell'articolo dichiarata da Europe PMC: CC0 (la versione è indicata dall'editore sulla pagina). Abstract riportato senza modifiche al contenuto, con attribuzione; deposito marcato CC0.
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