Cited by 74HIV Research and TreatmentT-cell and Retrovirus StudiesVirus-based gene therapy research

Chromatin Tethering of Incoming Foamy Virus by the Structural Gag Protein

Open access
Tobaly‐Tapiero, Joelle, Bittoun, Patricia, Lehmann‐Che, Jacqueline, Delelis, Olivier, Giron, Marie‐Lou, De Thé, Hugues, Saïb, Ali·2008·Traffic

Abstract

Retroviruses hijack cellular machineries to productively infect their hosts. During the early stages of viral replication, proviral integration relies on specific interactions between components of the preintegration complex and host chromatin‐bound proteins. Here, analyzing the fate of incoming primate foamy virus, we identify a short domain within the C‐terminus of the structural Gag protein that efficiently binds host chromosomes, by interacting with H2A/H2B core histones. While viral particle production, virus entry and intracellular trafficking are not affected by mutation of this domain, chromosomal attachment of incoming subviral complexes is abolished, precluding proviral integration. We thus highlight a new function of the structural foamy Gag protein as the main tether between incoming subviral complexes and host chromatin prior to integration.

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Crossref · 10.1111/j.1600-0854.2008.00792.x

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  • The PFV Gag chromatin binding sequence binds nucleosomes via an acidic patch predominantly composed of core histone H2A/H2B heterodimers.

    “The PFV Gag CBS binds nucleosomes via an acidic patch predominantly composed of core histone H2A/H2B heterodimers91,92”

    From Structure and function of retroviral integrase (2022) · cites this paper as [91]

    The section “The CBS of PFV Gag interacts with core histones H2A/H2B” (p. 6) reports that the PFV Gag CBS associates with H2A and H2B and binds host chromosomes through them. The Discussion (p. 7) cautions that additional factors or other nucleosomal components may be involved. The paper does not identify an acidic patch as the binding site or establish direct binding to an H2A/H2B heterodimer. (LLM, conf=0.88)

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Research works printed but not linked: 1

  1. [24]24. Life RB, Lee EG, Eastman SW, Linial ML. Mutations in the aminoterminus of foamy virus Gag disrupt morphology and infectivity, but not targeting of assembly. J Virol 2008;82:6109-6119.

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Authors
Tobaly‐Tapiero, J., Bittoun, P., Lehmann‐Che, J., Delelis, O., Giron, M., De Thé, H., & Saïb, A.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • École Normale Supérieure Paris-Saclay (FR)
Venue
Traffic
Publisher
Wiley
Published
2008-09-15
Volume
9
Issue
10
Pages
1717-1727
ISSN
  • 1398-9219 (ISSN-L)
  • 1600-0854
OpenAlex
W2011996850
Cited by
74
References
52
Citations by year
2025: 3 · 2024: 3 · 2022: 1 · 2021: 6 · 2020: 4 · 2019: 1 · 2018: 5 · 2017: 3 · 2016: 10 · 2015: 3 · 2014: 2 · 2013: 9 · 2012: 6
FWCI
2.02
Type
journal article
Language
en
Open access
Locations
  • Traffic (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
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
Keywords
Gag protein, chromatin tethering, preintegration complex, proviral integration, retroviral replication
MeSH terms
Animals, Binding Sites, Cell Line, Chlorocebus aethiops, Chromatin, DNA, Viral, Electrophoresis, Polyacrylamide Gel, Cricetinae, Histones, Microscopy, Fluorescence, Mutation, Protein Binding, Recombinant Fusion Proteins, Transfection, Virus Replication, Gene Products, gag, Spumavirus, Virus Integration, Green Fluorescent Proteins

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