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Cited by 211HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.

Requirement for an Intact T-Cell Actin and Tubulin Cytoskeleton for Efficient Assembly and Spread of Human Immunodeficiency Virus Type 1

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Jolly, Clare, Mitar, Ivonne, Sattentau, Quentin J.·2007·Journal of Virology
DOI 10.1128/jvi.01469-06PMC PMC1900271
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Abstract

Human immunodeficiency virus type 1 (HIV-1) infection of CD4 + T cells leads to the production of new virions that assemble at the plasma membrane. Gag and Env accumulate in the context of lipid rafts at the inner and outer leaflets of the plasma membrane, respectively, forming polarized domains from which HIV-1 buds. HIV-1 budding can result in either release of cell-free virions or direct cell-cell spread via a virological synapse (VS). The recruitment of Gag and Env to these plasma membrane caps in T cells is poorly understood but may require elements of the T-cell secretory apparatus coordinated by the cytoskeleton. Using fixed-cell immunofluorescence labeling and confocal microscopy, we observed a high percentage of HIV-1-infected T cells with polarized Env and Gag in capped, lipid raft-like assembly domains. Treatment of infected T cells with inhibitors of actin or tubulin remodeling disrupted Gag and Env compartmentalization within the polarized raft-like domains. Depolymerization of the actin cytoskeleton reduced Gag release and viral infectivity, and actin and tubulin inhibitors reduced Env incorporation into virions. Live- and fixed-cell confocal imaging and assay of de novo DNA synthesis by real-time PCR allowed quantification of HIV-1 cell-cell transfer. Inhibition of actin and tubulin remodeling in infected cells interfered with cell-cell spread across a VS and reduced new viral DNA synthesis. Based on these data, we propose that HIV-1 requires both actin and tubulin components of the T-cell cytoskeleton to direct its assembly and budding and to elaborate a functional VS.

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Metadata

Authors
Jolly, C., Mitar, I., & Sattentau, Q. J.
Affiliations
University of Oxford (GB)
ORCID
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
2007-06
Volume
81
Issue
11
Pages
5547-5560
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
DOI
10.1128/jvi.01469-06
PMC
PMC1900271
OpenAlex
W2137870598
Cited by
211
References
66
Citations by year
2025: 3 · 2024: 4 · 2023: 6 · 2022: 13 · 2021: 6 · 2020: 5 · 2019: 4 · 2018: 13 · 2017: 5 · 2016: 9 · 2015: 9 · 2014: 20 · 2013: 15 · 2012: 22
FWCI
7.01
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Virology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Funders
  • National Institutes of Health
  • Medical Research Council
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, actin cytoskeleton, tubulin, virological synapse, cell-to-cell transmission, viral budding, Gag, Env, lipid rafts, actin depolymerization, tubulin polymerization inhibitors, CD4+ T cells, viral assembly
MeSH terms
Actins, Cell Communication, Cytoskeleton, Humans, T-Lymphocytes, Tubulin, HIV-1, HIV Infections, Virus Assembly, Jurkat Cells, Tubulin Modulators

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