Direct interaction between the envelope and matrix proteins of HIV-1
Open accessAbstract
The incorporation of the envelope (env) glycoprotein of the human immunodeficiency virus type 1 (HIV-1) into budding virions has been proposed to be mediated by an interaction between its cytoplasmic domain and the matrix protein of HIV-1. However, this interaction was never directly demonstrated and its role in the biogenesis of HIV-1 virions is still debated. Here, a direct interaction is reported between the matrix protein of HIV-1 and the cytoplasmic domain of the env protein of HIV-1. No interaction was seen with the env cytoplasmic domain of other retroviruses. The region of the HIV-1 env involved in the interaction was delineated by mutagenesis and is comprised of the C-terminal 67 amino acid residues of env. These results, as well as the analysis of mutants of the matrix protein, suggest that the interaction between the HIV-1 env and matrix proteins accounts for the specific incorporation of the env glycoprotein into HIV-1 virions.
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The self-association of HIV-1 MA, especially its trimerization, is crucial for incorporation of envelope glycoprotein into nascently forming virus particles.
“The self-association of HIV-1 MA, and especially its trimerization, has also been shown to be crucial for the incorporation of envelope glycoprotein into the nascently forming virus particles”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Cosson 1996
Proper localization of Env at the plasma membrane is critical for its selective incorporation into budding virions, a process mediated by interactions between the gp41 cytoplasmic tail and the MA domain of the Gag protein.
“Proper localization of Env at the plasma membrane is critical for its selective incorporation into budding virions, a process mediated by interactions between gp41 cytoplasmic tail and the MA domain of the Gag protein”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Cosson 1996
Cites
Dorfman, T., Mammano, F., Haseltine, W. A., & Göttlinger, H. G. (1994) · Journal of Virology · doi:10.1128/jvi.68.3.1689-1696.1994 · Cited by 288 · see citing works
Crystal structure of SIV matrix antigen and implications for virus assembly
Rao, Z., Belyaev, A. S., Fry, E., Roy, P., Jones, I. M., & Stuart, D. I. (1995) · Nature · doi:10.1038/378743a0 · Cited by 183 · see citing works
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HIV-1 Gag proteins: diverse functions in the virus life cycle
Freed, E. O. (1998) · Virology · doi:10.1006/viro.1998.9398 · Cited by 717 · see citing works
Viral and host factors regulating HIV-1 envelope protein trafficking and particle incorporation
Anokhin, B., & Spearman, P. (2022) · Viruses · doi:10.3390/v14081729 · Cited by 21 · see citing works
Sun, W., Reyes-Serratos, E., Barilla, D., Santos, J. R. L., Bujold, M., Graves, S., & Marcet-Palacios, M. (2019) · PLOS ONE · doi:10.1371/journal.pone.0224965 · Cited by 6 · see citing works
Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5 · see citing works
“…is critical for its selective incorporation into budding virions, a process mediated by interactions between gp41 cytoplasmic tail and the MA domain of the Gag protein (Dorf-man et al. 1994 , Freed et al. 1995 , Cosson 1996 , Freed and Martin 1996 , Vincent et al. 1999 , Murakami and Freed 2000 ).”
- Authors
- Cosson, P.
- Corresponding author
- Cosson, P.
- ORCID
- Cosson, P.
- Venue
- The EMBO Journal
- Published
- 1996-11-01
- Volume
- 15
- Issue
- 21
- Pages
- 5783-5788
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC452325
- OpenAlex
- W170446279
- Cited by
- 211
- References
- 2
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 2 · 2022: 6 · 2021: 3 · 2020: 4 · 2019: 6 · 2018: 2 · 2017: 6 · 2016: 4 · 2015: 3 · 2014: 5 · 2013: 15 · 2012: 8
- FWCI
- 3.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (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, envelope glycoprotein, matrix protein, protein-protein interaction, viral budding, cytoplasmic domain, retroviruses
- MeSH terms
- Amino Acid Sequence, Animals, Cytoplasm, Humans, Molecular Sequence Data, Mutation, Recombinant Fusion Proteins, Viral Matrix Proteins, HIV-1, Gene Products, env, Sequence Deletion, COS Cells
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