Molecular determinants that regulate plasma membrane association of HIV-1 Gag
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Human immunodeficiency virus type 1 assembly is a multistep process that occurs at the plasma membrane (PM). Targeting and binding of Gag to the PM are the first steps in this assembly process and are mediated by the matrix domain of Gag. This review highlights our current knowledge on viral and cellular determinants that affect specific interactions between Gag and the PM. We will discuss potential mechanisms by which the matrix domain might integrate three regulatory components, myristate, phosphatidylinositol-(4,5)-bisphosphate, and RNA, to ensure that human immunodeficiency virus type 1 assembly occurs at the PM.
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The MA domain contains a highly basic region essential for regulating Gag relocalization to the plasma membrane by specifically interacting with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).
“The MA domain contains a highly basic region essential for regulating Gag relocalization to the plasma membrane by specifically interacting with phosphatidylinositol 4,5bisphosphate (PI(4,5)P 2 ) (77).”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [77]
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Investigation of HIV-1 Gag binding with RNAs and lipids using Atomic Force Microscopy
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Editorial: Role of lipids in virus assembly
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Cooperative Membrane Binding of HIV-1 Matrix Proteins
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“Later it became apparent that Gag localization to the plasma membrane is contingent on interactions between the HBR and phosphatidylinositol 4,5-bisphosphate (PIP 2 ) (Ono et al. 2004 , Chukkapalli et al. 2008 , Chukkapalli and Ono 2011 , Dick et al. 2012 ).”
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The Role of Lipids in Retroviral Replication
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- Authors
- Chukkapalli, V., & Ono, A.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Ono, Akira
- ORCID
- Ono, Akira
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 410
- Issue
- 4
- Pages
- 512-524
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC3139151
- OpenAlex
- W1982692592
- Cited by
- 129
- References
- 121
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 8 · 2023: 1 · 2022: 5 · 2021: 8 · 2020: 10 · 2019: 11 · 2018: 12 · 2017: 8 · 2016: 11 · 2015: 9 · 2014: 17 · 2013: 12 · 2012: 11
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R56AI089282, R01AI071727)
- 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, Gag, matrix domain, plasma membrane association, viral assembly, myristoylation, phosphatidylinositol 4,5-bisphosphate, RNA binding, membrane targeting
- MeSH terms
- Amino Acid Sequence, Cell Membrane, Humans, Membrane Lipids, Molecular Sequence Data, Protein Binding, Viral Matrix Proteins, HIV-1, gag Gene Products, Human Immunodeficiency Virus
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