Cited by 229HIV Research and TreatmentLipid Membrane Structure and BehaviorCellular transport and secretion

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Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain

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Chukkapalli, Vineela, Oh, Seung J., Ono, Akira·2010·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0908661107PMC PMC2824378

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Abstract

Membrane binding of Gag, a crucial step in HIV-1 assembly, is facilitated by bipartite signals within the matrix (MA) domain: N-terminal myristoyl moiety and the highly basic region (HBR). We and others have shown that Gag interacts with a plasma-membrane-specific acidic phospholipid, phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P(2)], via the HBR, and that this interaction is important for efficient membrane binding and plasma membrane targeting of Gag. Generally, in protein-PI(4,5)P(2) interactions, basic residues promote the interaction as docking sites for the acidic headgroup of the lipid. In this study, toward better understanding of the Gag-PI(4,5)P(2) interaction, we sought to determine the roles played by all of the basic residues in the HBR. We identified three basic residues promoting PI(4,5)P(2)-dependent Gag-membrane binding. Unexpectedly, two other HBR residues, Lys25 and Lys26, suppress membrane binding in the absence of PI(4,5)P(2) and prevent promiscuous intracellular localization of Gag. This inhibition of nonspecific membrane binding is likely through suppression of myristate-dependent hydrophobic interaction because mutating Lys25 and Lys26 enhances binding of Gag with neutral-charged liposomes. These residues were reported to bind RNA. Importantly, we found that RNA also negatively regulates Gag membrane binding. In the absence but not presence of PI(4,5)P(2), RNA bound to MA HBR abolishes Gag-liposome binding. Altogether, these data indicate that the HBR is unique among basic phosphoinositide-binding domains, because it integrates three regulatory components, PI(4,5)P(2), myristate, and RNA, to ensure plasma membrane specificity for particle assembly.

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Authors: Chukkapalli, V., Oh, S. J., & Ono, A.
Affiliations: University of Michigan (US)
Corresponding author: Ono, Akira
ORCID: Ono, Akira
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2010-01-04
Volume: 107
Issue: 4
Pages: 1600-1605
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0908661107
PMC: PMC2824378
OpenAlex: W2017522157
Cited by: 229
References: 63
Citations by year: 2026: 7 · 2025: 4 · 2024: 12 · 2023: 6 · 2022: 12 · 2021: 13 · 2020: 15 · 2019: 11 · 2018: 13 · 2017: 7 · 2016: 25 · 2015: 22 · 2014: 25 · 2013: 13 · 2012: 12
FWCI: 6.42
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute
National Institute of Allergy and Infectious Diseases (R01AI071727)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: HIV-1 Gag, matrix domain, membrane binding, phosphatidylinositol 4,5-bisphosphate, myristoylation, RNA binding, plasma membrane targeting, viral assembly, lysine residues, liposome binding
MeSH terms: Cell Membrane, HeLa Cells, Humans, RNA, Viral, HIV-1, Protein Structure, Tertiary, Phosphatidylinositol 4,5-Diphosphate, Virus Internalization, gag Gene Products, Human Immunodeficiency Virus, Hydrophobic and Hydrophilic Interactions

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Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain

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