The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
Analysis of Human Immunodeficiency Virus Type 1 Matrix Binding to Membranes and Nucleic Acids
Open accessAbstract
The human immunodeficiency virus type 1 (HIV-1) matrix (MA) protein targets HIV-1 precursor Gag (PrGag) proteins to assembly sites at plasma membrane (PM) sites that are enriched in cholesterol and phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P 2 ]. MA is myristoylated, which enhances membrane binding, and specifically binds PI(4,5)P 2 through headgroup and 2′ acyl chain contacts. MA also binds nucleic acids, although the significance of this association with regard to the viral life cycle is unclear. We have devised a novel MA binding assay and used it to examine MA interactions with membranes and nucleic acids. Our results indicate that cholesterol increases the selectivity of MA for PI(4,5)P 2 -containing membranes, that PI(4,5)P 2 binding tolerates 2′ acyl chain variation, and that the MA myristate enhances membrane binding efficiency but not selectivity. We also observed that soluble PI(4,5)P 2 analogues do not compete effectively with PI(4,5)P 2 -containing liposomes for MA binding but surprisingly do increase nonspecific binding to liposomes. Finally, we have demonstrated that PI(4,5)P 2 -containing liposomes successfully outcompete nucleic acids for MA binding, whereas other liposomes do not. These results support a model in which RNA binding protects MA from associating with inappropriate cellular membranes prior to PrGag delivery to PM assembly sites.
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“and that PI(4,5)P 2 outcompetes RNA for MA interaction (80).”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [80]
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Cites
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Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
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Metadata
- Authors
- Alfadhli, A., Still, A., & Barklis, E.
- Affiliations
- Oregon Health & Science University (US)
- Corresponding author
- Barklis, Eric
- ORCID
- Barklis, Eric
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2009-12
- Volume
- 83
- Issue
- 23
- Pages
- 12196-12203
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC2786731
- OpenAlex
- W2122077692
- Cited by
- 145
- References
- 59
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 8 · 2023: 2 · 2022: 4 · 2021: 5 · 2020: 8 · 2019: 10 · 2018: 11 · 2017: 3 · 2016: 17 · 2015: 9 · 2014: 14 · 2013: 10 · 2012: 11
- FWCI
- 4.66
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM060170, R01GM060170)
- National Institute of Allergy and Infectious Diseases (AI071798, R01AI071798)
- 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 matrix protein, membrane binding, phosphatidylinositol 4,5-bisphosphate, cholesterol, myristoylation, nucleic acid binding, RNA binding, viral assembly, Gag protein, liposomes
- MeSH terms
- Cell Membrane, Cholesterol, Humans, Liposomes, Nucleic Acids, Protein Binding, HIV Antigens, HIV-1, Virus Assembly, Phosphatidylinositol 4,5-Diphosphate, gag Gene Products, Human Immunodeficiency Virus
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