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Cited by 145HIV Research and TreatmentLipid Membrane Structure and BehaviorCellular transport and secretion

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

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Alfadhli, Ayna, Still, Amelia, Barklis, Eric·2009·Journal of Virology
DOI 10.1128/jvi.01197-09PMC PMC2786731
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Abstract

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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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
DOI
10.1128/jvi.01197-09
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
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
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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