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

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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

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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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The Hydrophobic Effect: Formation of Micelles and Biological Membranes
Tanford, C. (1991) · Medical Entomology and Zoology · Cited by 3,327
Cholesterol interactions with phospholipids in membranes
Ohvo-RekilÃ¤, H. (2002) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00020-0 · Cited by 1,003
Evidence for Budding of Human Immunodeficiency Virus Type 1 Selectively from Glycolipid-Enriched Membrane Lipid Rafts
Nguyen, D., & Hildreth, J. E. K. (2000) · Journal of Virology · doi:10.1128/jvi.74.7.3264-3272.2000 · Cited by 788
The HIV lipidome: A raft with an unusual composition
Brügger, B., Glass, B., Haberkant, P., Leibrecht, I., Wieland, F., & Kräusslich, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511136103 · Cited by 730
Plasma membrane rafts play a critical role in HIV-1 assembly and release
Ono, A., & Freed, E. O. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241320298 · Cited by 700
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1.
Bryant, M. L., & Ratner, L. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.523 · Cited by 624
Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., & Freed, E. O. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405596101 · Cited by 553
Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
Saad, J. S., Miller, J., Tai, J., Kim, A., Ghanam, R. H., & Summers, M. F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602818103 · Cited by 545
Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
Zhou, W., Parent, L. J., Wills, J. W., & Resh, M. D. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2556-2569.1994 · Cited by 529
Synthesis, Assembly, and Processing of Viral Proteins
Swanstrom, R. I., & Wills, J. (1997) · Europe PMC (PubMed Central) · Cited by 518

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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: green
www.ncbi.nlm.nih.gov
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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Analysis of Human Immunodeficiency Virus Type 1 Matrix Binding to Membranes and Nucleic Acids

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