Cited by 87HIV Research and TreatmentHIV/AIDS drug development and treatmentT-cell and Retrovirus Studies

HIV-1 matrix protein binding to RNA

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Alfadhli, Ayna, McNett, Henry, Tsagli, Seyram, Bächinger, Hans Peter, Peyton, David H., Barklis, Eric·2011·Journal of Molecular Biology

Abstract

The matrix (MA) domain of the human immunodeficiency virus type 1 (HIV-1) precursor Gag (PrGag) protein plays multiple roles in the viral replication cycle. One essential role is to target PrGag proteins to their lipid raft-associated phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P(2)] assembly sites at the plasma membranes of infected cells. In addition to this role, several reports have implicated nucleic acid binding properties to retroviral MAs. Evidence indicates that RNA binding enhances the binding specificity of MA to PI(4,5)P(2)-containing membranes and supports a hypothesis in which RNA binding to MA acts as a chaperone that protects MA from associating with inappropriate cellular membranes prior to PrGag delivery to plasma membrane assembly sites. To gain a better understanding of HIV-1 MA-RNA interactions, we have analyzed the interaction of HIV MA with RNA ligands that were selected previously for their high affinities to MA. Binding interactions were characterized via bead binding, fluorescence anisotropy, gel shift, and analytical ultracentrifugation methods. Moreover, MA residues that are involved in RNA binding were identified from NMR chemical shift data. Our results indicate that the MA RNA and PI(4,5)P(2) binding sites overlap and suggest models for Gag-membrane and Gag-RNA interactions and for the HIV assembly pathway.

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Crossref · 10.1016/j.jmb.2011.04.063

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  • The MA domain of HIV-1 Gag interacts with RNAs in vitro and in cells.

    “In addition to NC, which is well known for its viral gRNA binding and chaperone activities, the MA domain of HIV-1 Gag also interacts with RNAs in vitro and in cells (74 -76).”

    From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [75]

    The Results (‘Analysis of MA binding to RNA’; page not provided) show that purified HIV-1 MA binds RNA in vitro. The Discussion (page not provided) proposes MA–RNA binding in vivo but says the identity of the RNAs involved remains unknown; it does not establish the claimed interaction in cells. (LLM, conf=0.86)

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Authors
Alfadhli, A., McNett, H., Tsagli, S., Bächinger, H. P., Peyton, D. H., & Barklis, E.
Affiliations
  • Oregon Health & Science University (US)
  • Portland State University (US)
Corresponding author
  • Alfadhli, Ayna
  • Barklis, Eric
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2011-07
Volume
410
Issue
4
Pages
653-666
ISSN
0022-2836 (ISSN-L)
OpenAlex
W2020867902
Cited by
87
References
6
Citations by year
2026: 2 · 2025: 1 · 2024: 5 · 2023: 1 · 2022: 2 · 2021: 6 · 2020: 7 · 2019: 6 · 2018: 7 · 2017: 2 · 2016: 12 · 2015: 9 · 2014: 11 · 2013: 9 · 2012: 7
FWCI
3.42
Type
journal article
Language
en
Open access
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • PDXScholar (Portland State University) (submittedVersion)
Funders
  • National Institutes of Health
  • 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
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords
HIV-1 matrix protein, RNA binding, Gag protein, phosphatidylinositol 4,5-bisphosphate, lipid rafts, viral assembly, RNA ligands, binding site overlap
MeSH terms
Binding Sites, Binding, Competitive, Fluorescence, Humans, Magnetic Resonance Spectroscopy, Protein Binding, RNA, Viral, Viral Matrix Proteins, HIV-1, Anisotropy, Electrophoretic Mobility Shift Assay, gag Gene Products, Human Immunodeficiency Virus

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