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Cited by 48HIV Research and TreatmentHIV/AIDS drug development and treatmentRNA and protein synthesis mechanisms

HIV-1 matrix-tRNA complex structure reveals basis for host control of Gag localization

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Bou-Nader, Charles, Muecksch, Frauke, Brown, Janae B., Gordon, Jackson M., York, Ashley, Peng, Chen, Ghirlando, Rodolfo, Summers, Michael F. +2 more·2021·Cell Host & Microbe
DOI 10.1016/j.chom.2021.07.006PMC PMC8650744
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Abstract

The HIV-1 virion structural polyprotein, Gag, is directed to particle assembly sites at the plasma membrane by its N-terminal matrix (MA) domain. MA also binds to host tRNAs. To understand the molecular basis of MA-tRNA interaction and its potential function, we present a co-crystal structure of HIV-1 MA-tRNA Lys3 complex. The structure reveals a specialized group of MA basic and aromatic residues preconfigured to recognize the distinctive structure of the tRNA elbow. Mutational, cross-linking, fluorescence, and NMR analyses show that the crystallographically defined interface drives MA-tRNA binding in solution and living cells. The structure indicates that MA is unlikely to bind tRNA and membrane simultaneously. Accordingly, single-amino-acid substitutions that abolish MA-tRNA binding caused striking redistribution of Gag to the plasma membrane and reduced HIV-1 replication. Thus, HIV-1 exploits host tRNAs to occlude a membrane localization signal and control the subcellular distribution of its major structural protein.

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  • NRTI resistance mainly arises from the high error rate of HIV reverse transcriptase, with key mechanisms being excision and discrimination.

    “Resistance to them mainly arises from the high error rate of HIV reverse transcriptase (RT) during replication. The key resistance mechanisms involve either excision, where a mutated RT removes an incorporated NRTI, or discrimination, where mutations alter the dNTP-binding pocket to selectively block NRTI-triphosphate incorporation (4, 40).”

    From Research progress on HIV-1 structural proteins and antiviral therapies (2026) · cites this paper as [4]

    The Results section on MA:tRNA binding reports reverse-transcriptase activity as a measure of viral replication, not RT's error rate or NRTI resistance. Searches for NRTI resistance, excision, discrimination, and the dNTP-binding pocket found no passage in our copy addressing those mechanisms. (LLM, conf=0.76)

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Authors
Bou-Nader, C., Muecksch, F., Brown, J. B., Gordon, J. M., York, A., Peng, C., Ghirlando, R., Summers, M. F., Bieniasz, P. D., & Zhang, J.
Affiliations
  • Rockefeller University (US)
  • University of Maryland, Baltimore County (US)
  • National Institute of Diabetes and Digestive and Kidney Diseases (US)
  • Howard Hughes Medical Institute (US)
  • National Institutes of Health (US)
Corresponding author
  • Bieniasz, Paul D.
  • Zhang, Jinwei
ORCID
Venue
Cell Host & Microbe
Publisher
Elsevier BV
Published
2021-09
Volume
29
Issue
9
Pages
1421-1436.e7
ISSN
1931-3128 (ISSN-L)
DOI
10.1016/j.chom.2021.07.006
PMC
PMC8650744
OpenAlex
W3188530856
Cited by
48
References
5
Citations by year
2026: 6 · 2025: 9 · 2024: 12 · 2023: 8 · 2022: 8 · 2021: 5
FWCI
4.64
Type
journal article
Language
en
Open access
Licence
Locations
  • Cell Host & Microbe (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Maryland Shared Open Access Repository (USMAI Consortium) (submittedVersion, cc-by-nc-nd)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • Digital Repository at the University of Maryland (University of Maryland College Park)
Funders
  • National Institutes of Health
  • University of Maryland, Baltimore County
  • Howard Hughes Medical Institute
  • Rockefeller University
  • U.S. Department of Energy (W-31-109-Eng-38)
  • National Institute of Allergy and Infectious Diseases (R01AI150498, R01AI50111, U54AI50470)
  • Argonne National Laboratory
  • National Institute of Diabetes and Digestive and Kidney Diseases (ZIADK075136)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
HIV-1, Gag protein, matrix domain, tRNA binding, co-crystal structure, host-virus interaction, membrane localization, particle assembly, plasma membrane, HIV-1 replication, protein-protein interaction
MeSH terms
Protein Domains, Binding Sites, Cell Membrane, HeLa Cells, Humans, RNA, Transfer, HIV Antigens, HIV-1, RNA-Binding Proteins, Virus Assembly, gag Gene Products, Human Immunodeficiency Virus, HEK293 Cells

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