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The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.

On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?

Open access
Datta, Siddhartha A. K., Temeselew, Lakew G., Crist, Rachael M., Soheilian, Ferri, Kamata, Anne, Mirro, Jane, Harvin, Demetria, Nagashima, Kunio, Cachau, Raul E., Rein, Alan·2011·Journal of Virology
DOI 10.1128/jvi.00006-11PMC PMC3126284
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Abstract

Expression of a retroviral protein, Gag, in mammalian cells is sufficient for assembly of immature virus-like particles (VLPs). VLP assembly is mediated largely by interactions between the capsid (CA) domains of Gag molecules but is facilitated by binding of the nucleocapsid (NC) domain to nucleic acid. We have investigated the role of SP1, a spacer between CA and NC in HIV-1 Gag, in VLP assembly. Mutational analysis showed that even subtle changes in the first 4 residues of SP1 destroy the ability of Gag to assemble correctly, frequently leading to formation of tubes or other misassembled structures rather than proper VLPs. We also studied the conformation of the CA-SP1 junction region in solution, using both molecular dynamics simulations and circular dichroism. Consonant with nuclear magnetic resonance (NMR) studies from other laboratories, we found that SP1 is nearly unstructured in aqueous solution but undergoes a concerted change to an α-helical conformation when the polarity of the environment is reduced by addition of dimethyl sulfoxide (DMSO), trifluoroethanol, or ethanol. Remarkably, such a coil-to-helix transition is also recapitulated in an aqueous medium at high peptide concentrations. The exquisite sensitivity of SP1 to mutational changes and its ability to undergo a concentration-dependent structural transition raise the possibility that SP1 could act as a molecular switch to prime HIV-1 Gag for VLP assembly. We suggest that changes in the local environment of SP1 when Gag oligomerizes on nucleic acid might trigger this switch.

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Research works printed but not linked: 2

  1. CreightonT. E. 1993. Proteins, 2nd ed. W. H. Freeman and Co., New York, NY.
  2. WarburgO. ChristianW.. 1942. Isolierung und Kristallisation des Garungsferments Enolase. Biochem. Z. 310:384–421.

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Metadata

Authors
Datta, S. A. K., Temeselew, L. G., Crist, R. M., Soheilian, F., Kamata, A., Mirro, J., Harvin, D., Nagashima, K., Cachau, R. E., & Rein, A.
Affiliations
  • National Cancer Institute (US)
  • Science Applications International Corporation (United States) (US)
  • Information Systems Program, SAIC-Frederick, Inc., Frederick, Maryland 21702-1201
Corresponding author
  • Datta, Siddhartha A. K.
  • Rein, Alan
ORCID
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
2011-05
Volume
85
Issue
9
Pages
4111-4121
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
DOI
10.1128/jvi.00006-11
PMC
PMC3126284
OpenAlex
W2115382947
Cited by
127
References
77
Citations by year
2026: 5 · 2025: 1 · 2024: 4 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 10 · 2019: 6 · 2018: 8 · 2017: 13 · 2016: 12 · 2015: 19 · 2014: 9 · 2013: 9 · 2012: 15
FWCI
4.56
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 Institutes of Health
  • U.S. Public Health Service (26120080001E)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords
HIV-1 Gag, virus-like particle assembly, capsid protein, nucleocapsid protein, molecular switches, helix-coil transition, protein conformational change, retroviral assembly
MeSH terms
Animals, Circular Dichroism, DNA Mutational Analysis, Protein Conformation, HIV-1, Virus Assembly, Virosomes, gag Gene Products, Human Immunodeficiency Virus, Molecular Dynamics Simulation

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