Cited by 127HIV Research and TreatmentProtein Structure and DynamicsHIV/AIDS drug development and treatment

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

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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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Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
Sreerama, N., & Woody, R. W. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4880 · Cited by 3,046
Estimation of globular protein secondary structure from circular dichroism
Provencher, S. W., & Gloeckner, J. (1981) · Biochemistry · doi:10.1021/bi00504a006 · Cited by 2,165
The helical hydrophobic moment: a measure of the amphiphilicity of a helix
Eisenberg, D. S., Weiss, R. M., & Terwilliger, T. C. (1982) · Nature · doi:10.1038/299371a0 · Cited by 1,080
Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins
Buck, M. (1998) · Quarterly Reviews of Biophysics · doi:10.1017/s003358359800345x · Cited by 829
Measurement of protein by spectrophotometry at 205 nm
Scopes, R. K. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90034-7 · Cited by 762
DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
Lobley, A., Whitmore, L., & Wallace, B. A. (2002) · Bioinform. · doi:10.1093/bioinformatics/18.1.211 · Cited by 741
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706
Structure of the HIV-1 Nucleocapsid Protein Bound to the SL3 Ψ-RNA Recognition Element
De Guzman, R. N., Wu, Z. R., Stalling, C. C., Pappalardo, L., Borer, P. N., & Summers, M. F. (1998) · Science · doi:10.1126/science.279.5349.384 · Cited by 659
Isolierung und Kristallisation des G�rungsferments Zymohexase
Warburg, O. H., & Walter, C. A. (1942) · Die Naturwissenschaften · doi:10.1007/bf01488995 · Cited by 635
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598

Show all 77 references

Research works printed but not linked: 2

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

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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: Datta, Siddhartha A. K.
Crist, Rachael M.
Nagashima, Kunio
Rein, Alan
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: 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 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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On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?

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