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 accessAbstract
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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“The second region proposed to act as a structural switch is the SP1 spacer peptide downstream of CA”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [74]
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Cites
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
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
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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Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814
An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation
Schur, F. K. M., Obr, M., Hagen, W. J. H., Wan, W., Jakobi, A. J., Kirkpatrick, J. M., Sachse, C., Kräusslich, H., & Briggs, J. A. G. (2016) · Science · doi:10.1126/science.aaf9620 · Cited by 423
HIV Gag polyprotein: processing and early viral particle assembly
Bell, N. M., & Lever, A. M. L. (2013) · Trends in Microbiology · doi:10.1016/j.tim.2012.11.006 · Cited by 222
Retroviral proteases and their roles in virion maturation
Konvalinka, J., Kräusslich, H.-G., & Müller, B. (2015) · Virology · doi:10.1016/j.virol.2015.03.021 · Cited by 148
Crystal structure of an HIV assembly and maturation switch
Wagner, J. M., Zadrozny, K. K., Chrustowicz, J., Purdy, M. D., Yeager, M. J., Ganser‐Pornillos, B. K., & Pornillos, O. (2016) · eLife · doi:10.7554/elife.17063 · Cited by 136
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
- 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
- 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
- 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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