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

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

doi:10.1128/jvi.00006-11

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

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 +2 more·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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The second region proposed to act as a structural switch is the SP1 spacer peptide downstream of CA.
“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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Immature HIV-1 lattice assembly dynamics are regulated by scaffolding from nucleic acid and the plasma membrane
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Morphology and ultrastructure of retrovirus particles
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“The second region proposed to act as a structural switch is the SP1 spacer peptide downstream of CA [74].”
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Structural and functional insights into the HIV-1 maturation inhibitor binding pocket
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Nucleocapsid Protein: A Desirable Target for Future Therapies Against HIV-1
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A Two-Pronged Structural Analysis of Retroviral Maturation Indicates that Core Formation Proceeds by a Disassembly-Reassembly Pathway Rather than a Displacive Transition
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Retroviral Gag protein–RNA interactions: Implications for specific genomic RNA packaging and virion assembly
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Atomic Modeling of an Immature Retroviral Lattice Using Molecular Dynamics and Mutagenesis
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Identification of an HIV-1 Mutation in Spacer Peptide 1 That Stabilizes the Immature CA-SP1 Lattice
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Biochemical Reconstitution of HIV-1 Assembly and Maturation
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Mechanisms of PI(4,5)P2 Enrichment in HIV-1 Viral Membranes
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How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain
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Resistance to Second-Generation HIV-1 Maturation Inhibitors
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Functional Redundancy in HIV-1 Viral Particle Assembly
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HIV-1 Gag protein with or without p6 specifically dimerizes on the viral RNA packaging signal
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Biochemical and Biological Studies of Mouse APOBEC3
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Recent advances in HIV-1 Gag inhibitor design and development
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The Nucleocapsid Domain of Gag Is Dispensable for Actin Incorporation into HIV-1 and for Association of Viral Budding Sites with Cortical F-Actin
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Aspects of HIV-1 assembly that promote primer tRNALys3 annealing to viral RNA
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Higher-Order Structure of the Rous Sarcoma Virus SP Assembly Domain
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Relationship between HIV-1 Gag Multimerization and Membrane Binding
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The HIV-1 Gag Protein Displays Extensive Functional and Structural Roles in Virus Replication and Infectivity
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Inositol Hexakisphosphate (IP6) Accelerates Immature HIV-1 Gag Protein Assembly toward Kinetically Trapped Morphologies
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Magic angle spinning NMR of viruses
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Investigation of the Structure and Dynamics of the Capsid–Spacer Peptide 1–Nucleocapsid Fragment of the HIV‐1 Gag Polyprotein by Solution NMR Spectroscopy
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Mechanistic Studies and Modeling Reveal the Origin of Differential Inhibition of Gag Polymorphic Viruses by HIV-1 Maturation Inhibitors
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HIV-1 matrix-31 membrane binding peptide interacts differently with membranes containing PS vs. PI(4,5)P2
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Role of Mason-Pfizer Monkey Virus CA-NC Spacer Peptide-Like Domain in Assembly of Immature Particles
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Alpha-helicoidal HEAT-like Repeat Proteins (αRep) Selected as Interactors of HIV-1 Nucleocapsid Negatively Interfere with Viral Genome Packaging and Virus Maturation
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HIV-1 Protease Uses Bi-Specific S2/S2′ Subsites to Optimize Cleavage of Two Classes of Target Sites
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Distinct Contributions of Different Domains within the HIV-1 Gag Polyprotein to Specific and Nonspecific Interactions with RNA
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Role of Gag mutations in PI resistance in the Swiss HIV cohort study: bystanders or contributors?
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Insight into the mechanism of action of EP-39, a bevirimat derivative that inhibits HIV-1 maturation
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Natural Occurring Polymorphisms in HIV-1 Integrase and RNase H Regulate Viral Release and Autoprocessing
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An Insight to HIV-1 Assembly Through Normal Mode Analysis
Sadre‐Marandi, F. (2017) · Biomath Communications Supplement

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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