ArticleJournal of virology2008
Mutations in the spacer peptide and adjoining sequences in Rous sarcoma virus Gag lead to tubular budding.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- Structural Determinants of Virion Assembly and Release in the C Terminus of the Mason-Pfizer Monkey Virus Capsid Protein.Journal of virology · 2021Article
- Effect of Small Polyanions on In Vitro Assembly of Selected Members of Alpha-, Beta- and Gammaretroviruses.Viruses · 2021Article
- Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.PLoS pathogens · 2020Article
- Functional and Structural Characterization of Novel Type of Linker Connecting Capsid and Nucleocapsid Protein Domains in Murine Leukemia Virus.The Journal of biological chemistry · 2016Article
- Helical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.Journal of the American Chemical Society · 2016Article
- Orchestrating the Selection and Packaging of Genomic RNA by Retroviruses: An Ensemble of Viral and Host Factors.Viruses · 2016Review
- Article
- Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.Journal of virology · 2016Article
- Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and Dependent on the Spacer Peptide Assembly Domain.Journal of virology · 2015Article
- The Structure of Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10 Domain in Assembly.Journal of virology · 2015Article
- Atomic Modeling of an Immature Retroviral Lattice Using Molecular Dynamics and Mutagenesis.Structure (London, England : 1993) · 2015Article
- Role of Mason-Pfizer monkey virus CA-NC spacer peptide-like domain in assembly of immature particles.Journal of virology · 2014Article
- Potential role for CA-SP in nucleating retroviral capsid maturation.Journal of virology · 2014Article
- Higher-order structure of the Rous sarcoma virus SP assembly domain.Journal of virology · 2014Article
- A two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition.Journal of virology · 2013Article
- Effect of multimerization on membrane association of Rous sarcoma virus and HIV-1 matrix domain proteins.Journal of virology · 2013Article
- In vitro assembly of virus-like particles of a gammaretrovirus, the murine leukemia virus XMRV.Journal of virology · 2012Article
- Assembly and architecture of HIV.Advances in experimental medicine and biology · 2012Review
- Design of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assembly.Journal of molecular biology · 2011Article
- On the role of the SP1 domain in HIV-1 particle assembly: a molecular switch?Journal of virology · 2011Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
All orthoretroviruses encode a single structural protein, Gag, which is necessary and sufficient for the assembly and budding of enveloped virus-like particles from the cell. The Gag proteins of Rous sarcoma virus (RSV) and human immunodeficiency virus type 1 (HIV-1) contain a short spacer peptide (SP or SP1, respectively) separating the capsid (CA) and nucleocapsid (NC) domains. SP or SP1 and the residues immediately upstream are known to be critical for proper assembly. Using mutagenesis and electron microscopy analysis of insect cells or chicken cells overexpressing RSV Gag, we defined the SP assembly domain to include the last 8 residues of CA, all 12 residues of SP, and the first 4 residues of NC. Five- or two-amino acid glycine-rich insertions or substitutions in this critical region uniformly resulted in the budding of abnormal, long tubular particles. The equivalent SP1-containing HIV-1 Gag sequence was unable to functionally replace the RSV sequence in supporting normal RSV spherical assembly. According to secondary structure predictions, RSV and HIV-1 SP/SP1 and adjoining residues may form an alpha helix, and what is likely the functionally equivalent sequence in murine leukemia virus Gag has been inferred by mutational analysis to form an amphipathic alpha helix. However, our alanine insertion mutagenesis did not provide evidence for an amphipathic helix in RSV Gag. Taken together, these results define a short assembly domain between the folded portions of CA and NC, which is essential for formation of the immature Gag shell.
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