ArticleJournal of virology2008
Critical role of conserved hydrophobic residues within the major homology region in mature retroviral capsid assembly.
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 29 papers.
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Who cites it
29 citing papers in PubMed.
- Determinants in the HTLV-1 Capsid Major Homology Region that are Critical for Virus Particle Assembly.Journal of molecular biology · 2024Article
- Endogenous capsid-forming protein ARC for self-assembling nanoparticle vaccines.Journal of nanobiotechnology · 2024Article
- The Rous sarcoma virus Gag Polyprotein Forms Biomolecular Condensates Driven by Intrinsically-disordered Regions.Journal of molecular biology · 2023Article
- Review
- Bottleneck Size-Dependent Changes in the Genetic Diversity and Specific Growth Rate of a Rotavirus A Strain.Journal of virology · 2020Article
- Article
- Article
- Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.Journal of virology · 2016Article
- Episodic Diversifying Selection Shaped the Genomes of Gibbon Ape Leukemia Virus and Related Gammaretroviruses.Journal of virology · 2016Article
- Mutations of Conserved Residues in the Major Homology Region Arrest Assembling HIV-1 Gag as a Membrane-Targeted Intermediate Containing Genomic RNA and Cellular Proteins.Journal of virology · 2016Article
- Biophysical analysis of the MHR motif in folding and domain swapping of the HIV capsid protein C-terminal domain.Biophysical journal · 2015Article
- 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
- One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions.Journal of structural biology · 2013Article
- Article
- The maturational refolding of the β-hairpin motif of equine infectious anemia virus capsid protein extends its helix α1 at capsid assembly locus.The Journal of biological chemistry · 2013Article
- Biophysical characterization of the feline immunodeficiency virus p24 capsid protein conformation and in vitro capsid assembly.PloS one · 2013Article
- Structural and functional insights into the HIV-1 maturation inhibitor binding pocket.PLoS pathogens · 2012Article
- Assembly and architecture of HIV.Advances in experimental medicine and biology · 2012Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
During retroviral maturation, the CA protein undergoes dramatic structural changes and establishes unique intermolecular interfaces in the mature capsid shell that are different from those that existed in the immature precursor. The most conserved region of CA, the major homology region (MHR), has been implicated in both immature and mature assembly, although the precise contribution of the MHR residues to each event has been largely undefined. To test the roles of specific MHR residues in mature capsid assembly, an in vitro system was developed that allowed for the first-time formation of Rous sarcoma virus CA into structures resembling authentic capsids. The ability of CA to assemble organized structures was destroyed by substitutions of two conserved hydrophobic MHR residues and restored by second-site suppressors, demonstrating that these MHR residues are required for the proper assembly of mature capsids in addition to any role that these amino acids may play in immature particle assembly. The defect caused by the MHR mutations was identified as an early step in the capsid assembly process. The results provide strong evidence for a model in which the hydrophobic residues of the MHR control a conformational reorganization of CA that is needed to initiate capsid assembly and suggest that the formation of an interdomain interaction occurs early during maturation.
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