ArticleProceedings of the National Academy of Sciences of the United States of America2004
Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 89 citations in OpenAlex.
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- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Mechanical Properties of Viruses.Sub-cellular biochemistry · 2024Review
- Article
- Structural and Biophysical Analysis of Adeno-Associated Virus Serotype 2 Capsid Assembly Variants.Journal of virology · 2023Article
- Molecular Determinants of Human Rhinovirus Infection, Assembly, and Conformational Stability at Capsid Protein Interfaces.Journal of virology · 2022Article
- Article
- Rapid prediction of crucial hotspot interactions for icosahedral viral capsid self-assembly by energy landscape atlasing validated by mutagenesis.PLoS computational biology · 2020Article
- Physical virology: From virus self-assembly to particle mechanics.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2020Review
- Structural Characterization of Cuta- and Tusavirus: Insight into Protoparvoviruses Capsid Morphology.Viruses · 2020Article
- Engineering viable foot-and-mouth disease viruses with increased acid stability facilitate the development of improved vaccines.Applied microbiology and biotechnology · 2020Article
- Systematic analysis of biological roles of charged amino acid residues located throughout the structured inner wall of a virus capsid.Scientific reports · 2018Article
- Molecular jenga: the percolation phase transition (collapse) in virus capsids.Physical biology · 2018Article
- Protoparvovirus Cell Entry.Viruses · 2017Review
- Article
- Beyond icosahedral symmetry in packings of proteins in spherical shells.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations.Scientific reports · 2017Article
- AAV-ID: A Rapid and Robust Assay for Batch-to-Batch Consistency Evaluation of AAV Preparations.Molecular therapy : the journal of the American Society of Gene Therapy · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Twenty-eight amino acid residues involved in most noncovalent interactions between trimeric protein subunits in the capsid of the parvovirus minute virus of mice were truncated individually to alanine, and the effects on capsid assembly, thermostability, and conformation were analyzed. Only seven side chains were essential for protein subunit recognition. These side chains virtually corresponded with those that either buried a large hydrophobic surface on trimer association or formed buried intertrimer hydrogen bonds or salt bridges. The seven residues are evolutionarily conserved, and they define regularly spaced spots on a thin equatorial belt surrounding each trimer. Truncation of the many side chains that were dispensable for assembly, including those participating in solvent-accessible polar interactions, did not substantially affect capsid thermostability either. However, the interfacial residues located at the base of the pores delineating the capsid five-fold axes participated in a heat-induced conformational rearrangement associated with externalization of the capsid protein N terminus, and they were needed for infectivity. Thus, at the subunit interfaces of this model virus capsid, only key residues involved in the strongest interactions are critical for assembly and stability, but additional residues fulfill other important biological roles.
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