Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Site-directed mutation affecting polyomavirus capsid self-assembly in vitro.

R L Garcea, D M Salunke, D L Caspar

    Nature
    |September 3, 1987
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    STRUCTURE OF FILAMENTOUS BACTERIOPHAGE Pf1.

    Biophysical journal·2009
    Same author

    Gap Junction Structures: III. The Effect of Variations in the Isolation Procedure.

    Biophysical journal·2009
    Same author

    Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction.

    Acta crystallographica. Section D, Biological crystallography·2004
    Same author

    SV40: A human pathogen?

    Disease markers·2002
    Same author

    Enhanced binding of a rationally designed peptide ligand of concanavalin a arises from improved geometrical complementarity.

    Biochemistry·2001
    Same author

    Disordered to ordered folding in the regulation of diphtheria toxin repressor activity.

    Proceedings of the National Academy of Sciences of the United States of America·2001

    Identical protein subunits in polyomavirus capsids exhibit nonequivalent bonding. A mutation affecting the VP1 protein

    Area of Science:

    • Structural biology
    • Virology
    • Protein self-assembly

    Background:

    • Polyomavirus capsids are formed by identical pentameric protein subunits (capsomeres).
    • These capsomeres occupy distinct positions (hexavalent and pentavalent) within the icosahedral lattice, indicating nonequivalent bonding.
    • The major capsid protein, VP1, is responsible for capsid formation and exhibits self-assembly properties.

    Purpose of the Study:

    • To investigate the molecular basis of nonequivalent bonding in polyomavirus capsids.
    • To identify the specific regions of the VP1 protein involved in subunit association.
    • To utilize in vitro self-assembly as an assay for studying VP1 mutations.

    Main Methods:

    • Recombinant expression of the polyomavirus VP1 gene in Escherichia coli.

    Related Experiment Videos

  • Purification of VP1 protein and isolation of capsomeres.
  • In vitro self-assembly assay to observe capsid formation.
  • Site-directed mutagenesis to create a carboxy-terminal truncation mutant of VP1.

    • Main Results:

    • Purified VP1 protein self-assembles into capsid-like structures in vitro.
    • A VP1 mutant with a truncated carboxy terminus forms capsomeres but fails to assemble into complete capsids in vitro.
    • This suggests the carboxy terminus is crucial for the specific interactions driving capsid formation.

    Conclusions:

    • The carboxy terminus of the polyomavirus VP1 protein plays a critical role in mediating the specific, nonequivalent bonding required for capsid assembly.
    • Understanding these interactions provides insights into viral structure and assembly mechanisms.
    • The in vitro self-assembly assay is a valuable tool for dissecting protein-protein interactions in viral capsids.