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A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation.

Harumi Kasamatsu1, Jennifer Woo, Akiko Nakamura

  • 1Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.

Protein Science : a Publication of the Protein Society
|August 3, 2006
PubMed
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Temperature-sensitive mutants of SV40 major capsid protein (VP1) reveal two distinct classes of assembly defects. Mutations affecting the C-terminal invading arm (C-arm) interactions disrupt virion assembly, explaining complementation patterns.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • SV40 major capsid protein (VP1) is crucial for virion assembly.
  • Temperature-sensitive (ts) mutants (ts B, ts C, ts BC) exhibit assembly defects at non-permissive temperatures.
  • Complementation studies suggest distinct functional roles for different VP1 regions.

Purpose of the Study:

  • To classify SV40 VP1 temperature-sensitive mutants based on structural and functional defects.
  • To elucidate the role of C-terminal invading arm (C-arm) interactions in SV40 capsid assembly.
  • To understand the basis of intracistronic complementation in VP1 mutants.

Main Methods:

  • Analysis of temperature-sensitive mutants (ts B, ts C, ts BC) of SV40 VP1.
  • Characterization of virion assembly defects at non-permissive temperatures.

Related Experiment Videos

  • Mapping of mutations to specific regions of the VP1 protein and their predicted structural impact.

    • Main Results:

    • Mutations were categorized into two classes based on structural and functional defects.
    • Class 1 (ts C, some ts BC) mutations near Ca2+ sites disrupt distal C-arm insertion, causing severe assembly defects.
    • Class 2 (ts B, most ts BC) mutations affect proximal C-arm interactions and intrapentamer contacts, forming assembly intermediates.

    Conclusions:

    • Accurate SV40 virion assembly requires proper interactions involving both proximal and distal C-arm regions.
    • Disruption of distal C-arm interactions has a more significant impact on assembly than proximal C-arm disruptions.
    • The spatial localization and distinct assembly defects of mutant classes explain their complementation behavior and inform capsid assembly models.