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Epitopes on the major capsid protein of simian virus 40

L M Babé1, K Brew, S E Matsuura

  • 1Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.

The Journal of Biological Chemistry
|February 15, 1989
PubMed

Insights

Researchers identified key regions on simian virus 40 (SV40) major capsid protein (VP1) using monoclonal antibodies. A specific nine-amino-acid sequence on VP1 forms a continuous epitope, likely protruding from the virus surface.

Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Simian virus 40 (SV40) is a well-studied DNA tumor virus.
  • The major capsid protein (VP1) is crucial for SV40 structure and infectivity.
  • Understanding SV40 VP1 epitopes is vital for developing antiviral strategies.

Purpose of the Study:

  • To characterize monoclonal antibodies targeting SV40 VP1.
  • To map the antigenic sites on the SV40 major capsid protein.
  • To elucidate the structural basis of SV40 antigenicity.

Main Methods:

  • Isolation and characterization of thirteen monoclonal antibodies against SV40 VP1.
  • Neutralization assays to assess antibody function.
  • Epitope mapping using denatured protein, protease fragments, and synthetic peptides.
  • Analysis of VP1 amino acid sequence for hydrophilicity, hydropathy, and secondary structure predictions.

Main Results:

  • Five monoclonal antibodies neutralized SV40 infectivity.
  • Seven antibodies recognized a continuous epitope within a nine-amino-acid segment (312-321) of VP1.
  • This region exhibits high hydrophilicity and low hydropathy, suggesting surface protrusion.
  • The continuous epitope is part of larger discontinuous epitopes recognized by other antibodies.

Conclusions:

  • A nine-amino-acid segment in the carboxyl-terminal region of SV40 VP1 forms a continuous, surface-exposed antigenic site.
  • This protruding region is a key component of SV40's antigenic structure.
  • The findings provide insights into SV40-host interactions and potential therapeutic targets.

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