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Related Experiment Videos

RGD-mutants of B-lymphotropic polyomavirus capsids specifically bind to alpha(v)beta3 integrin.

J Langner1, B Neumann, S L Goodman

  • 1Research Program Infection and Cancer, Deutsches Krebsforschungszentrum, Heidelberg, Germany.

Archives of Virology
|August 4, 2004
PubMed
Summary
This summary is machine-generated.

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Researchers modified the B-lymphotropic polyomavirus (LPV) major capsid protein VP1 to alter its receptor binding. Mutants assembled into capsids and lost LPV receptor binding, with some selectively binding to alpha(v)beta3 integrin.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Integrins are cell surface receptors that bind extracellular matrix ligands and some viruses.
  • A subset of integrins recognizes the arginine-glycine-aspartic acid (RGD) motif.
  • B-lymphotropic polyomavirus (LPV) uses a sialylated receptor, not RGD-binding integrins.

Purpose of the Study:

  • To engineer B-lymphotropic polyomavirus (LPV) VP1 capsid protein to bind RGD-recognizing integrins.
  • To investigate the structural and functional consequences of altering LPV capsid surface loops.

Main Methods:

  • Site-directed mutagenesis was used to introduce RGD motifs into surface loops of the LPV VP1 protein.
  • Recombinant VP1 proteins were expressed in insect cells using a baculovirus vector.

Related Experiment Videos

  • Capsid assembly, receptor binding, and antibody neutralization assays were performed on mutant capsids.

    • Main Results:

    • Ten VP1 mutants expressed as 40 kDa proteins; five assembled into capsids.
    • All mutant capsids lost binding to the native LPV receptor.
    • Three mutants exhibited specific binding to alpha(v)beta3 integrin, but not other RGD-binding integrins, and this binding was inhibited by specific peptides.

    Conclusions:

    • Modification of LPV VP1 surface loops can redirect capsid binding specificity from a sialylated receptor to specific integrins.
    • The engineered capsids demonstrate selective binding to alpha(v)beta3 integrin, highlighting the potential for targeted delivery applications.
    • Structural changes in mutant capsids were confirmed by differential antibody reactivity.