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Related Experiment Videos

A humanized antibody specific for the platelet integrin gpIIb/IIIa

M S Co1, S Yano, R K Hsu

  • 1Protein Design Labs, Inc., Mountain View, CA 94043.

Journal of Immunology (Baltimore, Md. : 1950)
|March 15, 1994
PubMed
Summary

Humanizing the C4G1 antibody for treating thrombosis maintained its binding affinity and ability to inhibit platelet aggregation. This engineered antibody and its fragments show promise for antithrombotic therapies.

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Area of Science:

  • Immunology
  • Biochemistry
  • Pharmacology

Background:

  • The C4G1 murine monoclonal antibody targets the platelet glycoprotein IIb/IIIa (gpIIb/IIIa) integrin.
  • This integrin plays a crucial role in platelet aggregation and thrombosis.
  • Humanization of antibodies is a key strategy for developing therapeutic agents with reduced immunogenicity.

Purpose of the Study:

  • To humanize the C4G1 murine monoclonal antibody for potential therapeutic applications in thrombosis-related disorders.
  • To assess the binding affinity and functional activity of the humanized antibody and its fragments.
  • To develop genetic constructs for producing Fab and F(ab')2 fragments of the humanized C4G1 antibody.

Main Methods:

  • Cloning and sequencing of variable regions from C4G1 hybridoma light and heavy chains.

Related Experiment Videos

  • Construction of humanized C4G1 antibody (IgG1 isotype) using complementarity-determining regions from C4G1 and human framework/constant regions.
  • Utilizing a computer model to optimize the human framework sequence for homology.
  • Development of genetic constructs for producing Fab and F(ab')2 fragments.

    • Main Results:

    • Humanized C4G1 IgG1, Fab, and F(ab')2 fragments demonstrated equivalent binding affinities to the murine antibody.
    • No loss of binding affinity was observed during the humanization process.
    • The humanized antibody and its fragments effectively inhibited platelet aggregation in vitro.
    • Inhibition of fibrinogen binding to gpIIb/IIIa was also observed in vitro.

    Conclusions:

    • The humanization process successfully retained the binding affinity and functional activity of the C4G1 antibody.
    • Humanized C4G1 antibody and its fragments are viable candidates for antithrombotic therapies.
    • These findings support the potential clinical utility of humanized C4G1 for managing thrombosis.