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Related Experiment Videos

Convulxin binds to native, human glycoprotein Ib alpha.

Sachiko Kanaji1, Taisuke Kanaji, Kenichi Furihata

  • 1Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037, USA.

The Journal of Biological Chemistry
|July 26, 2003
PubMed
Summary

Convulxin (CVX), a snake venom protein, binds to both platelet receptors GPVI and GPIb alpha. This dual specificity suggests GPIb alpha may contribute to CVX-induced platelet activation, requiring re-evaluation of its role.

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Area of Science:

  • Biochemistry
  • Hematology
  • Pharmacology

Background:

  • Convulxin (CVX) from Crotalus durissus terrificus venom is a known agonist for glycoprotein VI (GPVI), crucial for platelet adhesion.
  • GPVI mediates platelet aggregation and activation in response to collagen.
  • The role of other platelet receptors in CVX-mediated responses is less understood.

Purpose of the Study:

  • To investigate the binding specificities of purified Convulxin (CVX).
  • To determine if CVX interacts with platelet receptors beyond GPVI.
  • To re-evaluate the contribution of GPIb alpha to CVX-induced platelet responses.

Main Methods:

  • Purification of Convulxin (CVX) from Crotalus durissus terrificus venom.
  • Binding assays using cell lines expressing human GPIb alpha and GPVI.

Related Experiment Videos

  • Comparative binding studies in wild-type and genetically modified mice (GPVI-/-, FcR gamma-/-, GPIb alpha transgenic).
  • Inhibition studies using soluble GPVI and anti-GPIb alpha antibodies.
  • Analysis of CVX binding to native versus denatured GPIb alpha.

    • Main Results:

    • CVX binds to both platelet GPVI and native human GPIb alpha, but not denatured GPIb alpha.
    • CVX exhibits differential binding to murine versus human GPIb alpha, with stronger binding to human.
    • CVX binding to GPIb alpha is inhibited by soluble GPVI and function-blocking anti-GPIb alpha antibodies.
    • Key tyrosine residues (Y276, Y278, Y279) on GPIb alpha are critical for CVX binding, similar to von Willebrand factor and alpha-thrombin.

    Conclusions:

    • Convulxin (CVX) demonstrates dual specificity, binding to both GPVI and native GPIb alpha.
    • The binding site for CVX on GPIb alpha may overlap with or be near the von Willebrand factor binding site.
    • The role of GPIb alpha in CVX-induced platelet activation warrants further investigation and potential re-evaluation.