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Related Experiment Videos

Eosinophil-granule major basic protein, a C-type lectin, binds heparin.

G Jawahar Swaminathan1, David G Myszka, Phinikoula S Katsamba

  • 1Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom.

Biochemistry
|October 26, 2005
PubMed
Summary

Eosinophil major basic protein (EMBP) binds to heparin, a sugar molecule, independent of calcium. This finding offers new insights into EMBP

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Eosinophil major basic protein (EMBP) is a key component of eosinophil granules, contributing to cytotoxicity and allergic diseases like asthma.
  • EMBP belongs to the C-type lectin family but lacks typical calcium- and carbohydrate-binding sites found in other family members.

Purpose of the Study:

  • To determine the crystal structure of EMBP in complex with a heparin disaccharide without calcium.
  • To investigate the binding interaction between EMBP and heparin/heparin disaccharide.

Main Methods:

  • X-ray crystallography was used to obtain the structure of EMBP bound to a heparin disaccharide.
  • Surface plasmon resonance (SPR) was employed to provide direct evidence of EMBP binding to heparin and its disaccharide.

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Main Results:

  • The crystal structure of EMBP in complex with a heparin disaccharide in the absence of calcium was determined.
  • Direct binding of EMBP to heparin and heparin disaccharide was confirmed using surface plasmon resonance.

Conclusions:

  • EMBP recognizes and binds to heparin and heparin disaccharides, likely through proteoglycans.
  • This interaction suggests novel functions for EMBP beyond its known cytotoxic roles, particularly in the context of allergic inflammation.