Specific binding of silkworm Bombyx mori 30-kDa lipoproteins to carbohydrates containing glucose

Biosci Biotechnol Biochem. 2002 Oct;66(10):2264-6. doi: 10.1271/bbb.66.2264.

Abstract

Insect lectins are important as part of nonspecific self-defense, but their antifungal mechanisms remain to be elucidated. Fungi contain glucans on the cell surface and insect glucan-binding proteins are considered to be essential for antifungal mechanisms. We purified glucose-binding proteins from hemolymph of pupae of the silkworm Bombyx mori, and the amino acid sequence analysis showed that their two proteins are 30-kDa lipoproteins, major components of B. mori hemolymph. These lipoproteins specifically bound to glucose and glucans, suggesting that they are involved in insect self-defense systems.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bombyx / metabolism*
  • Carbohydrate Metabolism*
  • Glucans / chemistry
  • Glucose / metabolism*
  • Hemolymph / chemistry
  • Hemolymph / metabolism
  • Lipoproteins / isolation & purification
  • Lipoproteins / metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Monosaccharide Transport Proteins / chemistry
  • Monosaccharide Transport Proteins / isolation & purification
  • Protein Binding
  • Pupa

Substances

  • Glucans
  • Lipoproteins
  • Monosaccharide Transport Proteins
  • Glucose