Structural and biological characterization of Nattectin, a new C-type lectin from the venomous fish Thalassophryne nattereri

Biochimie. 2011 Jun;93(6):971-80. doi: 10.1016/j.biochi.2011.03.001. Epub 2011 Mar 17.

Abstract

Lectins are glycan-binding receptors that recognize glycan epitopes on foreign pathogens and in the host systems. They can be involved in functions that include innate immunity, development, immune regulation and homeostasis. Several lectins have been purified and characterized from fish species. In this work, using cation-exchange chromatography, a galactose-specific lectin belonging to the family of C-type lectins was isolated from the venom of the Brazilian venomous fish Thalassophryne nattereri. Nattectin is a basic, non-glycosilated, 15 kDa monomeric protein. It exhibits hemagglutination activity that is independent of Ca(2+). We also demonstrated a lectin activity for Nattectin in the innate immune system, especially in neutrophil mobilization in mice, indicating that marine organisms are source of immunomodulator agents.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Batrachoidiformes*
  • Binding Sites
  • Calcium / metabolism
  • Cell Movement
  • Conserved Sequence
  • Fish Venoms / administration & dosage
  • Fish Venoms / chemistry
  • Fish Venoms / isolation & purification
  • Fish Venoms / metabolism*
  • Galactose / metabolism
  • Hemagglutination Tests
  • Hindlimb / pathology
  • Humans
  • Immunity, Innate
  • Immunologic Factors / administration & dosage
  • Immunologic Factors / chemistry
  • Immunologic Factors / isolation & purification
  • Immunologic Factors / metabolism*
  • Inflammation / chemically induced
  • Inflammation / immunology
  • Lectins, C-Type / administration & dosage
  • Lectins, C-Type / chemistry
  • Lectins, C-Type / isolation & purification
  • Lectins, C-Type / metabolism*
  • Leukocytes / drug effects
  • Leukocytes / physiology
  • Matrix Metalloproteinases / metabolism
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein
  • Structural Homology, Protein

Substances

  • Fish Venoms
  • Immunologic Factors
  • Lectins, C-Type
  • nattectin protein, Thalassophryne nattereri
  • Matrix Metalloproteinases
  • Calcium
  • Galactose