Expression of the carbohydrate recognition domain of lung surfactant protein D and demonstration of its binding to lipopolysaccharides of gram-negative bacteria

Biochem Biophys Res Commun. 1994 Aug 15;202(3):1674-80. doi: 10.1006/bbrc.1994.2127.

Abstract

Surfactant protein D is a collagenous C-type lectin (collectin) that is found almost exclusively in the lung. A recombinant protein, composed of the neck-region and the carbohydrate binding domain of bovine lung surfactant protein D, has been overexpressed in E. coli. The recombinant protein showed the same sugar binding specificity as the native protein and was able to bind to the lipopolysaccharides of several strains of Gram-negative bacteria, such as Klebsiella pneumoniae, Pseudomonas aeruginosa and Escherichia coli, which are known to cause lung infections. The binding was calcium-dependent and was inhibited by maltose. Native bovine surfactant protein D was also shown to be able to bind to these lipopolysaccharides in the same manner.

MeSH terms

  • Animals
  • Binding Sites
  • Carbohydrate Metabolism*
  • Cattle
  • Escherichia coli / metabolism*
  • Glutathione Transferase / metabolism
  • Glycoproteins / genetics
  • Glycoproteins / metabolism*
  • Klebsiella pneumoniae / metabolism*
  • Lipopolysaccharides / metabolism*
  • Pseudomonas aeruginosa / metabolism*
  • Pulmonary Surfactant-Associated Protein D
  • Pulmonary Surfactants / genetics
  • Pulmonary Surfactants / metabolism*
  • Recombinant Fusion Proteins / metabolism

Substances

  • Glycoproteins
  • Lipopolysaccharides
  • Pulmonary Surfactant-Associated Protein D
  • Pulmonary Surfactants
  • Recombinant Fusion Proteins
  • Glutathione Transferase