The N-domain of the Human CD66a Adhesion Molecule Is a Target for Opa Proteins of Neisseria Meningitidis and Neisseria Gonorrhoeae

Mol Microbiol. 1996 Dec;22(5):929-39. doi: 10.1046/j.1365-2958.1996.01548.x.

Abstract

Using COS (African green monkey kidney) cells transfected with cDNAs encoding human cell surface molecules, we have identified human cellular receptors for meningococcal virulence-associated Opa proteins, which are expressed by the majority of disease and carrier isolates. These receptors belong to the immunoglobulin superfamily of adhesion molecules and are expressed on epithelial, endothelial and phagocytic cells. Using soluble chimeric receptor molecules, we have demonstrated that meningococcal Opa proteins bind to the N-terminal domain of biliary glycoproteins (classified as BGP or CD66a) that belong to the CEA (CD66) family. Moreover, the Opa proteins of the related pathogen Neisseria gonorrhoeae, responsible for urogenital infections, also interact with this receptor, making CD66a a common target for pathogenic neisseriae. Over 95% of Opa-expressing clinical and mucosal isolates of meningococci and gonococci were shown to bind to the CD66 N-domain, demonstrating the presence of a conserved receptor-binding function in the majority of neisserial Opa proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Bacterial / immunology*
  • Antigens, CD / genetics
  • Antigens, CD / immunology*
  • Antigens, Differentiation / genetics
  • Antigens, Differentiation / immunology*
  • Binding Sites
  • CHO Cells
  • COS Cells
  • Cell Adhesion Molecules / immunology*
  • Cell Line, Transformed
  • Cricetinae
  • Humans
  • Ligands
  • Neisseria gonorrhoeae / immunology*
  • Neisseria meningitidis / immunology*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / immunology
  • Transfection

Substances

  • Antigens, Bacterial
  • Antigens, CD
  • Antigens, Differentiation
  • CD66 antigens
  • Cell Adhesion Molecules
  • Ligands
  • Recombinant Fusion Proteins
  • opacity proteins