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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.

Original publication

DOI

10.1046/j.1365-2958.1996.01548.x

Type

Journal article

Journal

Molecular microbiology

Publication Date

12/1996

Volume

22

Pages

929 - 939

Addresses

Department of Paediatrics, University of Oxford, John Radcliffe Hospital, UK. mumtaz.virji@paediatrics.oxford.ac.uk

Keywords

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