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Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
Author(s) -
Källström Helena,
Liszewski M. Kathryn,
Atkinson John P.,
Jonsson AnnBeth
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.4841857.x
Subject(s) - pilus , cd46 , neisseria , biology , neisseria meningitidis , microbiology and biotechnology , neisseria gonorrhoeae , fimbriae proteins , recombinant dna , bacterial outer membrane , complement control protein , monoclonal antibody , bacteria , antibody , complement system , escherichia coli , biochemistry , gene , genetics , immunology
Pili of Neisseria gonorrhoeae and Neisseria meningitidis mediate binding of the bacteria to human cell‐surface receptors. We found that purified pili bound to a 55‐ to 60‐kDa doublet band on SDS–PAGE of separated human epithelial cell extracts. This is a migration pattern typical of membrane cofactor protein (MCP or CD46). MCP is a widely distributed human complement regulatory protein. Attachment of the bacteria to epithelial cells was blocked by polyclonal and monoclonal antibodies directed against MCP, suggesting that this complement regulator is a receptor for piliated Neisseria . We proved this hypothesis by demonstrating that piliated, but not non‐piliated, gonococci bound to CHO cells transfected with human MCP‐cDNA. We also demonstrated a direct interaction between purified recombinant MCP and piliated Neisseria . Finally, recombinant MCP protein produced in E . coli inhibited attachment of the bacteria to target cells. Taken together, our data show that MCP is a human cell‐surface receptor for piliated pathogenic Neisseria .