TY - JOUR
T1 - Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
AU - Källström, Helena
AU - Liszewski, M. Kathryn
AU - Atkinson, John P.
AU - Jonsson, Ann Beth
PY - 1997
Y1 - 1997
N2 - Pili of Neisseria gonorrhoeae and Neisseria meningitidis mediate binding of the bacteria to human cell-surface receptors. We found that purified pill 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.
AB - Pili of Neisseria gonorrhoeae and Neisseria meningitidis mediate binding of the bacteria to human cell-surface receptors. We found that purified pill 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.
UR - http://www.scopus.com/inward/record.url?scp=0030779080&partnerID=8YFLogxK
U2 - 10.1046/j.1365-2958.1997.4841857.x
DO - 10.1046/j.1365-2958.1997.4841857.x
M3 - Article
C2 - 9379894
AN - SCOPUS:0030779080
SN - 0950-382X
VL - 25
SP - 639
EP - 647
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 4
ER -