Complement C2 receptor inhibitor trispanning: A novel human complement inhibitory receptor

Jameel M. Inal, Kwok Min Hui, Sylvie Miot, Sigrun Lange, Marcel Ivan Ramirez, Brigitte Schneider, Gerhard Krueger, Jürg A. Schifferli

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)


The complement system presents a powerful defense against infection and is tightly regulated to prevent damage to self by functionally equivalent soluble and membrane regulators. We describe complement C2 receptor inhibitor trispanning (CRIT), a novel human complement regulatory receptor, expressed on haemopoietic cells and a wide range of tissues throughout the body. CRIT is present in human parasites through horizontal transmission. Serum complement component C2 binds to the N-terminal extracellular domain 1 of CRIT, which, in peptide form, blocks C3 convertase formation and complement-mediated inflammation. Unlike C1 inhibitor, which inhibits the cleavage of C4 and C2, CRIT only blocks C2 cleavage but, in so doing, shares with C1 inhibitor the same functional effect, of preventing classical pathway C3 convertase formation. Ab blockage of cellular CRIT reduces inhibition of cytolysis, indicating that CRIT is a novel complement regulator protecting autologous cells.

Original languageEnglish
Pages (from-to)356-366
Number of pages11
JournalJournal of Immunology
Issue number1
Publication statusPublished - 1 Jan 2005


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