Function
Metalloprotease able to cleave casein, gelatin, elastin, fibrinogen and fibronectin. Shows exclusive preference for hydrophobic residues, especially Leu, Tyr and Met, at the P1' position of substrates, and for Pro or Ala at P3. Can efficiently cleave the antimicrobial peptide LL-37 which is a component of the immune system, leading to a significant reduction of its bactericidal activity. Is also able to inhibit all pathways of the human complement system. The classical and lectin complement pathways are inhibited because of the efficient degradation of mannose-binding lectin, ficolin-2, ficolin-3, and C4 by karilysin, whereas inhibition of the terminal pathway is caused by cleavage of C5. Thus, karilysin appears to be a major virulence factor of T.forsythia that contributes to evasion of the human immune response and periodontal disease. Seems to act synergistically with gingipains from the periodontal pathogen P.gingivalis present at the same sites of infection.
Sequence
MKRFILLFFLSTIAIFKVYSQRLYDNGPLTGDNNYVLQGSKWNKTTLKYYIYNSSSHLTTTERENAIRSAFALWSDKSTLSFIQVYNPNQADIKIKWEKGNHGDGYPFDGNTGILAHAFYPPPAGGNYAGHLHFDGDENWSINGSGIDLITVAAHEIGHLLGIEHSNVSSALMYPYYTGIKRQLDNDDCLAVWDLYGYPFSISGPSSVCDQATYTVENLLSGATVQWSVSNPNIATINSSNGVLTCRGNGICEVRATINNSSVALTPLKICLGTPISQDITLTVESLNSNGTLCTDNPNAIMADHPGGNHLGYIREYEWRISNGWQIAHHPGDNGIYADHFIVTVIPLSPLPGSPTVSVRARSECGWGTWKEVQIPAVSCSRTISPFTLSPNPATDEVILQLMETDEVSGLSVLSTDRSAYEIQIWSGMRMLRSFRTNEPTFQISMTGLPAGLYFVRVVKNGQTYTQKLIKK