Open AccessListericidal activity of human neutrophil cathepsin G
Author(s) -
Charlotte Alford,
Elizabeth Amaral,
Priscilla A. Campbell
Publication year - 1990
Publication title -
journal of general microbiology/journal of general microbiology
Language(s) - English
Resource type - Journals
eISSN - 2059-9323
pISSN - 0022-1287
DOI - 10.1099/00221287-136-6-997
Subject(s) - cathepsin , listeria monocytogenes , cathepsin g , in vitro , chemistry , cathepsin s , antimicrobial , cathepsin l1 , cathepsin l , cathepsin d , microbiology and biotechnology , cathepsin b , biochemistry , enzyme , bacteria , biology , elastase , genetics
We demonstrate that cathepsin G, derived from human neutrophils, exhibits potent in vitro antimicrobial activity against Listeria monocytogenes. Cathepsin G listericidal activity was by a non-enzymic mechanism and was dependent on the cationic nature of the molecule. The listericidal activity of cathepsin G occurred in a manner that was both time-dependent and concentration-dependent.