HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bangalore, N. Articles by Shafer, W. M. Search for Related Content PubMed PubMed Citation Articles by Bangalore, N. Articles by Shafer, W. M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 23, 13584-13588, 08, 1990

Identification of the primary antimicrobial domains in human neutrophil cathepsin G

N Bangalore, J Travis, VC Onunka, J Pohl and WM Shafer
Department of Biochemistry, University of Georgia, Athens 30602.

Lysosomal cathepsin G from human neutrophils is a chymotrypsin-like protease which also possesses antimicrobial activity. The antimicrobial activity, however, is independent of protease activity, because treatment of this enzyme with the irreversible serine protease inhibitor diisopropylfluorophosphate has no effect on its antimicrobial action. In this study, we found that digestion of cathepsin G with clostripain caused a loss of proteolytic activity in this neutrophil proteinase. However, bactericidal activity in in vitro assays against Staphylococcus aureus and Neisseria gonorrhoeae was retained. Fractionation of the clostripain-digested cathepsin G mixture yielded two distinct antimicrobial peptides. The sequences of these peptides were IIGGR and HPQYNQR (residues 1-5 and 77-83 in cathepsin G, respectively). Synthetic peptides corresponding to these sequences were also prepared and found to exert broad-spectrum antimicrobial activity in vitro, displaying conditions of temperature- and pH-dependent optima for antimicrobial action resembling that of the full-length enzyme. Depending on the target bacterial strain, these peptides exhibited antimicrobial activity between 5.0 x 10(-5) and 4.0 x 10(-4) M. Significantly, replacement of certain residues within these peptides with either alanine or valine significantly reduced their antibacterial capacities. Our studies suggest that cathepsin G has two antimicrobial sequences, either or both of which may contribute to its bactericidal activity.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. F. de Haar, P. S. Hiemstra, M. T. J. M. van Steenbergen, V. Everts, and W. Beertsen Role of Polymorphonuclear Leukocyte-Derived Serine Proteinases in Defense against Actinobacillus actinomycetemcomitans Infect. Immun., September 1, 2006; 74(9): 5284 - 5291. [Abstract] [Full Text] [PDF]

				M. Liao, P. S. Ruddock, A. S. Rizvi, S. H. Hall, F. S. French, and J. R. Dillon Cationic peptide of the male reproductive tract, HE2{alpha}, displays antimicrobial activity against Neisseria gonorrhoeae, Staphylococcus aureus and Enterococcus faecalis J. Antimicrob. Chemother., November 1, 2005; 56(5): 957 - 961. [Abstract] [Full Text] [PDF]

				C. A. Rivera-Marrero, J. Stewart, W. M. Shafer, and J. Roman The Down-Regulation of Cathepsin G in THP-1 Monocytes after Infection with Mycobacterium tuberculosis Is Associated with Increased Intracellular Survival of Bacilli Infect. Immun., October 1, 2004; 72(10): 5712 - 5721. [Abstract] [Full Text] [PDF]

				Y. M. van der Geld, P. C. Limburg, and C. G. M. Kallenberg Proteinase 3, Wegener's autoantigen: from gene to antigen J. Leukoc. Biol., February 1, 2001; 69(2): 177 - 190. [Abstract] [Full Text]

				D. M. MacIvor, S. D. Shapiro, C. T.N. Pham, A. Belaaouaj, S. N. Abraham, and T. J. Ley Normal Neutrophil Function in Cathepsin G-Deficient Mice Blood, December 15, 1999; 94(12): 4282 - 4293. [Abstract] [Full Text] [PDF]

				H. F. Rosenberg and H. F. Rosenberg Recombinant Human Eosinophil Cationic Protein J. Biol. Chem., April 7, 1995; 270(14): 7876 - 7881. [Abstract] [Full Text] [PDF]