The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jin, T.
Right arrow Articles by Tarkowski, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jin, T.
Right arrow Articles by Tarkowski, A.
The Journal of Immunology, 2004, 172: 1169-1176.
Copyright © 2004 by The American Association of Immunologists

Staphylococcus aureus Resists Human Defensins by Production of Staphylokinase, a Novel Bacterial Evasion Mechanism1

Tao Jin*, Maria Bokarewa2,*, Timothy Foster{dagger}, Jennifer Mitchell{dagger}, Judy Higgins{dagger} and Andrej Tarkowski*

* Department of Rheumatology and Inflammation Research, Sahlgrenska University Hospital, Göteborg, Sweden; and {dagger} Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin, Ireland

{alpha}-Defensins are peptides secreted by polymorphonuclear cells and provide antimicrobial protection mediated by disruption of the integrity of bacterial cell walls. Staphylokinase is an exoprotein produced by Staphylococcus aureus, which activates host plasminogen. In this study, we analyzed the impact of interaction between {alpha}-defensins and staphylokinase on staphylococcal growth. We observed that staphylokinase induced extracellular release of {alpha}-defensins from polymorphonuclear cells. Moreover, a direct binding between {alpha}-defensins and staphylokinase was shown to result in a complex formation. The biological consequence of this interaction was an almost complete inhibition of the bactericidal effect of {alpha}-defensins. Notably, staphylokinase with blocked plasminogen binding site still retained its ability to neutralize the bactericidal effect of {alpha}-defensins. In contrast, a single mutation of a staphylokinase molecule at position 74, substituting lysine for alanine, resulted in a 50% reduction of its {alpha}-defensin-neutralizing properties. The bactericidal properties of {alpha}-defensins were tested in 19 S. aureus strains in vitro and in a murine model of S. aureus arthritis. Staphylococcal strains producing staphylokinase were protected against the bactericidal effect of {alpha}-defensins. When staphylokinase was added to staphylokinase-negative S. aureus cultures, it almost totally abrogated the effect of {alpha}-defensins. Finally, human neutrophil peptide 2 injected intra-articularly along with bacteria alleviated joint destruction. In this study, we report a new property of staphylokinase, its ability to induce secretion of defensins, to complex bind them and to neutralize their bactericidal effect. Staphylokinase production may therefore be responsible in vivo for defensin resistance during S. aureus infections.




This article has been cited by other articles:


Home page
 MicrobiologyHome page
S. Arafah, M.-L. Rosso, L. Rehaume, R. E. W. Hancock, M. Simonet, and M. Marceau
An iron-regulated LysR-type element mediates antimicrobial peptide resistance and virulence in Yersinia pseudotuberculosis
Microbiology, July 1, 2009; 155(7): 2168 - 2181.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
E. Llobet, J. M. Tomas, and J. A Bengoechea
Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
Microbiology, December 1, 2008; 154(12): 3877 - 3886.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
H. C. Maisey, D. Quach, M. E. Hensler, G. Y. Liu, R. L. Gallo, V. Nizet, and K. S. Doran
A group B streptococcal pilus protein promotes phagocyte resistance and systemic virulence
FASEB J, June 1, 2008; 22(6): 1715 - 1724.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
S. C. Mullaly and P. Kubes
The Role of TLR2 In Vivo following Challenge with Staphylococcus aureus and Prototypic Ligands
J. Immunol., December 1, 2006; 177(11): 8154 - 8163.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
W. J. B. van Wamel, S. H. M. Rooijakkers, M. Ruyken, K. P. M. van Kessel, and J. A. G. van Strijp
The Innate Immune Modulators Staphylococcal Complement Inhibitor and Chemotaxis Inhibitory Protein of Staphylococcus aureus Are Located on {beta}-Hemolysin-Converting Bacteriophages
J. Bacteriol., February 15, 2006; 188(4): 1310 - 1315.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
C. Goerke, J. Koller, and C. Wolz
Ciprofloxacin and Trimethoprim Cause Phage Induction and Virulence Modulation in Staphylococcus aureus
Antimicrob. Agents Chemother., January 1, 2006; 50(1): 171 - 177.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
J. W. McMichael, A. I. Maxwell, K. Hayashi, K. Taylor, W. A. Wallace, J. R. Govan, J. R. Dorin, and J.-M. Sallenave
Antimicrobial Activity of Murine Lung Cells against Staphylococcus aureus Is Increased In Vitro and In Vivo after Elafin Gene Transfer
Infect. Immun., June 1, 2005; 73(6): 3609 - 3617.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
M. Sieprawska-Lupa, P. Mydel, K. Krawczyk, K. Wojcik, M. Puklo, B. Lupa, P. Suder, J. Silberring, M. Reed, J. Pohl, et al.
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases
Antimicrob. Agents Chemother., December 1, 2004; 48(12): 4673 - 4679.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 2004 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 2004 by The American Association of Immunologists, Inc. All rights reserved.