JBC Ideal method for primary cell transfection

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


     


Originally published In Press as doi:10.1074/jbc.M301995200 on March 5, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16561-16566, May 9, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/19/16561    most recent
M301995200v1
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 Email this article to a friend
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 reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Frick, I.-M.
Right arrow Articles by Björck, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Frick, I.-M.
Right arrow Articles by Björck, L.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

SIC, a Secreted Protein of Streptococcus pyogenes That Inactivates Antibacterial Peptides*

Inga-Maria FrickDagger §, Per Åkesson, Magnus RasmussenDagger , Artur Schmidtchen, and Lars BjörckDagger

From the Dagger  Section for Molecular Pathogenesis, Department of Cell and Molecular Biology, Lund University, and the  Department of Medical Microbiology, Dermatology, and Infection, Lund University Hospital, S-221 85 Lund, Sweden

Some isolates of the significant human pathogen Streptococcus pyogenes, including virulent strains of the M1 serotype, secrete protein SIC. This molecule, secreted in large quantities, interferes with complement function. As a result of natural selection, SIC shows a high degree of variation. Here we provide a plausible explanation for this variation and the fact that strains of the M1 serotype are the most frequent cause of severe invasive S. pyogenes infections. Thus, protein SIC was found to inactivate human neutrophil alpha -defensin and LL-37, two major antibacterial peptides involved in bacterial clearance. This inactivation protected S. pyogenes against the antibacterial effect of the peptides. Moreover, SIC isolated from S. pyogenes of the M1 serotype was more powerful in this respect than SIC variants from strains of M serotypes 12 and 55, serotypes rarely connected with invasive infections.


* This work was supported by grants from the Swedish Research Council (Projects 7480, 13471, and 14379), the Foundations of Crafoord, Bergvall, and Österlund, and the Royal Physiographic Society.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Cell and Molecular Biology, Lund University, BMC, B14, Tornavägen 10, S-221 84 Lund, Sweden. Tel.: 46-46-222-8569; Fax: 46-46-157756; E-mail: Inga-Maria.Frick@medkem.lu.se.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


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. Bacteriol.Home page
V. Sagar, R. Kumar, N. K. Ganguly, T. Menon, and A. Chakraborti
DRS Is Far Less Divergent than Streptococcal Inhibitor of Complement of Group A Streptococcus
J. Bacteriol., April 1, 2007; 189(7): 2933 - 2935.
[Abstract] [Full Text] [PDF]


Home page
CVIHome page
L. Maripuu, A. Eriksson, B. Eriksson, K. Pauksen, S. Holm, and M. Norgren
Dynamics of the Immune Response against Extracellular Products of Group A Streptococci during Infection
Clin. Vaccine Immunol., January 1, 2007; 14(1): 44 - 51.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Pathol.Home page
M. R. Graham, K. Virtaneva, S. F. Porcella, D. J. Gardner, R. D. Long, D. M. Welty, W. T. Barry, C. A. Johnson, L. D. Parkins, F. A. Wright, et al.
Analysis of the Transcriptome of Group A Streptococcus in Mouse Soft Tissue Infection
Am. J. Pathol., September 1, 2006; 169(3): 927 - 942.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
S. A. Shelburne III, P. Sumby, I. Sitkiewicz, N. Okorafor, C. Granville, P. Patel, J. Voyich, R. Hull, F. R. DeLeo, and J. M. Musser
Maltodextrin utilization plays a key role in the ability of group a streptococcus to colonize the oropharynx.
Infect. Immun., August 1, 2006; 74(8): 4605 - 4614.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
L. I. Pahlman, M. Morgelin, J. Eckert, L. Johansson, W. Russell, K. Riesbeck, O. Soehnlein, L. Lindbom, A. Norrby-Teglund, R. R. Schumann, et al.
Streptococcal M Protein: A Multipotent and Powerful Inducer of Inflammation
J. Immunol., July 15, 2006; 177(2): 1221 - 1228.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. A. Shelburne III, P. Sumby, I. Sitkiewicz, C. Granville, F. R. DeLeo, and J. M. Musser
Central role of a bacterial two-component gene regulatory system of previously unknown function in pathogen persistence in human saliva
PNAS, November 1, 2005; 102(44): 16037 - 16042.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
S. A. Kristian, V. Datta, C. Weidenmaier, R. Kansal, I. Fedtke, A. Peschel, R. L. Gallo, and V. Nizet
D-Alanylation of Teichoic Acids Promotes Group A Streptococcus Antimicrobial Peptide Resistance, Neutrophil Survival, and Epithelial Cell Invasion
J. Bacteriol., October 1, 2005; 187(19): 6719 - 6725.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
S. A. Shelburne III, C. Granville, M. Tokuyama, I. Sitkiewicz, P. Patel, and J. M. Musser
Growth Characteristics of and Virulence Factor Production by Group A Streptococcus during Cultivation in Human Saliva
Infect. Immun., August 1, 2005; 73(8): 4723 - 4731.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. J. Binks, B. A. Fernie-King, D. J. Seilly, P. J. Lachmann, and K. S. Sriprakash
Attribution of the Various Inhibitory Actions of the Streptococcal Inhibitor of Complement (SIC) to Regions within the Molecule
J. Biol. Chem., May 20, 2005; 280(20): 20120 - 20125.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
M. Tanaka, T. Hasegawa, A. Okamoto, K. Torii, and M. Ohta
Effect of Antibiotics on Group A Streptococcus Exoprotein Production Analyzed by Two-Dimensional Gel Electrophoresis
Antimicrob. Agents Chemother., January 1, 2005; 49(1): 88 - 96.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Nyberg, M. Rasmussen, and L. Bjorck
{alpha}2-Macroglobulin-Proteinase Complexes Protect Streptococcus pyogenes from Killing by the Antimicrobial Peptide LL-37
J. Biol. Chem., December 17, 2004; 279(51): 52820 - 52823.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.