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
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chaussee, M. S.
Right arrow Articles by van Putten, J. P. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chaussee, M. S.
Right arrow Articles by van Putten, J. P. M.

 Previous Article  |  Next Article 

Infection and Immunity, June 2000, p. 3226-3232, Vol. 68, No. 6
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Streptococcal Erythrogenic Toxin B Abrogates Fibronectin-Dependent Internalization of Streptococcus pyogenes by Cultured Mammalian Cells

Michael S. Chaussee,1,* Robert L. Cole,1 and Jos P. M. van Putten1,2

Laboratory of Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840,1 and Institute of Infectious Diseases and Immunology, University of Utrecht, NL-3584 CL Utrecht, The Netherlands2

Received 18 January 2000/Returned for modification 23 February 2000/Accepted 20 March 2000

Streptococcus pyogenes secretes several proteins that influence host-pathogen interactions. A tissue-culture model was used to study the influence of the secreted cysteine protease streptococcal erythrogenic toxin B (SPE B) on the interaction between S. pyogenes strain NZ131 (serotype M49) and mammalian cells. Inactivation of the speB gene enhanced fibronectin-dependent uptake of the pathogen by Chinese hamster ovary (CHO-K1) cells compared to that in the isogenic wild-type strain. Preincubation of the NZ131 speB mutant with purified SPE B protease significantly inhibited fibronectin-dependent uptake by both CHO-K1 and CHO-pgs745 cells. The effect was attributed to an abrogation of fibronectin binding to the surface of the bacteria that did not involve either the M49 protein or the streptococcal fibronectin-binding protein SfbI. In contrast, pretreatment of the NZ131 speB mutant with SPE B did not influence sulfated polysaccharide-mediated uptake by CHO-pgs745 cells. The results indicate that the SPE B protease specifically alters bacterial cell surface proteins and thereby influences pathogen uptake.


* Corresponding author. Mailing address: Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 903 South Fourth St., Hamilton, MT 59840. Phone: (406) 363-9306. Fax: (406) 363-9204. E-mail: mchaussee{at}nih.gov.


Infection and Immunity, June 2000, p. 3226-3232, Vol. 68, No. 6
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Wang, C.-C., Houng, H.-C., Chen, C.-L., Wang, P.-J., Kuo, C.-F., Lin, Y.-S., Wu, J.-J., Lin, M. T., Liu, C.-C., Huang, W., Chuang, W.-J. (2009). Solution Structure and Backbone Dynamics of Streptopain: INSIGHT INTO DIVERSE SUBSTRATE SPECIFICITY. J. Biol. Chem. 284: 10957-10967 [Abstract] [Full Text]  
  • McShan, W. M., Ferretti, J. J., Karasawa, T., Suvorov, A. N., Lin, S., Qin, B., Jia, H., Kenton, S., Najar, F., Wu, H., Scott, J., Roe, B. A., Savic, D. J. (2008). Genome Sequence of a Nephritogenic and Highly Transformable M49 Strain of Streptococcus pyogenes. J. Bacteriol. 190: 7773-7785 [Abstract] [Full Text]  
  • Wei, L., Pandiripally, V., Gregory, E., Clymer, M., Cue, D. (2005). Impact of the SpeB Protease on Binding of the Complement Regulatory Proteins Factor H and Factor H-Like Protein 1 by Streptococcus pyogenes. Infect. Immun. 73: 2040-2050 [Abstract] [Full Text]  
  • Yavlovich, A., Katzenell, A., Tarshis, M., Higazi, A. A.-R., Rottem, S. (2004). Mycoplasma fermentans Binds to and Invades HeLa Cells: Involvement of Plasminogen and Urokinase. Infect. Immun. 72: 5004-5011 [Abstract] [Full Text]  
  • Nyberg, P., Rasmussen, M., von Pawel-Rammingen, U., Bjorck, L. (2004). SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1. Microbiology 150: 1559-1569 [Abstract] [Full Text]  
  • Marouni, M. J., Sela, S. (2003). The luxS Gene of Streptococcus pyogenes Regulates Expression of Genes That Affect Internalization by Epithelial Cells. Infect. Immun. 71: 5633-5639 [Abstract] [Full Text]  
  • Rottem, S. (2003). Interaction of Mycoplasmas With Host Cells. Physiol. Rev. 83: 417-432 [Abstract] [Full Text]  
  • Eriksson, A., Norgren, M. (2003). Cleavage of Antigen-Bound Immunoglobulin G by SpeB Contributes to Streptococcal Persistence in Opsonizing Blood. Infect. Immun. 71: 211-217 [Abstract] [Full Text]  
  • Pandiripally, V., Gregory, E., Cue, D. (2002). Acquisition of Regulators of Complement Activation by Streptococcus pyogenes Serotype M1. Infect. Immun. 70: 6206-6214 [Abstract] [Full Text]  
  • Jadoun, J., Eyal, O., Sela, S. (2002). Role of CsrR, Hyaluronic Acid, and SpeB in the Internalization of Streptococcus pyogenes M Type 3 Strain by Epithelial Cells. Infect. Immun. 70: 462-469 [Abstract] [Full Text]  
  • Chaussee, M. S., Sylva, G. L., Sturdevant, D. E., Smoot, L. M., Graham, M. R., Watson, R. O., Musser, J. M. (2002). Rgg Influences the Expression of Multiple Regulatory Loci To Coregulate Virulence Factor Expression in Streptococcus pyogenes. Infect. Immun. 70: 762-770 [Abstract] [Full Text]  
  • Yavlovich, A., Higazi, A. A.-R., Rottem, S. (2001). Plasminogen Binding and Activation by Mycoplasma fermentans. Infect. Immun. 69: 1977-1982 [Abstract] [Full Text]  
  • Chaussee, M. S., Watson, R. O., Smoot, J. C., Musser, J. M. (2001). Identification of Rgg-Regulated Exoproteins of Streptococcus pyogenes. Infect. Immun. 69: 822-831 [Abstract] [Full Text]