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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 392, Issue 12

Issues

Cysteine proteinase SpeB from Streptococcus pyogenes – a potent modifier of immunologically important host and bacterial proteins

Daniel C. Nelson
  • Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, MD, USA
  • Department of Veterinary Medicine, Virginia-Maryland Regional College of Veterinary Medicine, College Park, MD, USA
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Julia Garbe
  • Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Mattias Collin

Abstract

Group A streptococcus (Streptococcus pyogenes) is an exclusively human pathogen that causes a wide spectrum of diseases ranging from pharyngitis, to impetigo, to toxic shock, to necrotizing fasciitis. The diversity of these disease states necessitates that S. pyogenes possess the ability to modulate both the innate and adaptive immune responses. SpeB, a cysteine proteinase, is the predominant secreted protein from S. pyogenes. Because of its relatively indiscriminant specificity, this enzyme has been shown to degrade the extracellular matrix, cytokines, chemokines, complement components, immunoglobulins, and serum protease inhibitors, to name but a few of the known substrates. Additionally, SpeB regulates other streptococcal proteins by degrading them or releasing them from the bacterial surface. Despite the wealth of literature on putative SpeB functions, there remains much controversy about this enzyme because many of reported activities would produce contradictory physiological results. Here we review all known host and bacterial protein substrates for SpeB, their cleavage sites, and discuss the role of this enzyme in streptococcal pathogenesis based on the current literature.

Keywords: animal models; C10 cysteine proteinase; human infection; immune evasion; proteolysis; SpeB; streptococcal cysteine proteinase; streptopain; virulence

About the article

Corresponding authors


Received: 2011-09-05

Accepted: 2011-09-26

Published in Print: 2011-12-01


Citation Information: Biological Chemistry, Volume 392, Issue 12, Pages 1077–1088, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2011.208.

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©2011 by Walter de Gruyter Berlin Boston.Get Permission

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