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Cited by 160Streptococcal Infections and TreatmentsBiochemical and Structural CharacterizationProtease and Inhibitor Mechanisms

The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.

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

Nelson, Daniel C., Garbe, Julia, Collin, Mattias·2011·bchm
DOI 10.1515/bc.2011.208
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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.

Overview

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Crossref · 10.1515/bc.2011.208

Cites

93 of 93 references verified0 citation errors · 0 not checkable

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Citations

Cites

Show all 93 references

Research works printed but not linked: 1

  1. Gerlach D., 1983, Zentralbl. Bakteriol. Mikrobiol. Hyg. A, 225, 221

Cited by

  • Epidermal hepcidin is required for neutrophil response to bacterial infection

    Malerba, M., Louis, S., Cuvellier, S., Shambat, S. M., Hua, C., Gomart, C., Fouet, A., Ortonne, N., Decousser, J.-W., Zinkernagel, A. S., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci126645 · Cited by 55

    “One of the principal mechanisms of GAS-immune escape is the production of 6 surface-associated serine proteases by GAS, such as SpyCEP (also designated ScpC), that 7 cleaves human IL-8/mouse CXCL1 to suppress chemokine-mediated neutrophil recruitment 8 (17) or SpeB, which allows GAS to translocate across the epithelia…”
    Background

See all 160

Metadata

Authors
Nelson, D. C., Garbe, J., & Collin, M.
Affiliations
  • Virginia–Maryland College of Veterinary Medicine (US)
  • Lund University (SE)
Corresponding author
Nelson, Daniel C.
ORCID
Venue
bchm
Publisher
Walter de Gruyter GmbH
Published
2011-12-01
Volume
392
Issue
12
Pages
1077-1088
ISSN
  • 1431-6730 (ISSN-L)
  • 1437-4315
DOI
10.1515/bc.2011.208
OpenAlex
W2012365327
Cited by
160
References
93
Citations by year
2026: 2 · 2025: 7 · 2024: 14 · 2023: 14 · 2022: 8 · 2021: 10 · 2020: 9 · 2019: 16 · 2018: 8 · 2017: 12 · 2016: 17 · 2015: 11 · 2014: 15 · 2013: 10 · 2012: 7
FWCI
1.57
Type
journal article
Language
en
Open access
closed
Locations
  • Biological Chemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Lund University Publications (Lund University) (submittedVersion)
Topics
  • Health Sciences › Medicine › Infectious Diseases › Streptococcal Infections and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
SpeB, cysteine protease, Streptococcus pyogenes, protein degradation, host immune modulation, bacterial virulence, secreted proteins, cleavage site, complement proteins, immunoglobulins, serum protease inhibitors, cytokines and chemokines, extracellular matrix, streptococcal pathogenesis
MeSH terms
Animals, Bacterial Proteins, Exotoxins, Humans

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CoChat. (2026). Citation check: Cysteine proteinase SpeB from Streptococcus pyogenes – a potent modifier of immunologically important host and bacterial proteins. https://app.cochat.ai/papers/10.1515/bc.2011.208
The paper
Nelson, D. C., Garbe, J., & Collin, M. (2011). Cysteine proteinase SpeB from Streptococcus pyogenes – a potent modifier of immunologically important host and bacterial proteins. bchm. https://doi.org/10.1515/bc.2011.208

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.