Cited by 160Streptococcal Infections and Treatments Biochemical and Structural Characterization Protease 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

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1515/bc.2011.208

Cites

93 of 93 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The global burden of group A streptococcal diseases
Carapetis, J. R., Steer, A. C., Mulholland, E. K., & Weber, M. (2005) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(05)70267-x · Cited by 2,998
Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope
Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391
Host-Pathogen Interactions: Redefining the Basic Concepts of Virulence and Pathogenicity
Casadevall, A., & Pirofski, L.-A. (1999) · Infection and Immunity · doi:10.1128/iai.67.8.3703-3713.1999 · Cited by 769
Chemokines in pathology and medicine
Baggiolini, M. (2001) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.2001.00867.x · Cited by 677
Many chemokines including CCL20/MIP-3α display antimicrobial activity
Yang, D., Chen, Q., Hoover, D. M., Staley, P., Tucker, K. D., Lubkowski, J., & Oppenheim, J. J. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0103024 · Cited by 464
DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection
Walker, M. J., Hollands, A., Sanderson-Smith, M. L., Cole, J. N., Kirk, J. K., Henningham, A., McArthur, J. D., Dinkla, K., Aziz, R. K., Kansal, R. G., et al. (2007) · Nature Medicine · doi:10.1038/nm1612 · Cited by 426
EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
Collin, M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3046 · Cited by 372
Self-citation
Aspects of Pathogenesis of Serious Group A Streptococcal Infections in Sweden, 1988-1989
Holm, S. E., Norrby, A., Bergholm, A.-M., & Norgren, M. (1992) · Journal of Infectious Diseases · doi:10.1093/infdis/166.1.31 · Cited by 302
Clinical and Microbiological Characteristics of Severe Streptococcus pyogenes Disease in Europe
Luca-Harari, B., Darenberg, J., Neal, S., Siljander, T., Strakova, L., Tanna, A., Creti, R., Ekelund, K., Koliou, M., Tassios, P. T., et al. (2009) · Journal of Clinical Microbiology · doi:10.1128/jcm.02155-08 · Cited by 300
Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease from Streptococcus pyogenes.
Kapur, V, Majesky, M. W., Li, L. L., Black, R. A., & Musser, J. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7676 · Cited by 256
A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
Kapur, V., Topouzis, S., Majesky, M. W., Li, L.-L., Hamrick, M. R., Hamill, R. J., Patti, J. M., & Musser, J. M. (1993) · Microbial Pathogenesis · doi:10.1006/mpat.1993.1083 · Cited by 226
Streptococcal Cysteine Proteinase Releases Biologically Active Fragments of Streptococcal Surface Proteins
Berge, A., & Björck, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.9862 · Cited by 222
Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor
Björck, L., Åkesson, P., Bohus, M., Trojnar, J., Abrahamson, M., Olafsson, I., & Grubb, A. (1989) · Nature · doi:10.1038/337385a0 · Cited by 219
Molecular analysis of the role of the group A streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection.
Ashbaugh, C. D., Warren, H. B., Carey, V. J., & Wessels, M. R. (1998) · Journal of Clinical Investigation · doi:10.1172/jci3065 · Cited by 215
A PROTEOLYTIC ENZYME PRODUCED BY GROUP A STREPTOCOCCI WITH SPECIAL REFERENCE TO ITS EFFECT ON THE TYPE-SPECIFIC M ANTIGEN
Elliott, S. D. (1945) · Journal of Experimental Medicine · doi:10.1084/jem.81.6.573 · Cited by 208
Effect of SpeB and EndoS from Streptococcus pyogenes on Human Immunoglobulins
Collin, M., & Olsén, A. (2001) · Infection and Immunity · doi:10.1128/iai.69.11.7187-7189.2001 · Cited by 203
Self-citation
Molecular and Clinical Characteristics of Invasive Group A Streptococcal Infection in Sweden
Darenberg, J., Luca-Harari, B., Jasir, A., Sandgren, A., Pettersson, H., Schalen, C., Norgren, M., Romanus, V., Norrby-Teglund, A., & Normark, B. H. (2007) · Clinical Infectious Diseases · doi:10.1086/519936 · Cited by 197
Invasive M1T1 group A Streptococcus undergoes a phase‐shift in vivo to prevent proteolytic degradation of multiple virulence factors by SpeB
Aziz, R. K., Pabst, M. J., Jeng, A., Kansal, R., Low, D. E., Nizet, V., & Kotb, M. (2004) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03797.x · Cited by 196
Association of phenotypic and genotypic characteristics of invasive Streptococcus pyogenes isolates with clinical components of streptococcal toxic shock syndrome
Talkington, D. F., Schwartz, B., Black, C. M., Todd, J. K., Elliott, J., Breiman, R. F., & Facklam, R. R. (1993) · Infection and Immunity · doi:10.1128/iai.61.8.3369-3374.1993 · Cited by 195
Understanding how leading bacterial pathogens subvert innate immunity to reveal novel therapeutic targets
Nizet, V. (2007) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2007.06.005 · Cited by 194
Streptococcal cysteine proteinase releases kinins: a virulence mechanism.
Herwald, H., Collin, M., Müller-Esterl, W., & Björck, L. (1996) · The Journal of experimental medicine · doi:10.1084/jem.184.2.665 · Cited by 190
Self-citation
Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains.
Lukomski, S., Sreevatsan, S., Amberg, C., Reichardt, W., Woischnik, M., Podbielski, A., & Musser, J. M. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119445 · Cited by 179
Inverse Relation between Disease Severity and Expression of the Streptococcal Cysteine Protease, SpeB, among Clonal M1T1 Isolates Recovered from Invasive Group A Streptococcal Infection Cases
Kansal, R. G., McGeer, A., Low, D. E., Norrby‐Teglund, A., & Kotb, M. (2000) · Infection and Immunity · doi:10.1128/.68.11.6362-6369.2000 · Cited by 179
Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial α‐defensin
Schmidtchen, A., Frick, I., & Björck, L. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02251.x · Cited by 160
Extracellular Cysteine Protease Produced by Streptococcus pyogenes Participates in the Pathogenesis of Invasive Skin Infection and Dissemination in Mice
Łukomski, S., Montgomery, C. A., Rurangirwa, J., Geske, R. S., Barrish, J. P., Adams, G. J., & Musser, J. M. (1999) · Infection and Immunity · doi:10.1128/iai.67.4.1779-1788.1999 · Cited by 155
Trigger for group A streptococcal M1T1 invasive disease
Cole, J. N., McArthur, J. D., McKay, F. C., Sanderson‐Smith, M. L., Cork, A. J., Ranson, M., Rohde, M., Itzek, A., Sun, H., Ginsburg, D., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-5804fje · Cited by 154
Molecular Pathogenesis of Necrotizing Fasciitis
Olsen, R. J., & Musser, J. M. (2009) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-121808-102135 · Cited by 142
Group A Streptococcal Cysteine Protease Degrades C3 (C3b) and Contributes to Evasion of Innate Immunity
Terao, Y., Mori, Y., Yamaguchi, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704821200 · Cited by 135
EndoS and SpeB fromStreptococcus pyogenesInhibit Immunoglobulin-Mediated Opsonophagocytosis
Collin, M., Svensson, M. D., Sjöholm, A. G., Jensenius, J. C., Sjöbring, U., & Olsén, A. (2002) · Infection and Immunity · doi:10.1128/iai.70.12.6646-6651.2002 · Cited by 131
Self-citation
Genetic Inactivation of an Extracellular Cysteine Protease (SpeB) Expressed byStreptococcus pyogenesDecreases Resistance to Phagocytosis and Dissemination to Organs
Łukomski, S., Burns, E. H., Wyde, P. R., Podbielski, A., Rurangirwa, J., Moore‐Poveda, D. K., & Musser, J. M. (1998) · Infection and Immunity · doi:10.1128/iai.66.2.771-776.1998 · Cited by 130
Role of Streptococcal Pyrogenic Exotoxin B in the Mouse Model of Group A Streptococcal Infection
Kuo, C.-F., Wu, J.-J., Lin, K.-Y., Tsai, P.-J., Lee, S.-C., Jin, Y., Lei, H.-Y., & Lin, Y.-S. (1998) · Infection and Immunity · doi:10.1128/iai.66.8.3931-3935.1998 · Cited by 124
Rapidly progressive soft tissue infections
Vinh, D. C., & Embil, J. M. (2005) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(05)70191-2 · Cited by 123
Vaccination with streptococcal extracellular cysteine protease (interleukin-1β convertase) protects mice against challenge with heterologous group A streptococci
Kapur, V., Maffei, J. T., Greer, R. S., Li, L., Adams, G. J., & Musser, J. M. (1994) · Microbial Pathogenesis · doi:10.1006/mpat.1994.1044 · Cited by 120
Streptococcal Protein H Forms Soluble Complement-activating Complexes with IgG, but Inhibits Complement Activation by IgG-coated Targets
Berge, A., Kihlberg, B., Sjöholm, A. G., & Björck, L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20774 · Cited by 114
Activation of a 66-kilodalton human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine protease
Burns, E. H., Marciel, A. M., & Musser, J. M. (1996) · Infection and Immunity · doi:10.1128/iai.64.11.4744-4750.1996 · Cited by 112
Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine protease
Kagawa, T. F., Cooney, J. C., Baker, H. M., McSweeney, S. M., Liu, M., Gubba, S., Musser, J. M., & Baker, E. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040549997 · Cited by 108
A natural variant of the cysteine protease virulence factor of group A Streptococcus with an arginine-glycine-aspartic acid (RGD) motif preferentially binds human integrins α v β 3 and α IIb β 3
Stockbauer, K. E., Magoun, L., Liu, M., Burns, E. H., Gubba, S., Renish, S., Pan, X., Bodary, S. C., Baker, E. K., Coburn, J., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.242 · Cited by 103
Role for Serine Protease HtrA (DegP) ofStreptococcus pyogenesin the Biogenesis of Virulence Factors SpeB and the Hemolysin Streptolysin S
Lyon, W. R., & Caparon, M. G. (2004) · Infection and Immunity · doi:10.1128/iai.72.3.1618-1625.2004 · Cited by 102
Decreased necrotizing fasciitis capacity caused by a single nucleotide mutation that alters a multiple gene virulence axis
Olsen, R. J., Sitkiewicz, I., Ayeras, A. A., Gonulal, V. E., Cantu, C. C., Beres, S. B., Green, N. M., Lei, B., Humbird, T. L., Greaver, J. L., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911811107 · Cited by 101
The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strepadhesin, laminin‐binding and cysteine protease activity
Hytönen, J., Haataja, S., Gerlach, D., Podbielski, A., & Finne, J. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02269.x · Cited by 97
Frequency of the erythrogenic toxin B and C genes (speB and speC) among clinical isolates of group A streptococci
Yu, C. E., & Ferretti, J. J. (1991) · Infection and Immunity · doi:10.1128/iai.59.1.211-215.1991 · Cited by 96
α2-Macroglobulin-Proteinase Complexes Protect Streptococcus pyogenes from Killing by the Antimicrobial Peptide LL-37
Nyberg, P. B., Rasmussen, M., & Björck, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400485200 · Cited by 94
Reciprocal, Temporal Expression of SpeA and SpeB by Invasive M1T1 Group A Streptococcal Isolates In Vivo
Kazmi, S. U., Kansal, R. G., Aziz, R. K., Hooshdaran, M. Z., Norrby‐Teglund, A., Low, D. E., Halim, A., & Kotb, M. (2001) · Infection and Immunity · doi:10.1128/iai.69.8.4988-4995.2001 · Cited by 93
THE CRYSTALLIZATION AND SEROLOGICAL DIFFERENTIATION OF A STREPTOCOCCAL PROTEINASE AND ITS PRECURSOR
Elliott, S. D. (1950) · The Journal of Experimental Medicine · doi:10.1084/jem.92.3.201 · Cited by 91
A secreted streptococcal cysteine protease can cleave a surface-expressed M1 protein and alter the immunoglobulin binding properties
Raeder, R., Woischnik, M., Podbielski, A., et al. (1998) · Research in Microbiology · doi:10.1016/s0923-2508(99)80001-1 · Cited by 88
From transcription to activation: how group A streptococcus, the flesh‐eating pathogen, regulates SpeB cysteine protease production
Carroll, R. K., & Musser, J. M. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07709.x · Cited by 87
AN INACTIVE PRECURSOR OF STREPTOCOCCAL PROTEINASE
Elliott, S. D., & Dole, V. P. (1947) · The Journal of Experimental Medicine · doi:10.1084/jem.85.3.305 · Cited by 86
Extracellular Enzymes with Immunomodulating Activities: Variations on a Theme inStreptococcus pyogenes
Collin, M., & Olsén, A. (2003) · Infection and Immunity · doi:10.1128/iai.71.6.2983-2992.2003 · Cited by 86
Self-citation
Group A Streptococcus Induces Apoptosis in Human Epithelial Cells
Tsai, P.-J., Lin, Y.-S., Kuo, C.-F., Lei, H.-Y., & Wu, J.-J. (1999) · Infection and Immunity · doi:10.1128/iai.67.9.4334-4339.1999 · Cited by 86
Streptococcal Proteinase: the Zymogen to Enzyme Transformation
Liu, T., & Elliott, S. D. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97551-4 · Cited by 85
Isolation and characterization of erythrogenic toxins V. Communication: Identity of erythrogenic toxin type B and Streptococcal proteinase precursor
Gerlach, D., Knöll, H., Köhler, W., Ozegowski, J., & Hřı́balová, V. (1983) · Zentralblatt für Bakteriologie Mikrobiologie und Hygiene 1 Abt Originale A Medizinische Mikrobiologie Infektionskrankheiten und Parasitologie · doi:10.1016/s0174-3031(83)80161-9 · Cited by 85
Role for a secreted cysteine proteinase in the establishment of host tissue tropism by group A streptococci
Svensson, M. D., Scaramuzzino, D. A., Sjöbring, U., Olsén, A., Frank, C. F., & Bessen, D. E. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02144.x · Cited by 82
Roles of the plasminogen activator streptokinase and the plasminogen-associated M protein in an experimental model for streptococcal impetigo
Svensson, M. D., Sjöbring, U., Luo, F. H., & Bessen, D. E. (2002) · Microbiology · doi:10.1099/00221287-148-12-3933 · Cited by 78
Dispersal of Group A Streptococcal Biofilms by the Cysteine Protease SpeB Leads to Increased Disease Severity in a Murine Model
Connolly, K. L., Roberts, A. L., Holder, R. C., & Reid, S. D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018984 · Cited by 77
Chemical Properties of Streptococcal Proteinase and Its Zymogen
Liu, T., Neumann, N. P., Elliott, S. D., Moore, S., & Stein, W. H. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83988-1 · Cited by 76
Autocatalytic processing of the streptococcal cysteine protease zymogen
Doran, J., Nomizu, M., Takebe, S., Menard, R., Griffith, D. W., & Ziomek, E. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00473.x · Cited by 69
Cleavage of Antigen-Bound Immunoglobulin G by SpeB Contributes to Streptococcal Persistence in Opsonizing Blood
Eriksson, A., & Norgren, M. (2002) · Infection and Immunity · doi:10.1128/iai.71.1.211-217.2003 · Cited by 68
SpeB of Streptococcus pyogenes Differentially Modulates Antibacterial and Receptor Activating Properties of Human Chemokines
Egesten, A., Olin, A. I., Linge, H. M., Yadav, M. C., Mörgelin, M., Karlsson, A., & Collin, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004769 · Cited by 65
Self-citation
Purification and Characterization of a Novel Cysteine Proteinase (Periodontain) from Porphyromonas gingivalis
Nelson, D. C., Potempa, J., Kordula, T., & Travis, J. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12245 · Cited by 62
Self-citation
Streptococcal pyrogenic exotoxin B cleaves properdin and inhibits complement-mediated opsonophagocytosis
Tsao, N., Tsai, W.-H., Lin, Y.-S., Chuang, W., Wang, C.-H., & Kuo, C.-F. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.078 · Cited by 62
Proapoptotic Effect of Proteolytic Activation of Matrix Metalloproteinases byStreptococcus pyogenesThiol Proteinase (StreptococcusPyrogenic Exotoxin B)
Tamura, F., Nakagawa, R., Akuta, T., Okamoto, S., Hamada, S., Maeda, H., Kawabata, S., & Akaike, T. (2004) · Infection and Immunity · doi:10.1128/iai.72.8.4836-4847.2004 · Cited by 61
Degradation of Complement 3 by Streptococcal Pyrogenic Exotoxin B Inhibits Complement Activation and Neutrophil Opsonophagocytosis
Kuo, C.-F., Lin, Y.-S., Chuang, W., Wu, J.-J., & Tsao, N. (2008) · Infection and Immunity · doi:10.1128/iai.01116-07 · Cited by 60
Streptococcal cysteine protease augments lung injury induced by products of group A streptococci
Shanley, T. P., Schrier, D. J., Kapur, V., Kehoe, M., Musser, J. M., & Ward, P. A. (1996) · Infection and Immunity · doi:10.1128/iai.64.3.870-877.1996 · Cited by 59
Expression and Characterization of Group AStreptococcusExtracellular Cysteine Protease Recombinant Mutant Proteins and Documentation of Seroconversion during Human Invasive Disease Episodes
Gubba, S., Low, D. E., & Musser, J. M. (1998) · Infection and Immunity · doi:10.1128/iai.66.2.765-770.1998 · Cited by 57
Fibrinogen Cleavage by the Streptococcus pyogenes Extracellular Cysteine Protease and Generation of Antibodies That Inhibit Enzyme Proteolytic Activity
Matsuka, Y. V., Pillai, S., Gubba, S., Musser, J. M., & Olmsted, S. B. (1999) · Infection and Immunity · doi:10.1128/iai.67.9.4326-4333.1999 · Cited by 57
Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing
Musser, J. M., Stockbauer, K. E., Kapur, V., & Rudgers, G. W. (1996) · Infection and Immunity · doi:10.1128/iai.64.6.1913-1917.1996 · Cited by 57
Characterization of an Extracellular Virulence FactorMade by Group A Streptococcus with Homology to the Listeria monocytogenes Internalin Family ofProteins
Reid, S. D., Montgomery, A. G., Voyich, J. M., DeLeo, F. R., Lei, B., Ireland, R. M., Green, N. M., Liu, M., Lukomski, S., & Musser, J. M. (2003) · Infection and Immunity · doi:10.1128/iai.71.12.7043-7052.2003 · Cited by 54
Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain.
Tai, J. Y., Kortt, A. A., Liu, T. Y., & Elliott, S. D. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33640-2 · Cited by 54
Different forms of streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin: cleavage by streptococcal cysteine protease
Pinkney, M., Kapur, V., Smith, J. J., et al. (1995) · Infection and Immunity · doi:10.1128/iai.63.7.2776-2779.1995 · Cited by 51
Absence of a Cysteine Protease Effect on Bacterial Virulence in Two Murine Models of Human Invasive Group A Streptococcal Infection
Ashbaugh, C. D., & Wessels, M. R. (2001) · Infection and Immunity · doi:10.1128/iai.69.11.6683-6686.2001 · Cited by 51
Cloning of the gene, speB, for streptococcal pyrogenic exotoxin type B in Escherichia coli
Bohach, G. A., Hauser, A. R., & Schlievert, P. M. (1988) · Infection and Immunity · doi:10.1128/iai.56.6.1665-1667.1988 · Cited by 49
Activation of Streptococcal Proteinase and its Zymogen by Bacterial Cell Walls
LIU, T. Y., & Elliott, S. D. (1965) · Nature · doi:10.1038/206033a0 · Cited by 48
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1
Nyberg, P. B., Rasmussen, M., von Pawel‐Rammingen, U., & Björck, L. (2004) · Microbiology · doi:10.1099/mic.0.27076-0 · Cited by 48
Absence of SpeB Production in Virulent Large Capsular Forms of Group A Streptococcal Strain 64
Raeder, R., Harokopakis, E., Hollingshead, S. K., & Boyle, M. D. P. (2000) · Infection and Immunity · doi:10.1128/iai.68.2.744-751.2000 · Cited by 48
Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface.
Wolf, B. B., Gibson, C. A., Kapur, V., Hussaini, I. M., Musser, J. M., & Gonias, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43867-7 · Cited by 47
Inactivation of the streptococcal erythrogenic toxin B gene (speB) in Streptococcus pyogenes
Chaussee, M. S., Gerlach, D., Yu, C. E., & Ferretti, J. J. (1993) · Infection and Immunity · doi:10.1128/iai.61.9.3719-3723.1993 · Cited by 44
EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity
Allhorn, M., Olsén, A., & Collin, M. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-3 · Cited by 42
Self-citation
Impact of the SpeB Protease on Binding of the Complement Regulatory Proteins Factor H and Factor H-Like Protein 1 byStreptococcus pyogenes
Wei, L., Pandiripally, V., Gregory, E. J., Clymer, M., & Cue, D. R. (2005) · Infection and Immunity · doi:10.1128/iai.73.4.2040-2050.2005 · Cited by 38
Purification and characteristics of the streptococcal chemotactic factor inactivator
Wexler, D. E., & Cleary, P. P. (1985) · Infection and Immunity · doi:10.1128/iai.50.3.757-764.1985 · Cited by 37
Streptococcal Mitogenic Exotoxin, SmeZ, Is the Most Susceptible M1T1 Streptococcal Superantigen to Degradation by the Streptococcal Cysteine Protease, SpeB
Nooh, M. M., Aziz, R. K., Kotb, M., Eroshkin, A. M., Chuang, W.-J., Proft, T., & Kansal, R. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605544200 · Cited by 37
The Membrane Bound LRR Lipoprotein Slr, and the Cell Wall-Anchored M1 Protein from Streptococcus pyogenes Both Interact with Type I Collagen
Bober, M., Mörgelin, M., Olin, A. I., von Pawel‐Rammingen, U., & Collin, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020345 · Cited by 37
Self-citation
Separation of mitogenic and pyrogenic activities from so-called erythrogenic toxin type B (Streptococcal Proteinase)
Gerlach, D., Reichardt, W., Fleischer, B., & Schmidt, K. (1994) · Zentralblatt für Bakteriologie · doi:10.1016/s0934-8840(11)80510-4 · Cited by 36
Group A streptococcal sepsis
Stevens, D. L. (2003) · Current Infectious Disease Reports · doi:10.1007/s11908-003-0017-7 · Cited by 36
SpeB–Spi: a novel protease–inhibitor pair fromStreptococcus pyogenes
Kagawa, T. F., O’Toole, P. W., & Cooney, J. C. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04708.x · Cited by 33
Cysteine Protease Activity and Histamine Release from the Human Mast Cell Line HMC-1 Stimulated by Recombinant Streptococcal Pyrogenic Exotoxin B/Streptococcal Cysteine Protease
Watanabe, Y., Todome, Y., Ohkuni, H., Sakurada, S., Ishikawa, T., Yutsudo, T., Fischetti, V. A., & Zabriskie, J. B. (2002) · Infection and Immunity · doi:10.1128/iai.70.7.3944-3947.2002 · Cited by 33
Substrate Specificity of the Streptococcal Cysteine Protease
Nomizu, M., Pietrzyński, G., Kato, T., Lachance, P., Menard, R., & Ziomek, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106306200 · Cited by 31
Solution Structure and Backbone Dynamics of Streptopain
Wang, C., Houng, H.-C., Chen, C.-L., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807624200 · Cited by 23
Streptococcal Proteinase-catalyzed Hydrolysis of Some Ester and Amide Substrates
Liu, T., Nomura, N., Jonsson, E. K., & Wallace, B. G. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63622-1 · Cited by 21
Structure of the Mature Streptococcal Cysteine Protease Exotoxin mSpeB in Its Active Dimeric Form
Olsen, J. G., Dagil, R., Niclasen, L. M., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.046 · Cited by 21
The dissemination of C10 cysteine protease genes in Bacteroides fragilis by mobile genetic elements
Thornton, R. F., Kagawa, T. F., O’Toole, P. W., & Cooney, J. C. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-122 · Cited by 19
Inactivation of the cysteine protease SpeB affects hyaluronic acid capsule expression in group A streptococci
Woischnik, M., Buttaro, B. A., & Podbielski, A. (2000) · Microbial Pathogenesis · doi:10.1006/mpat.1999.0341 · Cited by 17
Replacement of Histidine 340 with Alanine Inactivates the Group A Streptococcus Extracellular Cysteine Protease Virulence Factor
Gubba, S., Cipriano, V. J., & Musser, J. M. (2000) · Infection and Immunity · doi:10.1128/iai.68.6.3716-3719.2000 · Cited by 15
Streptococcal pyogenic exotoxin B (SpeB) boosts the contact system via binding of α-1 antitrypsin
Niclasen, L. M., Olsen, J. G., Dagil, R., Zhang, Q., Sørensen, O. E., & Kragelund, B. B. (2010) · Biochemical Journal · doi:10.1042/bj20100984 · Cited by 9

Research works printed but not linked: 2

Gerlach D., 1983, Zentralbl. Bakteriol. Mikrobiol. Hyg. A, 225, 221
10.1128/IAI.68.11.6362-6369.2000 · doi:10.1128/iai.68.11.6362-6369.2000 · Paper page

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

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: Nelson, Daniel C.
Collin, Mattias
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

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.

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources