A novel, anchorless streptococcal surface protein that binds to human immunoglobulins

Kawabata, Shigetada; Tamura, Yasuharu; Murakami, Jumpei; Terao, Yutaka; Nakagawa, Ichirô; Hamada, Shigeyuki

doi:10.1016/s0006-291x(02)02078-8

Cited by 37 publications

(29 citation statements)

References 23 publications

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“…The IgG-degrading enzyme of S. pyogenes (IdeS), also known as Mac-1, Sib35, and MspA, inhibits phagocytosis, neutrophil activation, and the release of reactive oxygen species by binding Fc receptor CD16 (Fc␥RIIIB) on the surface of neutrophils (242,243). IdeS exhibits cysteine protease activity and contributes to opsonophagocytosis resistance in whole human blood by cleaving the lower Fc region of surfacebound human IgG (244).…”

Section: Resistance To Opsonophagocytosismentioning

confidence: 99%

Disease Manifestations and Pathogenic Mechanisms of Group A Streptococcus

et al. 2014

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SUMMARY Streptococcus pyogenes , also known as group A Streptococcus (GAS), causes mild human infections such as pharyngitis and impetigo and serious infections such as necrotizing fasciitis and streptococcal toxic shock syndrome. Furthermore, repeated GAS infections may trigger autoimmune diseases, including acute poststreptococcal glomerulonephritis, acute rheumatic fever, and rheumatic heart disease. Combined, these diseases account for over half a million deaths per year globally. Genomic and molecular analyses have now characterized a large number of GAS virulence determinants, many of which exhibit overlap and redundancy in the processes of adhesion and colonization, innate immune resistance, and the capacity to facilitate tissue barrier degradation and spread within the human host. This improved understanding of the contribution of individual virulence determinants to the disease process has led to the formulation of models of GAS disease progression, which may lead to better treatment and intervention strategies. While GAS remains sensitive to all penicillins and cephalosporins, rising resistance to other antibiotics used in disease treatment is an increasing worldwide concern. Several GAS vaccine formulations that elicit protective immunity in animal models have shown promise in nonhuman primate and early-stage human trials. The development of a safe and efficacious commercial human vaccine for the prophylaxis of GAS disease remains a high priority.

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Section: Resistance To Opsonophagocytosismentioning

confidence: 99%

Disease Manifestations and Pathogenic Mechanisms of Group A Streptococcus

et al. 2014

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“…Moreover, patients with S. pyogenes infections have antibody titers against IdeS, indicating in vivo expression (61). Interestingly, a recent study identified a protein identical to IdeS/Mac as a surface-localized anchorless protein that binds with high affinity to immunoglobulins, thus confirming the interaction with IgG, but did not discuss the cysteine proteinase activity or similarity to IdeS/Mac (56). Taken together, these data indicate that S. pyogenes expresses two unrelated cysteine proteinases that can cleave IgG, thus emphasizing the importance of this immunomodulating mechanism.…”

Section: Microbial Immunoglobulin Proteasesmentioning

confidence: 99%

Extracellular Enzymes with Immunomodulating Activities: Variations on a Theme inStreptococcus pyogenes

Collin

Olsén

2003

Infect Immun

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“…the inhibition of ROS production [18,44], or novel, as yet undiscovered activities of the protein. For instance, IdeS (designated Sib35 [52]) has been implicated as exerting a stimulatory mitogenic effect on B lymphocytes in an experimental mouse model [53]. …”

Section: Host Immune Response To Idesmentioning

confidence: 99%

Streptococcal IdeS and Its Impact on Immune Response and Inflammation

Pawel‐Rammingen¹

2012

J Innate Immun

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Survival of the important bacterial pathogen Streptococcus pyogenes relies on its ability to circumvent the antimicrobial actions of innate and specific immune responses and to modulate the inflammatory responses induced during the course of an infection. Inflammatory processes play key roles during streptococcal pathogenesis and streptococcal infections are accompanied by an intense inflammatory state. As an exclusively human pathogen, S. pyogenes has adapted to the various countermeasures employed by its host to fight bacterial infections, in particular to interfere with the effector functions of immunoglobulin G (IgG). For this purpose, S. pyogenes has evolved an IgG-specific endopeptidase, IdeS, which is highly specific for the lower hinge region of IgG. This review summarizes the current knowledge about this intriguing enzyme as well as its role in inflammation and in the attenuation of human immune responses towards streptococcal infection.

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A novel, anchorless streptococcal surface protein that binds to human immunoglobulins

Cited by 37 publications

References 23 publications

Disease Manifestations and Pathogenic Mechanisms of Group A Streptococcus

Disease Manifestations and Pathogenic Mechanisms of Group A Streptococcus

Extracellular Enzymes with Immunomodulating Activities: Variations on a Theme inStreptococcus pyogenes

Streptococcal IdeS and Its Impact on Immune Response and Inflammation

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