Host–pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development

Areschoug, Thomas; Carlsson, Fredric; Stålhammar‐Carlemalm, Margaretha; Lindahl, Gunnar

doi:10.1016/j.vaccine.2004.08.010

Cited by 28 publications

(15 citation statements)

References 45 publications

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“…An unrelated S. aureus protein, extracellular fibrinogen binding protein (Efb) also inhibits the complement pathway, in this case by binding C3 (33). Taken together these observations, including the binding of C5 and the inhibition of complement subsequent to C5 by SSL7 (8), suggest strong selection of pathogenic group A and group B streptococci (27)(28)(29)(30) and pathogenic S. aureus to evade both host complement and IgA/Fc receptor effector systems.…”

Section: Discussionmentioning

confidence: 98%

“…Interfering with Fc␣RI-mediated recognition of IgA opsonized bacteria by blocking the receptor binding site on IgA is a strategy utilized by pathogenic group A (27,28) and group B streptococci (29,30) to frustrate IgA-mediated protective immunity. Our report that SSL7 binds IgA with high affinity and inhibits interaction with Fc␣RI (8) clearly demonstrates that this evasion strategy is utilized by staphylococci as well as streptococci.…”

Section: Discussionmentioning

confidence: 99%

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A Competitive Mechanism for Staphylococcal Toxin SSL7 Inhibiting the Leukocyte IgA Receptor, FcαRI, Is Revealed by SSL7 Binding at the Cα2/Cα3 Interface of IgA

Wines

Willoughby

Fraser

et al. 2006

Journal of Biological Chemistry

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Leukocyte recruitment and effector functions like phagocytosis and respiratory burst are key elements of immunity to infection. Pathogen survival is dependent upon the ability to overwhelm, evade or inhibit the immune system. Pathogenic group A and group B streptococci are well known to produce virulence factors that block the binding of IgA to the leukocyte IgA receptor, Fc␣RI, thereby inhibiting IgA-mediated immunity. Recently we found Staphylococcus aureus also interferes with IgA-mediated effector functions as the putative virulence factor SSL7 also binds IgA and blocks binding to Fc␣RI. Herein we report that SSL7 and Fc␣RI bind many of the same key residues in the Fc region of human IgA. Residues Leu-257 and Leu-258 in domain C␣2 and residues 440 -443 PLAF in C␣3 of IgA lie at the C␣2/C␣3 interface and make major contributions to the binding of both the leukocyte receptor Fc␣RI and SSL7. It is remarkable this S. aureus IgA binding factor and unrelated factors from streptococci are functionally convergent, all targeting a number of the same residues in the IgA Fc, which comprise the binding site for the leukocyte IgA receptor, Fc␣RI.Staphylococcus aureus, a commensal organism of the human skin and nose (1), is also a significant human pathogen responsible for conditions such as Scarlet fever, toxin shock, septicemia, and endocarditis. The S. aureus genome contains three clusters of superantigen and superantigen-like genes, designated SaPIn1, -2, and -3 (2). SaPIn2 contains the Staphylococcus superantigen-like (ssl) genes, previously designated as staphylococcal enterotoxin-like (SET) genes (3). These genes are highly represented in clinical isolates of S. aureus and are inferred to contribute to pathogenicity of these strains (4). Crystallographic studies of SSL5 (SET3) (5) and SSL7 (SET1) (6, 7) proteins have indicated structural similarity to classical superantigens with the SSLs also comprising an OB-fold and ␤-grasp domain. We have recently defined two binding activities of the SSL7 protein demonstrating that SSL7 binds simultaneously to human complement factor C5 and IgA (8). The binding of IgA by SSL7 inhibited IgA binding to the leukocyte IgA receptor Fc␣RI (CD89) thus providing a potential mechanism for evasion of IgA-mediated cellular immunity, via the blockade of IgA-mediated leukocyte effector functions such as phagocytosis and respiratory burst (9 -11). General similarities with staphylococcal protein A are clear which, although an unrelated protein, is also capable of multiple interactions targeting the host immune response, including binding TNFR1 (12), C1qR (13), and IgG via V H 3 Fabs (14) and the Fc at the C␥2/C␥3 interface region (15). This study investigated the site of human IgA binding to SSL7. SSL7 was found to bind to the C␣2/C␣3 interface of IgA Fc and require residues essential for the interaction of Fc␣RI with IgA. Thus the SSL7 and Fc␣RI binding sites are likely to be the same or at least closely overlapping. Furthermore the interaction of SSL7 was independent of the IgA Asn-263 li...

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

A Competitive Mechanism for Staphylococcal Toxin SSL7 Inhibiting the Leukocyte IgA Receptor, FcαRI, Is Revealed by SSL7 Binding at the Cα2/Cα3 Interface of IgA

Wines

Willoughby

Fraser

et al. 2006

Journal of Biological Chemistry

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“…For example, emm28 and emm87 were overrepresented among females. The role of emm28 isolates in puerperal fever has already been recognized (2,32), as isolates of this type are known to express R28, which is related to the Rib protein in group B streptococci, the major cause of neonatal infections (38,39). Recently, it was shown that the gene encoding R28 is located on a 37.4-kb region (region of difference 2 [RD2]) that is similar in content and organization to a region described in group B streptococci and that is apparently acquired by horizontal gene transfer; RD2 enables emm28 strains to often cause puerperal sepsis (24,49).…”

Section: Discussionmentioning

confidence: 99%

Clinical and Microbiological Characteristics of SevereStreptococcus pyogenesDisease in Europe

Luca-Harari

Darenberg

Neal³

et al. 2009

J Clin Microbiol

264

218

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Streptococcus pyogenes (group A streptococcus [GAS]), a major human pathogen (9), has been studied for decades and may give rise to common throat and skin infections as well as to invasive diseases, such as arthritis, septicemia, cellulitis, puerperal fever, necrotizing fasciitis (NF), and streptococcal toxic shock syndrome (STSS) (14). Since the mid-1980s there have been increasing numbers of reports describing severe manifestations of GAS infections; however, the factors underlying the worldwide resurgence of this pathogen remain unknown (20).The M protein, which is encoded by the emm gene, is an important virulence factor and is also an epidemiological marker that is used throughout the world to characterize GAS isolates (5,(21)(22)(23). The type specificity of the M protein, of which more than 100 different types are known, is largely determined by the epitope located in 40 to 50 amino acid residues at the amino terminus (4,16,27). These regions of M proteins have been shown to evoke antibodies that have strong bactericidal activity and that are not likely cross-reactive with

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“…Interestingly, there is some evidence that the R28 protein may have played a pathogenetic role in the epidemics of puerperal fever (childbed fever) that caused the death of numerous parturient women during earlier centuries and represents the classical example of a nosocomial infection (3,235). These epidemics were due to infections with S. pyogenes (135) and should not be confused with neonatal infections caused by S. agalactiae, but in both cases the infection was most probably initiated by bacteria initially present in the vagina.…”

Section: Four Members Of the Family: The ␣ Rib R28 And Alp2 Proteinsmentioning

confidence: 99%

Surface Proteins ofStreptococcus agalactiaeand Related Proteins in Other Bacterial Pathogens

2005

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Streptococcus agalactiae (group B Streptococcus) is the major cause of invasive bacterial disease, including meningitis, in the neonatal period. Although prophylactic measures have contributed to a substantial reduction in the number of infections, development of a vaccine remains an important goal. While much work in this field has focused on the S. agalactiae polysaccharide capsule, which is an important virulence factor that elicits protective immunity, surface proteins have received increasing attention as potential virulence factors and vaccine components. Here, we summarize current knowledge about S. agalactiae surface proteins, with emphasis on proteins that have been characterized immunochemically and/or elicit protective immunity in animal models. These surface proteins have been implicated in interactions with human epithelial cells, binding to extracellular matrix components, and/or evasion of host immunity. Of note, several S. agalactiae surface proteins are related to surface proteins identified in other bacterial pathogens, emphasizing the general interest of the S. agalactiae proteins. Because some S. agalactiae surface proteins elicit protective immunity, they hold promise as components in a vaccine based only on proteins or as carriers in polysaccharide conjugate vaccines

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Host–pathogen interactions in Streptococcus pyogenes infections, with special reference to puerperal fever and a comment on vaccine development

Cited by 28 publications

References 45 publications

A Competitive Mechanism for Staphylococcal Toxin SSL7 Inhibiting the Leukocyte IgA Receptor, FcαRI, Is Revealed by SSL7 Binding at the Cα2/Cα3 Interface of IgA

A Competitive Mechanism for Staphylococcal Toxin SSL7 Inhibiting the Leukocyte IgA Receptor, FcαRI, Is Revealed by SSL7 Binding at the Cα2/Cα3 Interface of IgA

Clinical and Microbiological Characteristics of SevereStreptococcus pyogenesDisease in Europe

Surface Proteins ofStreptococcus agalactiaeand Related Proteins in Other Bacterial Pathogens

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