Group A streptococcal infections in humans

Cartwright, Keith

doi:10.1046/j.1365-2672.83.s1.6.x

Cited by 16 publications

(15 citation statements)

References 11 publications

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“…These localized infections can be complicated by spread to deeper tissues and by the postinfectious sequelae of acute rheumatic fever and glomerulonephritis (4,5). Recently, there has been an increase in severe, highly invasive streptococcal infections of soft tissues with high mortality (4, 6 -8).…”

Section: G Roup a Streptococcus Or Streptococcus Pyogenes Is Amentioning

confidence: 99%

“…For most S. pyogenes strains, this gene cluster includes not only the emm gene encoding M (Emm) protein, but also one or two additional genes encoding structurally related proteins designated Enn and Mrp (12,13). The Emm proteins have affinity for several plasma proteins, including fibrinogen, IgG, IgA, and the complement regulatory proteins, factor H, factor H-like protein 1 (FHL-1), 4 and C4b-binding protein (C4BP) (12,14,15). It has been suggested that bacterial binding of these plasma proteins contributes to the antiphagocytic properties conferred by most Emm proteins.…”

Section: G Roup a Streptococcus Or Streptococcus Pyogenes Is Amentioning

confidence: 99%

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Interaction between Complement Regulators andStreptococcus pyogenes: Binding of C4b-Binding Protein and Factor H/Factor H-Like Protein 1 to M18 Strains Involves Two Different Cell Surface Molecules

Pérez-Caballero

García-Laorden

Cortés

et al. 2004

The Journal of Immunology

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Streptococcus pyogenes, or group A Streptococcus, is one of the most frequent causes of pharyngitis and skin infections in humans. Many virulence mechanisms have been suggested to be involved in the infectious process. Among them is the binding to the bacterial cell surface of the complement regulatory proteins factor H, factor H-like protein 1 (FHL-1), and C4b-binding protein. Previous studies indicate that binding of these three regulators to the streptococcal cell involves the M protein encoded by the emm gene. M-type 18 strains are prevalent among clinical isolates and have been shown to interact with all three complement regulators simultaneously. Using isogenic strains lacking expression of the Emm18 or the Enn18 proteins, we demonstrate in this study that, in contradistinction to previously described S. pyogenes strains, M18 strains bind the complement regulators factor H, FHL-1, and C4b-binding protein through two distinct cell surface proteins. Factor H and FHL-1 bind to the Emm18 protein, while C4BP binds to the Enn18 protein. We propose that expression of two distinct surface structures that bind complement regulatory proteins represents a unique adaptation of M18 strains that enhances their resistance to opsonization by human plasma and increases survival of this particular S. pyogenes strain in the human host. These new findings illustrate that S. pyogenes has evolved diverse mechanisms for recruitment of complement regulatory proteins to the bacterial surface to evade immune clearance in the human host.

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Section: G Roup a Streptococcus Or Streptococcus Pyogenes Is Amentioning

confidence: 99%

Section: G Roup a Streptococcus Or Streptococcus Pyogenes Is Amentioning

confidence: 99%

Interaction between Complement Regulators andStreptococcus pyogenes: Binding of C4b-Binding Protein and Factor H/Factor H-Like Protein 1 to M18 Strains Involves Two Different Cell Surface Molecules

Pérez-Caballero

García-Laorden

Cortés

et al. 2004

The Journal of Immunology

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“…This agent is responsible for a wide variety of diseases, ranging from uncomplicated pharyngitis (5) and impetigo (14) to severe life-threatening invasive conditions such as toxic shock-like syndrome, necrotizing fasciitis, and scarlet fever (30,31). Complications of GAS infections can also lead to the poststreptococcal sequelae of rheumatic fever and glomerulonephritis (32).…”

mentioning

confidence: 99%

Identification and Characterization of a Novel Secreted Immunoglobulin Binding Protein from Group A Streptococcus

Fagan¹,

Reinscheid²,

Gottschalk³

et al. 2001

Infect Immun

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Immunoglobulin binding proteins are one of several pathogenicity factors which have been associated with invasive disease caused by group A streptococci. The surface-bound M and M-like proteins of Streptococcus pyogenes are the most characterized of these immunoglobulin binding proteins, and in most cases they bind only a single antibody class. Here we report the identification of a novel non-M-type secreted protein, designated SibA (for secreted immunoglobulin binding protein from group A streptococcus), which binds all immunoglobulin G (IgG) subclasses, the Fc and Fab fragments, and also IgA and IgM. SibA has no significant sequence homology to any M-related proteins, is not found in the vir regulon, and contains none of the characteristic M-protein regions, such as the A or C repeats. Like M proteins, however, SibA does have relatively high levels of alanine, lysine, glutamic acid, leucine, and glycine. SibA and M proteins also share an alpha-helical N-terminal secondary structure which has been previously implicated in immunoglobulin binding in M proteins. Evidence presented here indicates that this is also the case for SibA. SibA also has regions of local similarity with other coiled-coil proteins such as Listeria monocytogenes P45 autolysin, human myosin heavy chain, macrogolgin, and Schistoma mansoni paramyosin, some of which are of potential significance since cross-reactive antibodies between myosin proteins and M proteins have been implicated in the development of the autoimmune sequelae of streptococcal disease.The resurgence of severe group A streptococcal (GAS) disease has led to increased research efforts into the pathogenicity mechanisms of the causal bacterial species, Streptococcus pyogenes. This agent is responsible for a wide variety of diseases, ranging from uncomplicated pharyngitis (5) and impetigo (14) to severe life-threatening invasive conditions such as toxic shock-like syndrome, necrotizing fasciitis, and scarlet fever (30,31). Complications of GAS infections can also lead to the poststreptococcal sequelae of rheumatic fever and glomerulonephritis (32). The exact mechanisms of GAS pathogenesis have not yet been fully elucidated; however, it has been demonstrated that these bacteria are capable of interacting with a large number of host cells and tissues types. This diversity has led to the speculation that the type of colonization event, e.g., adhesion and at times internalization, contributes directly to the various manifestations of disease (for reviews, see references 11, 12, and 21).Immunoglobulin binding proteins are one of the pathogenicity factors which have been associated with invasive GAS disease (4, 23). The mechanism of their action is not fully understood; however, it is likely that they contribute to evasion of the host's immune defenses. Binding of both immunoglobulin A (IgA) and IgG or of IgG alone is found in all invasivedisease clinical isolates (24), whereas in septicemia and noninvasive throat strains, immunoglobulin binding is not a common characteristic (28). Near...

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“…For example, from a cluster of six NF cases in the UK, two had no predisposing history. 107 Other case series have also noted a similar lack of antecedent history, with no portal of entry in eight of 20 patients with invasive GAS infection in the USA, 19 and five of 14 consecutive NF cases over five-years in Northern Australia. 90 Occasionally, patients reported mild upper respiratory tract infection.…”

Section: Global Gas Resurgence and Non-penetrating Trauma Associated Nfmentioning

confidence: 74%

Bromine, bear-claw scratch fasciotomies, and the Eagle effect: management of group A streptococcal necrotising fasciitis and its association with trauma

Lamb

Sriskandan

Tan

2015

The Lancet Infectious Diseases

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Group A streptococcal infections in humans

Cited by 16 publications

References 11 publications

Interaction between Complement Regulators andStreptococcus pyogenes: Binding of C4b-Binding Protein and Factor H/Factor H-Like Protein 1 to M18 Strains Involves Two Different Cell Surface Molecules

Interaction between Complement Regulators andStreptococcus pyogenes: Binding of C4b-Binding Protein and Factor H/Factor H-Like Protein 1 to M18 Strains Involves Two Different Cell Surface Molecules

Identification and Characterization of a Novel Secreted Immunoglobulin Binding Protein from Group A Streptococcus

Bromine, bear-claw scratch fasciotomies, and the Eagle effect: management of group A streptococcal necrotising fasciitis and its association with trauma

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