Protein H—A novel igg binding bacterial protein

Åkesson, Per; Cooney, Jakki C.; Kishimoto, Fumitaka; Björck, Lars

doi:10.1016/0161-5890(90)90071-7

Cited by 109 publications

(92 citation statements)

References 22 publications

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“…1. On the other hand, receptors that bind only IgG have been purified from strains of group A streptococci which bind only this immunoglobulin class [7,16,17]. However, the data in Fig.…”

Section: Discussionmentioning

confidence: 99%

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Lindahl

Stenberg

1990

Epidemiol. Infect.

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SUMMARYCertain strains of group A streptococci are known to bind IgA and/or IgG via a cell surface receptor, which may act as a virulence factor. The distribution of such receptors among routine clinical isolates was studied, using a total of 225 strains and an assay based on the binding of radiolabelled immunoglobulins. Among 194 throat strains isolated during three different time periods in two different geographical areas of Sweden, 82% showed significant binding of IgA and/or IgG. Studies on 31 septicaemia strains, isolated over a period of more than 8 years, showed binding for 84% of the isolates. The binding strains were of several different T-types and could be subdivided into two groups, those binding both IgA and IgG and those binding IgG only. These data show that binding of IgA and/or IgG is a very common property among clinical isolates of group A streptococci.

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“…1. On the other hand, receptors that bind only IgG have been purified from strains of group A streptococci which bind only this immunoglobulin class [7,16,17]. However, the data in Fig.…”

Section: Discussionmentioning

confidence: 99%

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Lindahl

Stenberg

1990

Epidemiol. Infect.

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“…M proteins bind C4BP and factor H, which inhibits activation of the complement system through the alternative pathway, while binding of the Fc part of immunoglobulin G (IgG) by M proteins inhibits activation through the classical pathway (6,23,25,29). The M and M-like surface proteins bind several plasma proteins, including fibronectin, albumin, plasminogen, and the Fc part of IgG and IgA, thereby covering the bacteria with host proteins (1,7,18,20,38). Production of a hyaluronic capsule as a coat is another way by which GAS avoid the action of the immune system (3,36,41).…”

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confidence: 99%

Cleavage of Antigen-Bound Immunoglobulin G by SpeB Contributes to Streptococcal Persistence in Opsonizing Blood

Eriksson

Norgren²

2003

Infect Immun

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Group A streptococci (GAS) express a superantigen, SpeB, having cysteine protease activity. SpeB exhibits several properties that might contribute to virulence, the most recently discovered being the ability to cleave immunoglobulin G (IgG) in a manner similar to that of papain. In the present study, we confirmed this latter finding and found that the irreversible inhibition of SpeB protease activity completely abolishes IgG cleavage. SpeB cleavage of IgG was not species restricted since SpeB cleaved both human, rabbit, and mouse IgG. In order to investigate the nature of the SpeB cleavage of IgG, antibodies were immobilized prior to exposure to SpeB, either by unspecific binding of the Fc to GAS surface proteins or by antigen-specific binding. Analysis of the IgG molecules by SDS-PAGE showed that SpeB could cleave antigen-bound antibodies, while the IgG bound to IgG-binding proteins was protected from cleavage. In a phagocytosis assay using whole blood, the M49 GAS strain NZ131 showed a significantly higher survival than its isogenic speB mutant. Furthermore, the addition of extracellular supernatant derived from an overnight culture of native NZ131 increased the survival of its isogenic speB derivative. This indicates that SpeB's ability to cleave off the Fc part of antigen-bound IgG contributes to GAS escape from opsonophagocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding.

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“…Though most of these isolates contain a single emm gene, encoding the antiphagocytic M protein, some isolates possess an additional Mlike gene. This gene, sph, is located directly downstream of emm and encodes protein H. This protein has been found to bind Immunoglobulin G (IgG), fibronectin, and albumin (1,5,7) and has been implicated as a spreading factor in invasive infections (6,9). Boyle et al and Raeder and Boyle have also identified IgG Fc-binding proteins as important factors in the development of invasive infections in a mouse model of group A streptococcal skin infection (2,11).…”

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confidence: 99%

Streptococcus pyogenes Infection in Mouse Skin Leads to a Time-Dependent Up-Regulation of Protein H Expression

2003

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Streptococcus pyogenes protein H (sph) is an immunoglobulin-binding protein present in the Mga regulon of certain M1 serotype isolates. Although sph is present in many strains, it is frequently not expressed. In this paper we show that protein H was highly expressed after bacteria were injected into the skin of mice and were recovered from the blood, kidney, or spleen at various times postinfection. The percentage of protein H-positive colonies increased with time, reaching 100% in the spleen and kidney within 24 to 72 h postinfection. The up-regulation of sph expression was also observed in a mga mutant.

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Protein H—A novel igg binding bacterial protein

Cited by 109 publications

References 22 publications

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Binding of IgA and/or IgG is a common property among clinical isolates of group A streptococci

Cleavage of Antigen-Bound Immunoglobulin G by SpeB Contributes to Streptococcal Persistence in Opsonizing Blood

Streptococcus pyogenes Infection in Mouse Skin Leads to a Time-Dependent Up-Regulation of Protein H Expression

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