Type II IgGbinding proteins

Group A streptococci express an array of functionally distinct IgG-binding proteins (Table 1). The majority of the functional types of type II IgG-binding proteins have been cloned and sequenced. All of these IgG-binding proteins are encoded by M or M-related protein genes that are present in a virulence regulon of group A streptococci, suggesting a potential role for these proteins in pathogenesis. In addition to binding IgG, the majority of type II binding proteins also bind other plasma proteins, e.g. albumin, factor H, fibrinogen, plasminogen and IgA. Analysis of the binding domains of these proteins suggest they consist of different combinations of distinct functional modules that react with different IgG subclasses or other plasma proteins. Expression of type II IgG-binding proteins is associated more frequently with group A streptococcal skin isolates than with throat isolates. Studies in mice have indicated an association between IgG-binding protein expression and skin infectivity, while no such association occurs when the bacteria are injected intra-peritoneally.

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