Binding of complement regulatory proteins to group A Streptococcus
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Updated: Jun 23, 2026

A Murine Model of Group B Streptococcus Vaginal Colonization
Published on: November 16, 2016
Maria A Oliver1, José M Rojo, Santiago Rodríguez de Córdoba
1Institut Universitari d'Investigacions en Ciències de la Salut, Universitat de les Illes Balears, Crtra. Valldemosa, km 7.5, 07122 Palma de Mallorca, Spain.
Abstract:
Streptococcus pyogenes or Group A Streptococcus (GAS) is the etiologic agent of important human infections such as acute pharyngitis, impetigo, rheumatic fever and the streptococcal toxic shock syndrome. Binding of the complement regulatory proteins factor H, factor H-like protein 1 (FHL-1), C4b-binding protein (C4BP), or CD46 is a crucial step in the pathogenesis of these infections. M protein is the GAS protein that generally mediates these interactions. However, a detailed analysis of the reports that have investigated the binding of complement regulatory components to GAS indicates that this microorganism has evolved alternative mechanisms for the recruitment of complement regulatory proteins to the bacterial surface. This article summarizes these data to provide a starting point for future research aimed at the characterization of additional mechanisms developed by GAS to evade the immune system.
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