Binding of complement regulatory proteins to Group A Streptococcus

• Published in: Vaccine Vol. 26; pp. I75 - I78
• Main Authors: Oliver, Maria A, Rojo, José M, Rodríguez de Córdoba, Santiago, Alberti, Sebastián
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 30-12-2008
• Subjects: Allergy and Immunology; C4b-binding protein; CD46; Complement C3b Inactivator Proteins; Complement C4b-Binding Protein - physiology; Complement Factor H - physiology; Factor H; Factor H-like protein 1; Humans; Membrane Cofactor Protein - physiology; Streptococcal Infections - etiology; Streptococcal Infections - immunology; Streptococcus; Streptococcus pyogenes; Streptococcus pyogenes - immunology; Streptococcus pyogenes - pathogenicity; Virulence; Streptococcus pyogenes; Factor H; CD46; Factor H-like protein 1; C4b-binding protein
• ISSN: 0264-410X; 1873-2518
• DOI: 10.1016/j.vaccine.2008.11.054

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.