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  • Title: Inhibition of alternative complement pathway opsonization by group A streptococcal M protein.
    Author: Peterson PK, Schmeling D, Cleary PP, Wilkinson BJ, Kim Y, Quie PG.
    Journal: J Infect Dis; 1979 May; 139(5):575-85. PubMed ID: 374652.
    Abstract:
    Group A streptococcal M protein is known to be antiphagocytic; however, the exact basis for this property has not been established. In this study the hypothesis was tested that cell wall--associated M protein inhibits phagocytosis by interfering with bacterial opsonization. Two strains of group A Streptococcus pyogenes, CS44 (M+) and CS64 (an M- variant of CS44), were radiolabeled, and after incubation in serum these organisms were exposed to human polymorphonuclear leukocytes. Phagocytosis was quantitated by measurement of leukocyte-associated radioactivity. The contributions of complement and of immunoglobulin to streptococcal opsonization were evaluated by use of serum from a variety of sources. The results revealed that the M- strain was efficiently opsonized via the alternative complement pathway in a relative absence of immunoglobulins. In contrast, the M+ strain was poorly opsonized by all sera tested. These findings suggest that streptococcal M protein in some way prevents bacterial opsonization via the alternative complement pathway and that this property of M protein may partly explain its antiphagocytic characteristic.
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