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Immunity to common bacteria requires the generation of antibodies that promote opsonophagocytosis and neutralise toxins. Pooled human immunoglobulin is widely advocated as an adjunctive treatment for clinical  Streptococcus pyogenes  infection however, the protein targets of the reagent remain ill defined. Affinity purification of the anti-streptococcal antibodies present within pooled immunoglobulin resulted in the generation of an IgG preparation that promoted opsonophagocytic killing of  S. pyogenes in vitro  and provided passive immunity  in vivo . Isolation of the streptococcal surface proteins recognised by pooled human immunoglobulin permitted identification and ranking of 94 protein antigens, ten of which were reproducibly identified across four contemporary invasive  S. pyogenes  serotypes (M1, M3, M12 and M89). The data provide novel insight into the action of pooled human immunoglobulin during invasive  S. pyogenes  infection, and demonstrate a potential route to enhance the efficacy of antibody based therapies.

Identification of the Streptococcus pyogenes surface antigens recognised by pooled human immunoglobulin