DEMONSTRATION OF SEPARATE RECEPTORS FOR HUMAN IgA AND IgG IN GROUP A STREPTOCOCCI TYPE

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Abstract
The alkaline extract of group A streptococci type 4 was separated by electrophoresis and diffused against 27 normal human sera. One of the precipitates appeared with 85% of the sera. Addition of purified[immunoglobulin]A myeloma protein or sera containing IgA M-components to the extract changed the electrophoretic mobility of the precipitate anodically. Purified IgG Fc-fragments or sera containing IgG M-component did not affect mobility of the precipitate. This precipitate thus contained the streptococcal receptor for human IgA. A non-precipitating IgG Fc-receptor with agglutinating capacity for cells coated with human IgG1 but not IgG3 was localized by preparative electrophoresis to the same electrophoretic region as the IgA receptor. Mobility of the IgG receptor remained unaltered on addition of IgA myeloma protein permitting a separation of the 2 receptors by preparative electrophoresis. The receptors were distinct from the group specific carbohydrate, peptidoglycan and lipoteichoic acid. No M antigen or opacity factor was demonstrated in the extract.

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