Some human bacterial pathogens produce specific immunoglobulin A1 (IgA1) proteases that cleave the heavy chain of human IgA1, generating intact Fab and Fc fragments. Other pathogenic bacterial species express surface proteins which bind to the Fc part of human IgA in a non-immune manner. To analyse whether IgA-binding proteins affect the activity of IgA1 proteases, the ability of seven different IgA1 proteases to hydrolyse IgA1 in the presence of either of two different bacterial IgA-binding proteins was tested. Data obtained in two different types of experiment suggest that IgA1 bound to IgA-binding proteins still functions as a substrate for IgA1 proteases. As Fc fragments produced by cleaving IgA1 with IgA1 proteases still bind to IgA-binding proteins, we conclude that these two types of bacterial protein act independently of each other.


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