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Secretory Immunity and the Bacterial IgA Proteases

Stephen J. Kornfeld and Andrew G. Plaut
Reviews of Infectious Diseases
Vol. 3, No. 3 (May - Jun., 1981), pp. 521-534
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/4452581
Page Count: 14
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Secretory Immunity and the Bacterial IgA Proteases
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Abstract

The characteristics and functions of microbial IgA proteases are reveiwed. These enzymes represent a structurally heterogeneous group of proteins that are secreted into the extracellular environment by bacteria capable of causing human disease. The IgA proteases, which vary in their requirements for metal ions, are neutral endopeptidases whose role in the infectious process is not known but whose pronounced substrate specificity for human proteins of the IgA1 subclass has repeatedly been demonstrated. As reagents, the IgA proteases are useful in cleaving IgA molecules to yield intact Fcα and Fabα fragments that will allow the study of the structure and function of the two large regions of IgA immunoglobulin proteins. The role, if any, of these enzymes in promoting infection by pathogenic members of the genera Neisseria, Hemophilus, and Streptococcus is not known, although the secretory immune system is primarily mediated by antibodies of the IgA isotype, among which are IgA1 subclass proteins, and these proteins are susceptible to cleavage by IgA protease. The determination of the role of these enzymes in the pathogenesis of human infection must await clearer understanding of antigenicity and antibody function at secretory sites and of the relative roles of the two subclasses of human IgA in immune defense.

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