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Science 12 December 1975:
Vol. 190. no. 4219, pp. 1103 - 1105
DOI: 10.1126/science.810892

Articles

Science, Vol 190, Issue 4219, 1103-1105
Copyright © 1975 by American Association for the Advancement of Science


articles

Neisseria gonorrhoeae and neisseria meningitidis: extracellular enzyme cleaves human immunoglobulin A

AG Plaut, JV Gilbert, MS Artenstein, and JD Capra

The gonococcus and meningococcus, which infect human mucosal surfaces, elaborate a highly specific proteolytic enzyme which cleaves the immunoglobulin A1 subclass of the principal mucosal antibody, immunoglobulin A (IgA). The susceptible Pro-Thr bond lies in a unique region of the IgA heavy chain; the IgA2 subclass, lacking this peptide bond, is enzyme resistant.


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Characterization of igaB, a Second Immunoglobulin A1 Protease Gene in Nontypeable Haemophilus influenzae..
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Adaptive Evolution of the IgA Hinge Region in Primates.
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Neisserial Immunoglobulin A1 Protease Induces Specific T-Cell Responses in Humans.
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Effects of the Immunoglobulin A1 Protease on Neisseria gonorrhoeae Trafficking across Polarized T84 Epithelial Monolayers.
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Infect. Immun. 68, 906-911
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Immunoglobulin A1 Protease, an Exoenzyme of Pathogenic Neisseriae, Is a Potent Inducer of Proinflammatory Cytokines.
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Limited Local and Systemic Antibody Responses to Neisseria gonorrhoeae during Uncomplicated Genital Infections.
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Comparisons of the Ability of Human IgG3 Hinge Mutants, IgM, IgE, and IgA2, to Form Small Immune Complexes: A Role for Flexibility and Geometry.
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Pathogenesis of Pelvic Inflammatory Disease: What Are the Questions?.
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