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. 1980 Nov 1;152(5):1442-7.
doi: 10.1084/jem.152.5.1442.

IgA proteases of two distinct specificities are released by Neisseria meningitidis

M H Mulks, A G Plaut, H A Feldman, B Frangione

IgA proteases of two distinct specificities are released by Neisseria meningitidis

M H Mulks et al. J Exp Med. .

Abstract

Strains of Neisseria meningitidis produce two distinct extracellular IgA proteases that cleave the human IgA1 heavy chain at different points within the hinge region. Type 1 protease cleaves the prolyl-seryl peptide bond at position 237-238; type type 2 protease cleaves the prolyl-threonyl bond two residues amino terminal to that bond attacked by type 1 enzyme. Each meningococcal isolate elaborates only one of these two enzymes, and the type of protease produced correlates with certain serogroups: group A yielding only type 1, and groups X and Y only type 2 enzyme. In addition, analysis of amino acid sequences of human alpha-chain proteins reveals that the repeating octapeptide characteristic of the IgA1 hinge region is actually triplicated.

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