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Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease

Nature volume 325, pages 458–462 (1987)Cite this article

Abstract

Several human bacterial pathogens, including the Gram-negative diplococcus Neisseria gonorrhoeae, produce extracellular proteases that are specific for human immunoglobulin IgA1, (refs 1, 2). Immunoglobulin A (IgA) proteases have been studied extensively and the genes of some species cloned in Escherichia coli3–7, but their role in pathogenesis remains unclear8. Recently we derived a DNA fragment of 5 kilobases (kb) from N. gonorrhoeae MS 11 directing extracellular active enzyme in E. coli4. Although the mature enzyme of strain MS 11 was shown to have a relative molecular mass of 106,000 (Mr 106K) in gels4, the DNA sequence of this cloned fragment reveals a single gene coding for a 169K precursor of IgA protease. The precursor contains three functional domains, the amino-terminal leader which is assumed to initiate the inner membrane transport of the precursor, the protease, and a carboxyl-terminal 'helper' domain apparently required for extracellular secretion (excretion). Based on the structural features of the precursor, we propose a model in which the helper serves as a pore for excretion of the protease domain through the outer membrane. IgA protease acquires an active conformation as its extracellular transport proceeds and is released as a proform from the membrane-bound helper by autoproteolysis. The soluble proform further matures into the 106 K IgA protease and a small stable α-protein.

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Author information

Authors and Affiliations

  1. Max-Planck-Institut für Biologie, Spemannstrasse 34, D-74, Tübingen, FRG

    Johannes Pohlner, Roman Halter & Thomas F. Meyer

  2. Universität zu Köln, Institut für Genetik, D-5 Köln, FRG

    Konrad Beyreuther

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  1. Johannes Pohlner
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  2. Roman Halter
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  3. Konrad Beyreuther
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  4. Thomas F. Meyer
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Pohlner, J., Halter, R., Beyreuther, K. et al. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325, 458–462 (1987). https://doi.org/10.1038/325458a0

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