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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References
Plaut, A. G., Gilbert, J. V., Artenstein, M. S. & Capra, J. D. Science 1290, 1103–1105 (1975).
Kilian, M., Mestecky, J. & Schrohenloher, R. E. Infect Immun. 26, 143–149 (1979).
Koomey, J. M., Gill, R. E. & Falkow, S. Proc. natn. Acad. Sci. U.S.A. 79, 7881–7885 (1982).
Halter, R., Pohlner, J. & Meyer, T. F. EMBO J. 3, 1595–1601 (1984).
Bricker, J., Mulks, M. H., Plaut, A. G., Moxon, E. R. & Wright, A. Proc. natn. Acad. Sci. U.S.A. 80, 2681–2685 (1983).
Fishman, Y., Bricker, J., Gilbert, J. V., Plaut, A. G. & Wright, A. in Pathogenic Neisseriae Proc. Fourth Int. Microbiol. (eds Schoolnik, G. K. et al.) 164–168 (1985).
Rahr, S., Halter, R., Müller, H., Pohlner, J. & Meyer, T. F. in Pathogenic Neisseriae Proc. Fourth Int. Symp. Soc. Microbiol. (eds Schoolnik, G. K. et al.) 157–163 (1985).
Cooper, M. D., McGee, Z. A., Mulks, M. H., Koomey, J. M. & Hindman, T. L. J. inf. Dis. 150, 737–744 (1984).
Strebel, K., Beck, E., Strohmaier, K. & Schaller, H. Virology 57, 983–991 (1986).
Watson, M. E. E. Nucleic Acids Res. 12, 5145–5164 (1984).
Pollock, M. R. & Richmond, M. H. Nature 194, 446–449 (1962).
Mulks, M. H., Plaut, A. G., Feldman, H. A. & Frangione, B. J. exp. Med. 152, 1442–1447 (1980).
Lory, S., Tai, P. C. & Dabis, B. D. J. Bact. 156, 695–702 (1983).
Bayer, M. E. in Bacterial outer membranes: biogenesis and function (ed. Inouye, M.) 167–202 (Wiley, New York, 1979).
Wagner, W., Vogel, M. & Goebel, W. J. Bact. 154, 200–210 (1983).
Mackman, N., Nicaud, J.-M., Gray, L. & Holland, I. B. Molec. gen. Genet. 201, 529–536 (1985).
Hawley, D. K. & McClure, W. R. Nucleic Acids Res. 11, 2237–2255 (1983).
Schaller, H., Grey, C. & Herrmann, K. Proc. natn. Acad. Sci. U.S.A. 72, 737–456 (1975).
Gentz, R. Bujard, H. J. Bact. 164, 70–77 (1985).
Rosenberg, M. & Court, D. A. Rev. Genet. 13, 319–353 (1979).
Shine, J. & Dalgarno, L. Proc. natn. Acad. Sci. U.S.A. 71, 1342–1346 (1974).
Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Ghou, P. Y. & Fasman, G. D. A. Rev. Biochem. 47, 251–276 (1978).
Hopp, Th. P. & Woods, K. R. Proc. natn. Acad. Sci. U.S.A. 78, 3824–3828 (1981).
Neu, H. D. & Heppel, L. A. J. biol. Chem. 240, 3685–3692 (1965).
Craven, G. R., Steers, E. Jr, & Anfinsen, C. B. J. biol. Chem. 240, 2468–2473 (1965).
Howard, S. P. & Buckley, J. T. J. Bact. 161, 1118–1124 (1985).
Stern, A., Brown, M., Nickel, P. & Meyer, T. F. Cell 47, 61–71 (1986).
Hunkapiller, M. W., Lujan, E., Ostran der, F. & Hood, L. E. Meth. Emym. 91, 227–236 (1983).
Randall, L. L. & Hardy, S. J. S. Microbiol. Rev. 48, 290–298 (1984).
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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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DOI: https://doi.org/10.1038/325458a0
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