1887

Abstract

A putative serine protease expressed by subsp. was isolated from a lambda gt11 genomic expression library by screening with serum from a naturally infected sheep. The gene was contained in two overlapping clones, which were shown by antibody elution to encode a protein of 34 kDa in . The clones were sequenced and database searches detected a motif identical to the active serine site in trypsin, and 30% homology to the putative serine proteases (HtrA proteins) of and .

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1994-08-01
2021-10-28
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References

  1. Akrigg D., Bleasby A.J., Dix N.I.M., Findlay J.B.C., North A.C.T., Parry-Smith D.J., Wootton J.C., Blundell T.L., Gardner S.P., Hayes F., Islam S., Sternberg M.J.E., Thornton J.M., Tickle I.J., Murray-Rust P. A protein sequence/structure database. Nature 1988; 335:745–746
    [Google Scholar]
  2. Bairoch A. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res 1991; 19:2241–2245
    [Google Scholar]
  3. Beall J.A., Mitchell G.F. Identification of a particular antigen from a parasite cDNA library using antibodies affinity purified from selected portions of western blots. J Immunol Methods 1986; 86:217–223
    [Google Scholar]
  4. Bleasby A.J., Wootton J.C. Construction of validated, non-redundant composite protein sequence databases. Protein Eng 1990; 3:153–159
    [Google Scholar]
  5. Braun Breton C., Pereia da Silva L.H. Malarial proteases and red blood cell invasion. Parasitol Today 1993; 9:92–96
    [Google Scholar]
  6. Chiodini R.J., Van Kruiningen H.J., Merkal R.S. Ruminant paratubercuiosis (Johne's disease): the current status and future prospects. Cornell Vet 1984; 74:218–262
    [Google Scholar]
  7. Clark-Curtiss J.E., Thole J.E.R., Sathish M., Bosecker B.A., Sela S., De Carvalho E.F., Esser R.E. Protein antigens of Mycobacterium leprae. Res Microbiol 1990; 141:859–871
    [Google Scholar]
  8. De Kesel M., Gilot P., Misonne M.C., Coene M., Cocito C. Cloning and expression of portions of the 34-kilodalton protein gene of Mycobacterium paratubercuiosis: its application to serological analysis of Johne's disease. J Clin Microbiol 1993; 31:947–954
    [Google Scholar]
  9. Donachie W., Gilmour N.J.L. Sheep antibody response to cell wall antigens expressed in vivo by Pasteurella haemoiytica serotype A2. FEMS Microbiol Lett 1988; 56:271–276
    [Google Scholar]
  10. Dunn B.M. Determination of protease mechanism. In Proteolytic Enzymes: a Practical Approach 1989 Edited by Beynon R.J., Bond J.S. Oxford: Oxford University Press; pp 57–81
    [Google Scholar]
  11. Eaton N.R. New press for disruption of microorganisms. J Bacteriol 1962; 83:1359–1360
    [Google Scholar]
  12. Engers H.D., Bloom B.R., Godal T. Monoclonal antibodies against mycobacterial antigens. Immunol Today 1985; 6:345, 347–348
    [Google Scholar]
  13. Epstein D.M., Wensink P.C. The a-lytic protease gene of Eysobacter enyymogenes. J Biol Chem 1988; 263:16586–16590
    [Google Scholar]
  14. Gilot P., De Kesel M., Machtelinckx L., Coene M., Cocito C. Isolation and sequencing of the gene coding for an antigenic 34-kilodalton protein of Mycobacterium paratubercuiosis. J Bacteriol 1993; 175:4930–4935
    [Google Scholar]
  15. Goding J.W. Monoclonal Antibodies 1980 Principle and Practice. London: Academic Press;
    [Google Scholar]
  16. von Heijne G. How signal sequences maintain cleavage specificity. J Mol Biol 1984; 173:243–251
    [Google Scholar]
  17. Husson R.N., Young R.A. Genes for the major protein antigens of Mycobacterium tuberculosis-, the etiologic agents of tuberculosis and leprosy share an immunodominant antigen. Proc Natl Acad Sci USA 1987; 84:1679–1683
    [Google Scholar]
  18. Johnson K., Charles I., Dougan G., Pickard D., O'Gaora P., Costa G., Ali T., Miller I., Hormaeche C. The role of a stress response protein in Salmonella typhimurium virulence. Mol Microbiol 1991; 5:401–407
    [Google Scholar]
  19. Jonson G., Svennerholm A.-M., Holmgren J. Vibrio cholerae expresses cell surface antigens during intestinal infection which are not expressed during in vitro culture. Infect lmmun 1989; 57:1809–1815
    [Google Scholar]
  20. Kolk A.H.J., Evers R., Groothuis D.G., Gilis H., Kuijper S. Production and characterisation of monoclonal antibodies against specific serotypes of Mycobacterium avium and the Mycobacterium avium-Mycobacterium intracellulare-Mycobacterium scrofulaceum complex. Infect lmmun 1989; 57:2514–2521
    [Google Scholar]
  21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  22. Lipinska B., Sharma S., Georgopoulos C. Sequence analysis and regulation of the HtrA gene of Escherichia coli: a ct32-independent mechanism of heat-inducible transcription. Nucleic Acids Res 1988; 16:10053–10067
    [Google Scholar]
  23. Lipinska B., Fayet O., Baird L., Georgopoulos C. Identification, characterisation and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J Bacteriol 1989; 171:1574–1584
    [Google Scholar]
  24. Lipinska B., Zylicz M., Georgopoulos C. The HtrA (Deg P) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J Bacteriol 1990; 172:1791–1797
    [Google Scholar]
  25. Lu M.C., Lien M.H., Becker R.E., Heine H.C., Buggs A.M., Lipovesek D., Gupta R., Robbins P.W., Grosskinsky C.M., Hubbard S.C., Young R.A. Genes for immunodominant protein antigens are highly homologous in Mycobacterium tuberculosis, Mycobacterium africanum, and the vaccine strain Mycobacterium bovis BCG. Infect lmmun 1987; 55:2378–2382
    [Google Scholar]
  26. Matthews P.R.J., McDiarmid A. The production in bovine calves of a disease resembling paratubercuiosis with a Mycobacterium sp isolated from a wood pigeon (Columba palumbus L). Vet Rec 1979; 104:286
    [Google Scholar]
  27. Morris S.L., Rouse D.A., Hussong D., Chaparas S.D. Isolation and characterisation of a recombinant igtl 1 bacteriophage which expresses an immunoreactive Mycobacterium intracellulare protein in Escherichia coli. Infect lmmun 1988; 56:3026–3031
    [Google Scholar]
  28. Morris S.L., Rouse D.A., Hussong D., Chaparas S.D. Isolation and characterisation of recombinant X gtl 1 bacteriophages expressing four different Mycobacterium intracellulare antigens. Infect lmmun 1990; 58:17–20
    [Google Scholar]
  29. Neurath H. The diversity of proteolytic enzymes. In Proteolytic Enzymes: a Practical Approach 1989 Edited by Beynon R.J., Bond J.S. Oxford: Oxford University Press; pp 1–13
    [Google Scholar]
  30. Old R.W., Primrose S.B. In Principles of Gene Manipulation, chapter 7 1989 Oxford: Blackwell Scientific Publications;
    [Google Scholar]
  31. Rouse D.A., Morris S.L., Karpas A.B., Mackall J.C., Probst P.G., Chaparas S.D. Immunological characterisation of recombinant antigens isolated from a Mycobacterium avium Agtll expression library by using monoclonal antibody probes. Infect lmmun 1991; 59:2595–2600
    [Google Scholar]
  32. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: a Eaboratory Manual 1989 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  33. Sanger F., Nicklen S., Coulsen A.R. DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 1977; 74:5463–5467
    [Google Scholar]
  34. Sathish M., Esser R.E., Thole J.E.R., Clark-Curtiss J.E. Identification and characterisation of antigenic determinants of Mycobacterium leprae that react with antibodies in sera from leprosy patients. Infect lmmun 1990; 58:1327–1336
    [Google Scholar]
  35. Scherf A., Mattei D., Schreiber M. Parasite antigens expressed in Escherichia coli. A refined approach for epidemiological analysis. J Immunol Methods 1990; 128:81–87
    [Google Scholar]
  36. Stuart P. Vaccination against Johne's disease in cattle exposed to experimental infection. Br Vet J 1965; 121:289–318
    [Google Scholar]
  37. Wieles B., Van Agterveld M., Janson A., Clark-Curtiss J., Rinke De Wit T., Harboe M., Thole J. Characterisation of a Mycobacterium leprae antigen related to the secreted Mycobacterium tuberculosis protein MPT32. Infect lmmun 1994; 62:252–258
    [Google Scholar]
  38. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage vectors and host strains: nucleotide sequences of M13mpl8 and pUC19 vectors. Gene 1985; 33:103–119
    [Google Scholar]
  39. Young D.B., Mehlert A. Serology of mycobacteria: characterisation of antigens recognized by monoclonal antibodies. Rev Infect Dis 1989; ll:2 (suppl) S431–S435
    [Google Scholar]
  40. Young R.A., Bloom B.A., Grosskinsky C.M., Ivanyi J., Thomas D., Davis R.W. Dissection of Mycobacterium tuberculosis antigens using recombinant DNA. Proc Natl Acad Sci USA 1985; 82:2583–2587
    [Google Scholar]
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