Monoclonal antibodies to a 16-kDa antigen of Serpulina (Treponema) hyodysenteriae

References

1. Taylor D. J., Alexander T. J. L. The production of dysentery in swine by feeding cultures containing a spirochaete. Br Vet J 1971; 127:lviii–lxi
   [Google Scholar]
2. Stanton T. B., Jensen N. S., Casey T. A., Tordoff L. A., Dewhirst F. E., Paster B. J. Reclassification of Treponema hyodysenteriae and Treponema innocens in a new genus, Serpula gen. nov., as Serpula hyodysenteriae comb. nov. and Serpula innocens comb. nov. Int J Syst Bacteriol 1991; 41:50–58
   [Google Scholar]
3. Stanton T. B. Proposal to change the genus designation Serpula to Serpulina gen. nov. containing the species Serpulina hyodysenteriae comb. nov. and Serpulina innocens comb, nov. Int J Syst Bact 1992; 42:189–190
   [Google Scholar]
4. Femie D. S., Ripley P. H., Walker P. D. Swine dysentery: protection against experimental challenge following single dose parenteral immunisation with inactivated Treponema hyodysenteriae . Res Vet Sci 1983; 35:217–221
   [Google Scholar]
5. Joens L. A., Nord N. A., Kinyon J. M., Egan I. T. Enzyme-linked immunosorbent assay for detection of antibody to Treponema hyodysenteriae antigens . J Clin Microbiol 1982; 15:249–252
   [Google Scholar]
6. Joens L. A., DeYoung D. W., Glock R. D., Mapother M. E., Cramer J. D., Wilcox H. e. Passive Protection of Segmented Swine Colonic Loops Against Swine Dysentery. Am J Vet Res 1985; 46:2369–2371
   [Google Scholar]
7. Olson L. D. Clinical and pathological observations on the experimental passage of swine dysentery. Can J Comp Med 1974; 38:7–13
   [Google Scholar]
8. Rees A. S., Lysons R. J., Stokes C. R., Bourne F. J. Antibody production by the pig colon during infection with Treponema hyodysenteriae . Res Vet Sci 1989; 47:263–269
   [Google Scholar]
9. Joens L. A., Harris D. L., Baum D. H. Immunity to swine dysentery in recovered pigs. Am J Vet Res 1979; 40:1352–1354
   [Google Scholar]
10. Joens L. A., Whipp S. C., Glock R. D., Nuessen M. E. Serotype specific protection against Treponema hyodysenteriae infection in ligated colonic loops of pigs recovered from swine dysentery. Infect Immun 1983; 39:460–462
    [Google Scholar]
11. Nuessen M. E., Joens L. A. Serotype-specific opsonization of Treponema hyodysenteriae. Infect Immun 1982; 38:1029–1032
    [Google Scholar]
12. Chatfield S. N., Femie D. S., Penn C., Dougan G. Identification of the major antigens of Treponema hyodysenteriae and comparison with those of Treponema innocens . Infect Immun 1988; 56:1070–1075
    [Google Scholar]
13. Chatfield S. N., Fernie D. S., Beesley J., Penn C., Dougan G. Characterisation of the cell envelope of Treponema hyodysenteriae . FEMS Microbiol Lett 1988; 55:303–308
    [Google Scholar]
14. Joens L. A., Marquez R. B. Molecular characterization of proteins from porcine spirochetes. Infect Immun 1986; 54:893–896
    [Google Scholar]
15. Wannemuehler M. J., Hubbard R. D., Greer J. M. Characterization of the major outer membrane antigens of Treponema hyodysenteriae . Infect Immun y1988; 56:3032–3039
    [Google Scholar]
16. Sellwood R., Kent K. A., Burrows M. R., Lysons R. J., Bland A. P. Antibodies to a common outer envelope antigen of Treponema hyodysenteriae with antibacterial activity. J Gen Microbiol 1989; 135:2249–2257
    [Google Scholar]
17. Kent K. A., Sellwood R., Lemcke R. M., Burrows M. R., Lysons R. J. Analysis of the axial filaments of Treponema hyodysenteriae by SDS-PAGE and immunoblotting. J Gen Microbiol 1989; 135:1625–1632
    [Google Scholar]
18. Howard C. J., Parsons K. R., Jones B. V., Sopp P., Pocock D. H. Two monoclonal antibodies (CC17, CC29) recognizing an antigen (Bo5) on bovine T lymphocytes, analogous to human CD5. Vet Immunol Immunopathol 1988; 19:127–139
    [Google Scholar]
19. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350–4354
    [Google Scholar]
21. Lemcke R. M., Burrows M. R. A disc growth-inhibition test for differentiating Treponema hyodysenteriae from other intestinal spirochaetes. Vet Rec 1979; 104:548–551
    [Google Scholar]
22. Penn C. W. Avoidance of host defences by Treponema pallidum in situ and on extraction from infected rabbit testes. J Gen Microbiol 1981; 126:69–75
    [Google Scholar]
23. Stamm L. V., Hodinka R. L., Wyrick P. B., Bassford P. J. Changes in the cell surface properties of Treponema pallidum that occur during in vitro incubation of freshly extracted organisms. Infect Immun 1987; 55:2255–2261
    [Google Scholar]
24. Radolf J. D., Norgard M. V., Schulz W. W. Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidum . Proc Natl Acad Sci USA 1989; 86:2051–2055
    [Google Scholar]
25. Radolf J. D., Chamberlain N. R., Clausell A., Norgard M. V. Identification and localization of integral membrane proteins of virulent Treponema pallidum subsp. pallidum by phase partitioning with the nonionic detergent Triton X-114. Infect Immun 1988; 56:490–498
    [Google Scholar]
26. Chamberlain N. R., Brandt M. E., Erwin A. L., Radolf J. D., Norgard M. V. Major integral membrane protein immunogens of Treponema pallidum are proteolipids. Infect Immun 1989; 57:2872–2877
    [Google Scholar]
27. Swancutt M. A., Radolf J. D., Norgard M. V. The 34-kilodalton membrane immunogen of Treponema pallidum is a lipoprotein. Infect Immun 1990; 58:384–392
    [Google Scholar]
28. Barbour A. G., Tessier S. L., Hayes S. F. Variation in a major surface protein of Lyme disease spirochaetes. Infect Immun 1984; 45:94–100
    [Google Scholar]
29. Brandt M. E., Riley B. S., Radolf J. D., Norgard M. V. Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins. Infect Immun 1990; 58:983–991
    [Google Scholar]
30. Fikrig E., Barthold S. W., Kantor F. S., Flavell R. A. Protection of mice against Lyme disease agent by immunizing with recombinant OspA. Science 1990; 250:553–556
    [Google Scholar]
31. Thomas W., Sellwood R., Lysons R. J. A 16-kDa lipoprotein of the outer membrane of S hyodysenteriae . Infect Immun 1992 in press
    [Google Scholar]