Identification of the gene encoding BmpB, a 30 kDa outer envelope lipoprotein of Brachyspira (Serpulina) hyodysenteriae, and immunogenicity of recombinant BmpB in mice and pigs

Veterinary Microbiology

Volumn 76, Issue 3, 2000, Pages 245-257

  Lee, B J ^a   La, T ^a   Mikosza, A S J ^a   Hampson, D J ^a  

^a MURDOCH UNIVERSITY   (Australia)

Author keywords

Brachyspira hyodysenteriae; Immunisation; Intestinal spirochaete; Outer envelope lipoprotein; Serological response

Indexed keywords

ENVELOPE PROTEIN; RECOMBINANT PROTEIN BMPB; UNCLASSIFIED DRUG;

ARTICLE; BRACHYSPIRA; GENE EXPRESSION REGULATION; GENE ISOLATION; IMMUNOGENICITY; MOLECULAR CLONING; NONHUMAN; SEQUENCE HOMOLOGY; SIGNAL PROCESSING; SWINE DISEASE;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; BACTERIAL OUTER MEMBRANE PROTEINS; BLOTTING, WESTERN; FECES; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; GENE EXPRESSION REGULATION, BACTERIAL; IMMUNIZATION; LIPOPROTEINS; MICE; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; RECOMBINANT PROTEINS; SERPULINA HYODYSENTERIAE; SPIROCHAETALES INFECTIONS; SWINE;

ANIMALIA; BRACHYSPIRA; BRACHYSPIRA HYODYSENTERIAE; ESCHERICHIA COLI; MANNHEIMIA HAEMOLYTICA; PASTEURELLA; PROKARYOTA; SPIROCHAETA; SUS SCROFA;

EID: 0034307833     PISSN: 03781135     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1135(00)00244-3     Document Type: Article

References (33)

1. Becker P.S., Akins D.R., Radolf J.D., Norgard M.V. Similarity between the 38-kilodalton lipoprotein of Treponema pallidum and the glucose/galactose-binding (MglB) protein of Escherichia coli. Infect. Immun. 62:1994;1381-1391.
2. Bergstrom S., Bundoc V.G., Barbour A.G. Molecular analysis of linear plasmid-encoded major surface proteins, OspA and OspB, of the Lyme disease spirochaete Borrelia burgdorferi. Mol. Microbiol. 3:1989;479-486.
3. Boyden D.A., Albert F.G., Robinson C.S. Cloning and characterization of Treponema hyodysenteriae antigens and protection in a CF-1 mouse model by immunization with a cloned endoflagellar antigen. Infect. Immun. 57:1989;3808-3815.
4. Chatfield S.N., Fernie D.S., Penn C., Dougan G. Identification of the major antigens of Treponema hyodysenteriae and comparison with those of Treponema innocens. Infect. Immun. 56:1988;1070-1075.
5. Fernie 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. 35:1983;217-221.
6. Gabe J.D., Chang R.J., Slomiany R., Andrews W.H., McCaman M.T. Isolation of extracytoplasmic proteins from Serpulina hyodysenteriae B204 and molecular cloning of the flaB1 gene encoding a 38-kilodalton flagellar protein. Infect. Immun. 63:1995;142-148.
7. Gabe J.D., Dragon E., Chang R.J., McCaman M.T. Identification of a linked set of genes in Serpulina hyodysenteriae (B204) predicted to encode closely related 39-kilodalton extracytoplasmic proteins. J. Bacteriol. 180:1998;444-448.
8. Hansen E.B., Pedersen P.E., Schouls L.M., Severin E., van Embden J.D. Genetic characterization and partial sequence determination of a Treponema pallidum operon expressing two immunogenic membrane proteins in Escherichia coli. J. Bacteriol. 162:1985;1227-1237.
9. Harris, D.L., Hampson, D.J., Glock, R.D., 1999. Swine dysentery. In: Straw, B.E., D'Allaire, S., Mengeling, W.L., Taylor, D.J. (Eds.), Diseases of Swine. Iowa State University, Ames, IA, pp. 579-600.
10. Hudson M.J., Alexander T.L.J., Lysons R.J., Wellstead P.D. Swine dysentery: failure of an attenuated strain of spirochaete, given orally, to protect pigs against subsequent challenge. Br. Vet. J. 130:1974;xxxvii-xl.
11. Hyatt D.R., ter Huurne A.A., van der Zeijst B.A., Joens L.A. Reduced virulence of Serpulina hyodysenteriae hemolysin-negative mutants in pigs and their potential to protect pigs against challenge with a virulent strain. Infect. Immun. 62:1994;2244-2248.
12. Joens L.A., Harris D.L., Baum D.H. Immunity to swine dysentery in recovered pigs. Am. J. Vet. Res. 40:1979;1352-1354.
13. Kunkle R.A., Harris D.L., Kinyon J.M. Autoclaved liquid medium for propagation of Treponema hyodysenteriae. J. Clin. Microbiol. 24:1986;669-671.
14. Kyte J., Doolittle R.F. A simple method for displaying the hydrophobic character of a protein. J. Mol. Biol. 157:1982;105-132.
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
16. Lahdenne P., Porcella S.F., Hagman K.E., Akins D.R., Popova T.G., Cox D.L., Katona L.I., Radolf J.D., Norgard M.V. Molecular characterization of a 6.6-kilodalton Borrelia burgdorferi outer membrane-associated lipoprotein (lp6.6) which appears to be downregulated during mammalian infection. Infect. Immun. 65:1997;412-421.
17. Lee B.J., Hampson D.J. Production and characterisation of a monoclonal antibody to Serpulina hyodysenteriae. FEMS Microbiol. Lett. 136:1996;193-197.
18. Lysons R., Burrows M.R., Jones P.W., Collins P. Swine dysentry, a new and effective vaccine. Pig Vet. Soc. Proc. 18:1987;87-91.
19. McCaman M.T., Auer K., Foley W., Gabe J.D. Sequence characterization of two new members of a multi-gene family in Serpulina hyodysenteriae (B204) with homology to a 39 kDa surface exposed protein: vspC and D. Vet. Microbiol. 68:1999;273-283.
20. Nakai K., Kanehisa M. Expert system for predicting protein localization sites in Gram-negative bacteria. Proteins. 11:1991;95-110.
21. Parizek R., Stewart R., Brown K., Blevins D. Protection against swine dysentery with an inactivated Treponema hyodysentariae bacterin. Vet. Med. 80:1985;80-86.
22. Rosey E.L., Kennedy M.J., Yancey R.J. Jr. Dual flaA1 flaB1 mutant of Serpulina hyodysenteriae expressing periplasmic flagella is severely attenuated in a murine model of swine dysentery. Infect. Immun. 64:1996;4154-4162.
23. Schouls L.M., van der Heide H.G., van Embden J.D. Characterization of the 35-kilodalton Treponema pallidum subsp. pallidum recombinant lipoprotein TmpC and antibody response to lipidated and nonlipidated T. pallidum antigens. Infect. Immun. 59:1991;3536-3546.
24. Sellwood, R., Bland, A.P., 1997. Ultrastructure of intestinal spirochaetes. In: Hampson, D.J., Stanton, T.B. (Eds.), Intestinal Spirochaetes in Domestic Animals and Humans. CAB International, Wallingford, UK.
25. Sellwood R., Walton F., Thomas W., Burrows M.R., Chesham J. Expression of the SmpA outer membrane lipoprotein of Serpulina hyodysenteriae strain P18A in vivo. Vet. Microbiol. 44:1995;25-35.
26. Sharma A., Sojar H.T., Glurich I., Honma K., Kuramitsu H.K., Genco R.J. Cloning, expression, and sequencing of a cell surface antigen containing a leucine-rich repeat motif from Bacteroides forsythus ATCC 43037. Infect. Immun. 66:1998;5703-5710.
27. Shine J., Dalgarno L. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA. 71:1974;1342-1346.
28. Smith S.C., Roddick F., Ling S., Gerraty N.L., Coloe P.J. Biochemical and immunochemical characterisation of strains of Treponema hyodysenteriae. Vet. Microbiol. 24:1990;29-41.
29. Stamm L.V., Hardham J.M., Frye J.G. Expression and sequence analysis of a Treponema pallidum gene, tpn38(b), encoding an exported protein with homology to T. pallidum and Borrelia burgdorferi proteins. FEMS Microbiol. Lett. 135:1996;57-63.
30. Thomas W., Sellwood R. Molecular cloning, expression, and DNA sequence analysis of the gene that encodes the 16-kilodalton outer membrane lipoprotein of Serpulina hyodysenteriae. Infect. Immun. 61:1993;1136-1140.
31. 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. 76:1979;4350-4354.
32. Wannemuehler M.J., Hubbard R.D., Greer J.M. Characterization of the major outer membrane antigens of Treponema hyodysenteriae. Infect. Immun. 56:1988;3032-3039.
33. Wu H.C., Tokunaga M., Tokunaga H., Hayashi S., Giam C.-Z. Posttranslational modification and processing of membrane lipoproteins in bacteria. J. Cell. Biochem. 22:1983;161-171.