Abstract
Cell proteins from the porcine mycoplasmasMycoplasma hyorhinis, M. hyopneumoniae, andM. flocculare have been analyzed by SDS-gel electrophoresis and immunoblotting. The protein profiles ofM. hyopneumoniae andM. flocculare were similar, but the protein profile ofM. hyorhinis was quite different from the others. Antisera prepared against whole cells of the above three mycoplasmas were used in immunoblotting of electrophoretically separated antigens and in enzyme-linked immunosorbent assay. One major antigen, which had a molecular weight of 73 k, was found to be common to all three mycoplasmas. Another major antigen, with a molecular weight of 41 k, was common toM. hyopneumoniae andM. flocculare and may also be present inM. hyorhinis. Several antigens of comparatively high molecular weights (108 k, 102 k, 93 k, 89 k, and 87 k) seemed to be specific forM. hyopneumoniae. Three antisera prepared by immunization of rabbits with immunoprecipitates obtained by crossed immunoelectrophoresis ofM. hyopneumoniae were also used in blotting experiments. One of these antisera was found to be directed against the 73 k antigen common to the three porcine mycoplasmas investigated. The other two antisera were directed againstM. hyopneumoniae-specific antigens with molecular weights of 74 k, 58 k, 45 k, 44 k, and 38 k.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Literature Cited
Alexander AG, Kenny GE (1980) Characterization of the strain-specific and common surface antigens ofMycoplasma arginini. Infect Immun 29:442–451
Engvall E, Perlman P (1972) Enzyme-linked immunosorbent assay, ELISA. III. Quantitation of specific antibodies by enzyme-labelled anti-immunoglobulin in antigen coated tubes. J Immunol 109:129–135
Freeman MJ, Armstrong CH, Sands-Freeman LL, Lopez-Osuna M (1984) Serological cross-reactivity of porcine reference antisera toM. hyopneumoniae, M. flocculare, M. hyorhinis andM. hyosynoviae indicated by the enzyme-linked immunosorbent assay, complement fixation and indirect hemagglutination tests. Can J Comp Med 48:202–207
Freundt EA, Ernø H, Lemcke, RM (1979) Identification of mycoplasmas. In: Bergan T, Norris JR (eds) Methods in microbiology, vol 13. London: Academic Press, pp 391–406
Friis NF (1975) Some recommendations concerning primary isolation ofMycoplasma suipneumoniae andMycoplasma flocculare. Nord Veterinaermed 27:337–339
Friis NF, Jensen PT (1984) Serological comparison of type strains of porcine, bovine, and ovine mycoplasmas with atypical colony morphology. Acta Vet Scand 25:29–35
Haid A, Suissa M (1983) Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol 96:192–205
Heegaard NHH, Bjerrum OJ (1987) Immunoblotting: general principles and procedures. In: Bjerrum OJ, Heegaard NHH (eds) Handbook of immunoblotting. Boca Raton FL: CRC Press (in press)
Johansson K-E (1983) Characterization of theAcholeplasma laidlawii membrane by electroimmunochemical analysis methods. In: Bjerrum OJ (ed) Electroimmunochemical analysis ofmembrane proteins. Amsterdam: Elsevier, pp 321–346
Johansson K-E (1987) Separation of antigens by analytical gel electrophoresis. In: Bjerrum OJ, Heegaard NHH (eds) Handbook of immunoblotting. Boca Raton FL: CRC Press (in press)
Johansson K-E (1986) Double replica electroblotting: a method to produce two replicas from one gel. J Biochem Biophys Methods 13:197–203
Johansson K-E, Wróblewski H (1983) Characterization of membrane proteins by crossed immunoelectrophoresis. In: Razin S, Tully JG (eds) Methods in mycoplasmalogy New York: Academic Press, pp 257–267
Kenny GE, Cartwright FD (1984) Immunoblotting for determination of the antigenic specificties of antibodies to themycoplasmatales. Isr J Med Sci 20:908–911
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
Laurell C-B (1965) Antigen-antibody crossed immunoelectrophoresis. Anal Biochem 10:358–361
Laurell C-B (1972) Electroimmuno assay. Scand J Clin Lab Invest [Suppl 124] 29:21–37
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Martinsson K (1974) Preparation of antisera against different animal serum proteins, using cross-reacting specific anti-human sera. Zentralbl Vet Med [B] 21:302–306
Nicolet J, Paroz P, Bruggman S (1980) Tween 20 soluble proteins ofMycoplasma hyopneumoniae as antigens for an enzyme linked immunosorbent assay. Res Vet Sci 29:305–309
Nicolet J, Paroz PH, Kristensen B (1980) Growth medium constituents contaminating mycoplasma preparations and their role in the study of membrane glycoproteins in porcine mycoplasmas. J Gen Microbiol 119:17–26
Paroz PH, Krawinkler M, Nicolet J (1977) Verwendung der Polyacrylamid-Gel-Elektrophorese in der Diagnostik von Nutztier-Mykoplasmen. Zentralbl Vet Med [B] 24:668–677
Razin S, Rottem S (1967) Identification ofMycoplasma and other microorganisms by polyacrylamide-gel electrophoresis of cell proteins. J Bacteriol 94:1807–1810
Ro LH, Ross RF (1983) Comparison ofMycoplasma hyopneumoniae strains by serological methods. Am J Vet Res 44:2087–2094
Rose DL, Tully JG, Wittler RG (1979) Taxonomy of some swine mycoplasmas:Mycoplasma suipneumoniae Goodwin et al. 1965, a later objective synonym ofMycoplasma hyopneumoniae Mare and Switzer 1965, and the status ofMycoplasma flocculare Meyling and Friis 1972 Int J Syst Bacteriol 29:83–91
Towbin H, Staehlin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350–4354
Weber K, Osborn M (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 244:4406–4412
Whittlestone P (1979) Porcine myoplasmas. In: Barile MF, Razin S (eds) The mycoplasmas, vol 2 New York: Academic Press, pp 133–176
Wise KS, Watson RK (1983) Monoclonal antibodies toMycoplasma hyorhinis surface antigens: tools for analyzing mycoplasma-lymphoid cell interactions. Yale J Biol Med 56:623–629
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bölske, G., Strandberg, ML., Bergström, K. et al. Species-specific antigens ofMycoplasma hyopneumoniae and cross-reactions with other porcine mycoplasmas. Current Microbiology 15, 233–239 (1987). https://doi.org/10.1007/BF01577537
Issue Date:
DOI: https://doi.org/10.1007/BF01577537