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. 1993 Jul;61(7):2945–2951. doi: 10.1128/iai.61.7.2945-2951.1993

Cytoadhesins of Mycoplasma hominis.

B Henrich 1, R C Feldmann 1, U Hadding 1
PMCID: PMC280943  PMID: 8514399

Abstract

The mechanism of Mycoplasma hominis adherence to host cells of the urogenital tract was investigated with monoclonal antibodies (MAbs) directed against antigenic surface-localized polypeptides P50, P60, P80, and P100 of cytoadherent M. hominis FBG. A cell enzyme-linked immunosorbent assay was established allowing quantification of cytoadherent mycoplasmas detected by one of the following MAbs: four MAbs directed against P100 (molecular weight, about 100,000), three MAbs against P80, one MAb against P60, and three MAbs against P50. MAb binding to one of the surface proteins resulted in a decrease of mycoplasmal adherence to HeLa cells. To exclude the thesis that this is caused by nonspecific blocking of adherence, P100 and P50 were purified by affinity chromatography and tested instead of intact mycoplasmas in the cell enzyme-linked immunosorbent assay for cytoadherence. Both proteins bound to the surface of the eukaryotic cells. MAb binding to single epitopes of these proteins resulted in inhibition of protein adherence. These experiments strongly suggest that of the four surface-localized proteins at least P100 and P50 are adhesins of M. hominis FBG.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barile M. F., Grabowski M. W., Stephens E. B., O'Brien S. J., Simonson J. M., Izumikawa K., Chandler D. K., Taylor-Robinson D., Tully J. G. Mycoplasma hominis- tissue cell interactions: a review with new observations on phenotypic and genotypic properties. Sex Transm Dis. 1983 Oct-Dec;10(4 Suppl):345–354. [PubMed] [Google Scholar]
  2. Baseman J. B., Cole R. M., Krause D. C., Leith D. K. Molecular basis for cytadsorption of Mycoplasma pneumoniae. J Bacteriol. 1982 Sep;151(3):1514–1522. doi: 10.1128/jb.151.3.1514-1522.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blazek R., Schmitt K., Krafft U., Hadding U. Fast and simple procedure for the detection of cell culture mycoplasmas using a single monoclonal antibody. J Immunol Methods. 1990 Aug 7;131(2):203–212. doi: 10.1016/0022-1759(90)90191-w. [DOI] [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  5. Chandler D. K., Collier A. M., Barile M. F. Attachment of Mycoplasma pneumoniae to hamster tracheal organ cultures, tracheal outgrowth monolayers, human erythrocytes, and WiDr human tissue culture cells. Infect Immun. 1982 Mar;35(3):937–942. doi: 10.1128/iai.35.3.937-942.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  7. Dallo S. F., Chavoya A., Baseman J. B. Characterization of the gene for a 30-kilodalton adhesion-related protein of Mycoplasma pneumoniae. Infect Immun. 1990 Dec;58(12):4163–4165. doi: 10.1128/iai.58.12.4163-4165.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Elkins C., Rest R. F. Monoclonal antibodies to outer membrane protein PII block interactions of Neisseria gonorrhoeae with human neutrophils. Infect Immun. 1990 Apr;58(4):1078–1084. doi: 10.1128/iai.58.4.1078-1084.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Feldmann R. C., Henrich B., Kolb-Bachofen V., Hadding U. Decreased metabolism and viability of Mycoplasma hominis induced by monoclonal antibody-mediated agglutination. Infect Immun. 1992 Jan;60(1):166–174. doi: 10.1128/iai.60.1.166-174.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Feldner J., Göbel U., Bredt W. Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody. Nature. 1982 Aug 19;298(5876):765–767. doi: 10.1038/298765a0. [DOI] [PubMed] [Google Scholar]
  11. Fleming J. O., Pen L. B. Measurement of the concentration of murine IgG monoclonal antibody in hybridoma supernatants and ascites in absolute units by sensitive and reliable enzyme-linked immunosorbent assays (ELISA). J Immunol Methods. 1988 May 25;110(1):11–18. doi: 10.1016/0022-1759(88)90077-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hu P. C., Cole R. M., Huang Y. S., Graham J. A., Gardner D. E., Collier A. M., Clyde W. A., Jr Mycoplasma pneumoniae infection: role of a surface protein in the attachment organelle. Science. 1982 Apr 16;216(4543):313–315. doi: 10.1126/science.6801766. [DOI] [PubMed] [Google Scholar]
  13. Hu P. C., Schaper U., Collier A. M., Clyde W. A., Jr, Horikawa M., Huang Y. S., Barile M. F. A Mycoplasma genitalium protein resembling the Mycoplasma pneumoniae attachment protein. Infect Immun. 1987 May;55(5):1126–1131. doi: 10.1128/iai.55.5.1126-1131.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kamla V., Henrich B., Hadding U. Species differentiation of mycoplasmas by EF-Tu specific monoclonal antibodies. J Immunol Methods. 1992 Feb 14;147(1):73–81. doi: 10.1016/s0022-1759(12)80031-7. [DOI] [PubMed] [Google Scholar]
  15. Kotani H., McGarrity G. J. Rapid and simple identification of mycoplasmas by immunobinding. J Immunol Methods. 1985 Dec 27;85(2):257–267. doi: 10.1016/0022-1759(85)90136-x. [DOI] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Manchee R. J., Taylor-Robinson D. Studies on the nature of receptors involved in attachment of tissue culture cells to mycoplasmas. Br J Exp Pathol. 1969 Feb;50(1):66–75. [PMC free article] [PubMed] [Google Scholar]
  18. Olson L. D., Shane S. W., Karpas A. A., Cunningham T. M., Probst P. S., Barile M. F. Monoclonal antibodies to surface antigens of a pathogenic Mycoplasma hominis strain. Infect Immun. 1991 May;59(5):1683–1689. doi: 10.1128/iai.59.5.1683-1689.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Riethman H. C., Boyer M. J., Wise K. S. Triton X-114 phase fractionation of an integral membrane surface protein mediating monoclonal antibody killing of Mycoplasma hyorhinis. Infect Immun. 1987 May;55(5):1094–1100. doi: 10.1128/iai.55.5.1094-1100.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Stanbridge E. J. A reevaluation of the role of mycoplasmas in human disease. Annu Rev Microbiol. 1976;30:169–187. doi: 10.1146/annurev.mi.30.100176.001125. [DOI] [PubMed] [Google Scholar]
  21. de StGroth S. F., Scheidegger D. Production of monoclonal antibodies: strategy and tactics. J Immunol Methods. 1980;35(1-2):1–21. doi: 10.1016/0022-1759(80)90146-5. [DOI] [PubMed] [Google Scholar]

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