Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1977 May 1;145(5):1328–1343. doi: 10.1084/jem.145.5.1328

Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium

PMCID: PMC2180664  PMID: 870608

Abstract

Identification of the attachment factor on virulent Mycoplasma pneumoniae organisms which permits surface parasitism of respiratory epithelium was attempted. Brief pretreatment of M. pneumoniae monolayers with protease prevented mycoplasma attachment ot sensitive host cells without reducing viability of the microorganisms. Gel electrophoretic analysis of mycoplasma proteins before and after exposure of intact mycoplasmas to protease revealed the absence of a major protein species (P1) in enzyme-treated preparations while other protein bands with the exception of P2 were virtually unaffected. The absence of P1 correlated with the failure of enzyme-treated mycoplasmas to attach to tracheal explants. P1 regeneration after protease treatment of mycoplasma monolayers was directly associated with reattachment capabilities in M. pneumoniae. Erythromycin inhibited P1 resynthesis, thus preventing resumed attachment activity by mycoplasmas. Lactoperoxidase-catalyzed iodination of intact M. pneumoniae organisms further confirmed that P1 was an external membrane protein and suggested that his surface component was required for the successful membrane-membrane interaction between host and parasite.

Full Text

The Full Text of this article is available as a PDF (2.8 MB).

Selected References

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

  1. BARSKI G., KOURILSKY R., CORNEFERT F. Resistance of respiratory ciliated epithelium to action of polio and adeno viruses in vitro. Proc Soc Exp Biol Med. 1957 Nov;96(2):386–391. doi: 10.3181/00379727-96-23485. [DOI] [PubMed] [Google Scholar]
  2. Baseman J. B., Collier A. M. Diphtheria pathogenesis in Guinea pig tracheal organ culture. Infect Immun. 1974 Nov;10(5):1146–1151. doi: 10.1128/iai.10.5.1146-1151.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boatman E. S., Kenny G. E. Morphology and ultrastructure of Mycoplasma pneumoniae spherules. J Bacteriol. 1971 Jun;106(3):1005–1015. doi: 10.1128/jb.106.3.1005-1015.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bransome E. D., Jr, Sharpe S. E., 3rd Measurement of 131 I and 125 I by liquid scintillation counting. Anal Biochem. 1972 Oct;49(2):343–352. doi: 10.1016/0003-2697(72)90437-x. [DOI] [PubMed] [Google Scholar]
  5. Cherry J. D., Taylor-Robinson D. Growth and Pathogenesis of Mycoplasma mycoides var. capri in Chicken Embryo Tracheal Organ Cultures. Infect Immun. 1970 Oct;2(4):431–438. doi: 10.1128/iai.2.4.431-438.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Collier A. M., Clyde W. A., Jr Appearance of Mycoplasma pneumoniae in lungs of experimentally infected hamsters and sputum from patients with natural disease. Am Rev Respir Dis. 1974 Dec;110(6):765–773. doi: 10.1164/arrd.1974.110.6P1.765. [DOI] [PubMed] [Google Scholar]
  7. Deeb B. J., Kenny G. E. Characterizion of Mycoplasma pulmonis variants isolated from rabbits. II. Basis for differentiation of antigenic subtypes. J Bacteriol. 1967 Apr;93(4):1425–1429. doi: 10.1128/jb.93.4.1425-1429.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Denny F. W., Clyde W. A., Jr, Glezen W. P. Mycoplasma pneumoniae disease: clinical spectrum, pathophysiology, epidemiology, and control. J Infect Dis. 1971 Jan;123(1):74–92. doi: 10.1093/infdis/123.1.74. [DOI] [PubMed] [Google Scholar]
  9. Denny F. W. Effect of a toxin produced by Haemophilus influenzae on ciliated respiratory epithelium. J Infect Dis. 1974 Feb;129(2):93–100. doi: 10.1093/infdis/129.2.93. [DOI] [PubMed] [Google Scholar]
  10. FRITZ P. J., MELIUS P. Mechanism of activation of hog pancreatic lipase by sodium taurocholate. Can J Biochem Physiol. 1963 Mar;41:719–730. [PubMed] [Google Scholar]
  11. Gahmberg C. G., Hakomori S. I. External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes. J Biol Chem. 1973 Jun 25;248(12):4311–4317. [PubMed] [Google Scholar]
  12. Hollingdale M. R., Lemcke R. M. The antigens of Mycoplasma hominis. J Hyg (Lond) 1969 Dec;67(4):585–602. doi: 10.1017/s0022172400042042. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hollingdale M. R., Manchee R. J. The role of mycoplasma membrane proteins in the adsorption of animal cells to Mycoplasma hominis colonies. J Gen Microbiol. 1972 Apr;70(2):391–393. doi: 10.1099/00221287-70-2-391. [DOI] [PubMed] [Google Scholar]
  14. Hu P. C., Collier A. M., Baseman J. B. Alterations in the metabolism of hamster tracheas in organ culture after infection by virulent Mycoplasma pneumoniae. Infect Immun. 1975 Apr;11(4):704–710. doi: 10.1128/iai.11.4.704-710.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hu P. C., Collier A. M., Baseman J. B. Interaction of virulent Mycoplasma pneumoniae with hamster tracheal organ cultures. Infect Immun. 1976 Jul;14(1):217–224. doi: 10.1128/iai.14.1.217-224.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hynes R. O. Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3170–3174. doi: 10.1073/pnas.70.11.3170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hynes R. O. Cell surface proteins and malignant transformation. Biochim Biophys Acta. 1976 Apr 30;458(1):73–107. doi: 10.1016/0304-419x(76)90015-9. [DOI] [PubMed] [Google Scholar]
  18. Kapitany R. A., Zebrowski E. J. A high resolution PAS stain for polyacrylamide gel electrophoresis. Anal Biochem. 1973 Dec;56(2):361–369. doi: 10.1016/0003-2697(73)90202-9. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Powell D. A., Hu P. C., Wilson M., Collier A. M., Baseman J. B. Attachment of Mycoplasma pneumoniae to respiratory epithelium. Infect Immun. 1976 Mar;13(3):959–966. doi: 10.1128/iai.13.3.959-966.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Razin S., Prescott B., Caldes G., James W. D., Chanock R. M. Role of Glycolipids and Phosphatidylglycerol in the Serological Activity of Mycoplasma pneumoniae. Infect Immun. 1970 Apr;1(4):408–416. doi: 10.1128/iai.1.4.408-416.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Razin S., Prescott B., Chanock R. M. Immunogenicity of Mycoplasma pneumoniae glycolipids: a novel approach to the production of antisera to membrane lipids. Proc Natl Acad Sci U S A. 1970 Oct;67(2):590–597. doi: 10.1073/pnas.67.2.590. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Razin S. The cell membrane of mycoplasma. Ann N Y Acad Sci. 1967 Jul 28;143(1):115–129. doi: 10.1111/j.1749-6632.1967.tb27651.x. [DOI] [PubMed] [Google Scholar]
  24. Rittenhouse H. G., McFadden B. A., Shumway L. K., Heptinstall J. Cell surface protein of Pseudomonas (Hydrogenomonas) facilis. J Bacteriol. 1973 Jul;115(1):330–340. doi: 10.1128/jb.115.1.330-340.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Smith C. B., Friedewald W. T., Chanock R. M. Inactivated Mycoplasma pneumoniae vaccine. Evaluation in volunteers. JAMA. 1967 Feb 6;199(6):353–358. [PubMed] [Google Scholar]
  26. Steinberg P., Horswood R. L., Chanock R. M. Temperature-sensitive mutants of Mycoplasma pneumoniae. I. In vitro biologic properties. J Infect Dis. 1969 Aug;120(2):217–224. doi: 10.1093/infdis/120.2.217. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES