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Alternative Inhibitors Of Mycoplasma Adherence

  • Itzhak Kahane
  • Abed Athamna
  • David Yogev
  • Mordechai R. Kramer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 408)

Abstract

Mycoplasma is the trivial name of the class Mollicutes, a group of minute wall-less bacteria comprising now more than 140 species. They are characterized by their small genome size; the smallest of bacteria. It comprises about 500-1000 predicted coding sequences (genes) as compared to, for example, 1727 and about 4000 in Hœmphilus influenza and Escherichia coli respectively. The complete genome of the smallest mycoplasma, Mycoplasma genitalium which is a human pathogen, was elucidated very recently by Fraser et al. It is 580 kb long and comprises only 470 predicted coding sequences. By evolution, the mycoplasmas belong to the gram-positive bacteria with low G+C genome. They underwent genome reduction and with it, also lost much of their biosynthetic machinery. The organisms grow in broth, but need a complex medium. It is therefore not surprising that most mycoplasmas are parasites, and many are pathogens of a vast variety of hosts, including humans. In addition, they easily contaminate the rich culture media and then adhere to the cells grown there and therefore are considered to be pests of cells in culture.

Keywords

Sialic Acid Dextran Sulfate Mycoplasma Pneumoniae Sialic Acid Residue Host Cell Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Athamna, A., M. R. Kramer and I. Kahane 1996a. Adherence of Mycoplasma Pneumoniae to human alveolar macrophages, In: Toward Anti-Adhesion Therapy of Microbial Diseases (Kahane, I. and I. Ofek, eds) Plenum Press, New York and London (p. 266)Google Scholar
  2. Athamna, A., R. Rosengarten, S. Levisohn, I. Kahane and D. Yogev. 1996b. Hemadsorption of Mycoplasma Gallisepticum involves switching of variable surface membrane proteins. In: Toward Anti-Adhesion Therapy of Microbial Diseases (Kahane, I. and I. Ofek, eds) Plenum Press, New York and London (p. 265)Google Scholar
  3. Almagor, M., I. Kahane and S. Yatsiv. 1984. The role of superoxide anion in host cell injury induced by Mycoplamsa pneumoniae infection: Study in normal and trisomy 21 cells. J. Clin. Investigation, 73:842–847CrossRefGoogle Scholar
  4. Brunner, H. 1993. Mycoplasma Infections of Man: Respiratory and Male Genital Tract Diseases, In: Rapid Diagnosis Of Mycoplasmas (I. Kahane and A. Adoni, eds) pp.39–56, Plenum Press, New York and LondonGoogle Scholar
  5. Frser, C. M. et al. 1995. The minimal gene complement of Mycoplama genitalium.Science. 270:397–398Google Scholar
  6. Gerstenecker, B. and Jacobs, E. 1993. Development Of A Capture-Elisa For The Specific Detection of Mycoplasma Pneumoniae In Patients’ Material, In: Rapid Diagnosis Of Mycoplasmas (I. Kahane and A. Adoni, eds) pp. 195–205, Plenum Press, New York and LondonGoogle Scholar
  7. Kahane, I. 1992. Frontiers in mycoplasma pathogenicity. World J. Microbiol. Biotech. 8:50–51CrossRefGoogle Scholar
  8. Kahane, I. 1995. Adhesions of mycoplasmas, In: Methods in Enzymology: Adhesion of Microbial Pathogens (R. J. Doyle and I. Ofek, eds) vol.253, pp.367–373. Academic Press,Ine.Orlando,FLCrossRefGoogle Scholar
  9. Krivan, H. C., Olson, L.D., Barile, M. F., Ginsburg, V. and Roberts, E 1989 pneumoniae to sulfated glycolipids and inhibition by dextran s. Adhension of Mycoplasma pneumonia to sulfated glycolipids and inhibition by dextran sulfate. J Biol Chem. 264:9283–9288PubMedGoogle Scholar
  10. Loveless, R.W and Feizi, T. 1989 Sialo-oligosaccharide receptors for Mycoplasma pneumoniae and related oligosaccharide of poly-N-acetyl-lactosamine series are polarized at the cilia and apical-microvillar domains of the ciliated cells in human bronchial epithelium. Infect. Immun. 57:1285–1289PubMedGoogle Scholar
  11. Montagnier, L. 1993. HIV cofactors and AIDS. Proceedings of IX International Congress on AIDS and STDGoogle Scholar
  12. Nir-Paz, R., Israel, S., Honigman, A. and Kahane, I. 1995. Mycoplasmas regulate HIV-LTR-dependent gene expression. FEMS Microbial. Lett. 128:63–68Google Scholar
  13. Thomas, L. and Bitensky, M. W. 1966. Studies of PPLO infection. IV. The neurotoxicity of intact mycoplasma, and their production of toxin in vivo and in vitro. J. Exp. Med. 124:1089–1098PubMedCrossRefGoogle Scholar
  14. Yogev, D., Rosengarten,R., Watson-McKown, R. and Wise, K. S. 1991. Molecular basis of Mycoplasma surface antigenic variation: a novel set of divergent genes undergo spontaneous mutations of periodic coding regions and 5’regulatory sequences. EMBO J. 10:4069–4079PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Itzhak Kahane
    • 1
  • Abed Athamna
    • 1
  • David Yogev
    • 1
  • Mordechai R. Kramer
    • 2
  1. 1.Department of Membrane and Ultrastructure ResearchThe Hebrew University-Hadassah Medical SchoolJerusalemIsrael
  2. 2.Pulmonary InstituteHadassah University HospitalJerusalemIsrael

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