Invasion of HeLa cells by Mycoplasma penetrans and the induction of tyrosine phosphorylation of a 145-kDa host cell protein

FEMS Microbiol Lett. 1995 Oct 15;132(3):189-94. doi: 10.1111/j.1574-6968.1995.tb07832.x.


The ability of Mycoplasma penetrans to invade eukaryotic cells was studied using a HeLa cell line. The bactericidal antibiotic, gentamicin, in combination with low concentrations of Triton X-100, was utilized to kill mycoplasmas that had not entered the cells, allowing the quantitation of internalized organisms. The intracellular location of the mycoplasma was also documented by transmission electron microscopy. The actin polymerization inhibitor cytochalasin-D markedly inhibited the internalization process, whereas the tyrosine phosphorylation inhibitors, staurosporin and genistein had only a slight effect. As against the invasion of enteropathogenic Escherichia coli which depends on tyrosine phosphorylation of a 90-kDa (Hp90) HeLa cell protein, internalization of M. penetrans by HeLa cells was independent of the phosphorylation of Hp90. Nonetheless, tyrosine phosphorylation of a 145-kDa HeLa cell protein was found to be associated with the interaction of M. penetrans with HeLa cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion
  • Escherichia coli / growth & development
  • Gentamicins / pharmacology
  • HeLa Cells
  • Humans
  • Mycoplasma Infections / metabolism*
  • Mycoplasma penetrans / drug effects
  • Mycoplasma penetrans / growth & development*
  • Mycoplasma penetrans / ultrastructure
  • Octoxynol / pharmacology
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Tyrosine / metabolism


  • Gentamicins
  • Phosphoproteins
  • Tyrosine
  • Octoxynol