INVASION OF HELA-CELLS BY MYCOPLASMA PENETRANS AND THE INDUCTION OF TYROSINE PHOSPHORYLATION OF A 145-KDA HOST-CELL PROTEIN

The ability of Mycoplasma penetrans to invade eukaryotic cells was stu died using a HeLa cell line. The bactericidal antibiotic, gentamicin, in combination with low concentrations of Triton X-100, was utilized t o kill mycoplasmas that had not entered the cells, allowing the quanti tation of internalized organisms. The intracellular location of the my coplasma was also documented by transmission electron microscopy. The actin polymerization inhibitor cytochalasin-D markedly inhibited the i nternalization process, whereas the tyrosine phosphorylation inhibitor s, staurosporin and genistein had only a slight effect. As against the invasion of enteropathogenic Escherichia coli which depends on tyrosi ne phosphorylation of a 90-kDa (Hp90) HeLa cell protein, internalizati on of M. penetrans by HeLa cells was independent of the phosphorylatio n of Hp90. Nonetheless, tyrosine phosphorylation of a 145-kDa HeLa cel l protein was found to be associated with the interaction of M. penetr ans with HeLa cells.