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

Julian Andreev, Zipora Borovsky, Ilan Rosenshine, Shlomo Rottem*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

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.

Original languageAmerican English
Pages (from-to)189-194
Number of pages6
JournalFEMS Microbiology Letters
Volume132
Issue number3
DOIs
StatePublished - 15 Oct 1995

Bibliographical note

Funding Information:
We would like to thank A. Katzenel for excellent technical assistance,D r. M. Kessel for his help and advice with the electron microscopy and Dr. M. Tarshis for his help at the preliminary stageso f this study. This study was supported by the German-Israeli Foundation (GIF).

Keywords

  • Bacterial invasion
  • HeLa cells
  • Mycoplasma penetrans
  • Tyrosine phosphorylation

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