Open AccessInvasion of HeLa cells by Mycoplasma penetrans and the induction of tyrosine phosphorylation of a 145‐kDa host cell protein
Author(s) -
Andreev Julian,
Borovsky Zipora,
Rosenshine Ilan,
Rottem Shlomo
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07832.x
Subject(s) - hela , tyrosine phosphorylation , internalization , biology , phosphorylation , cytochalasin d , tyrosine , protein phosphorylation , cytochalasin , intracellular , microbiology and biotechnology , cell , biochemistry , protein kinase a , cytoskeleton
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.