Abstract
Adenosine phosphorylase (adenosine: orthophosphate ribosyltransferase) activity is low in mammalian cells, but is abundant in certain prokaryotes. It is an appropriate target enzyme for the development of diagnostic and chemotherapeutic agents. Adenosine phosphorylase from Bacillus subtilis and mycoplasmas that commonly infect cell cultures converted the non-toxic deoxyadenosine analog, 6-methylpurine deoxyriboside (6MPDR) into the potent anti-metabolites 6-methylpurine and 6-methylpurine riboside. Consequently 6MPDR selectively killed mammalian cell cultures infected with mycoplasmas. 6MPDR was cytotoxic to 87 of 90 mycoplasma-infected cultures (96.6%). No toxicity was observed in nine different types of mycoplasma-free cell cultures. Use of a 3T6 mouse embryo fibroblast indicator cell culture improved standardization. Cytotoxicity was apparent 3–4 days after inoculation of 10 μM of 6MPDR to 3T6 cultures infected with the following mycoplasmas: M. hyorhinis, M. orale, M. arginini, M. salivarium, A, laidlawii, M. hominis, M. fermentons, M. sp. 70–159 and M. buccale. Cytotoxicity was produced in 28/28 3T6 indicator cultures inoculated with mycoplasma-infected cell cultures in the presence of 10 μM 6MPDR. The analog is apparently non-toxic to the mycoplasmas.
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