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Comparative Metabolism of Mesoplasma, Entomoplasma, Mycoplasma, and Acholeplasma

¹Department of Medical Microbiology and Immunology, The Ohio State University, Columbus. Ohio 43210
²Mycoplasma Section, National Institute of Allergy and Infectious Diseases, Frederick Cancer Research Facility, Frederick, Maryland 21702

^* Corresponding author. Mailing address: Department of Medical Microbiology and Immunology, The Ohio State University, 333 West 10th Ave., Columbus, OH 43210. Phone: (614) 292-8352. Fax: (614) 292-9805. Electronic mail address: pollack.1{at}osu.edu.

ABSTRACT

Cytoplasmic fractions from species of the Mollicutes genera Entomoplasma, Mesoplasma, Mycoplasma, and Acholeplasma were assayed for NADH oxidase (NADH ox), ATP- and PP_i-dependent phosphofructokinase (PFK), ATP- and PP_i-dependent deoxyguanosine kinase (dGUOK), thymidine kinase (TK), TMP kinase (TMPK), glucose-6-phosphate dehydrogenase (G6Pde), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), phosphoenolpyruvate carboxylase, hypoxanthine-guanine phosphoribosyl transferase, dUTPase, and uracil-DNA glycosylase (UNG) activities. Membrane fractions were also examined for NADH ox activity. These activities were used as indicators of the presence and relative activities of major Mollicutes metabolic and DNA repair pathways. This was the first study to determine the presence of these enzymes in members of the genera Entomoplasma and Mesoplasma. Using the data obtained, we constructed a preliminary scheme for distinguishing genera of the class Mollicutes on the basis of the results of signature functional enzyme assays. This scheme includes phylogenetic relationships deduced from rRNA analyses, but is more informative with respect to metabolic potential. The criteria used include the presence of PP_i-dependent PFK, urease, dUTPase, and dGUOK activities. Entomoplasma ellychniae ELCN-1^T (T = type strain), Entomoplasma melaleucae M-1^T, Mesoplasma seiffertii F7^T, Mesoplasma entomophilum TAC^T, Mesoplasma florum L1^T, Mycoplasma fermentans PG18^T, and Acholeplasma multilocale PN525^T were similar in most respects. NADH ox activity was localized in the cytoplasm of these organisms. These strains had ATP-dependent PFK, MDH, LDH, ATP- and PP_i-dependent dGUOK, and UNG activities, but not dUTPase or G6Pde activities. In contrast, Acholeplasma equifetale C112^T, Acholeplasma oculi 19L^T, Acholeplasma hippikon C1^T, Acholeplasma modicum PG49^T, and Acholeplasma morum 72-043^T had membrane-localized NADH ox activity, PP_i-dependent PFK, G6Pde, and dUTPase activities, and significantly lower MDH and LDH activities and exhibited a faster rate with PP_i than with ATP in the dGUOK reaction. All of the members of the Mollicutes tested had hypoxanthine-guanine phosphoribosyl transferase, phosphoenolpyruvate carboxylase, and (except for Mesoplasma entomophilum TACf) UNG activities. All of the Acholeplasma strains except Acholeplasma multilocale PN525^T had TK, TMPK, and UNG activities. Mesoplasma entomophilum TAC^T was distinguished by having no detectable dUTPase, UNG, TK, and TMPK activities, indicating that there is a severe restriction in or an absence of a synthetic route to dTTP. Our data also suggest that A. multilocale PN525^T is a member of an unrecognized metabolic subgroup of the genus Acholeplasma or is not an Acholeplasma strain.

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