title: Arginine metabolism in Trichomonas vaginalis infected with Mycoplasma hominis.
abstract: Both Mycoplasma hominis and Trichomonas vaginalis utilize arginine as an energy source via the arginine dihydrolase (ADH) pathway. It has been previously demonstrated that M. hominis forms a stable intracellular relationship with T. vaginalis; hence, in this study we examined the interaction of two localized ADH pathways by comparing T. vaginalis strain SS22 with the laboratory-generated T. vaginalis strain SS22-MOZ2 infected with M. hominis MOZ2. The presence of M. hominis resulted in an approximately 16-fold increase in intracellular ornithine and a threefold increase in putrescine, compared with control T. vaginalis cultures. No change in the activity of enzymes of the ADH pathway could be demonstrated in SS22-MOZ2 compared with the parent SS22, and the increased production of ornithine could be attributed to the presence of M. hominis. Using metabolic flow analysis it was determined that the elasticity of enzymes of the ADH pathway in SS22-MOZ2 was unchanged compared with the parent SS22; however, the elasticity of ornithine decarboxylase (ODC) in SS22 was small, and it was doubled in SS22-MOZ2 cells. The potential benefit of this relationship to both T. vaginalis and M. hominis is discussed.
authors.affiliation: Haskins Laboratories, Pace University, NY 10038, USA.
authors.forename: Mary
authors.initials: M
authors.lastname: Morada
authors.affiliation: Haskins Laboratories, Pace University, NY 10038, USA.
authors.forename: Mafruha
authors.initials: M
authors.lastname: Manzur
authors.affiliation: The Department of Chemistry and Physical Sciences, Pace University, NY 10038, USA.|Haskins Laboratories, Pace University, NY 10038, USA.
authors.forename: Brian
authors.initials: B
authors.lastname: Lam
authors.affiliation: The Department of Chemistry and Physical Sciences, Pace University, NY 10038, USA.|Haskins Laboratories, Pace University, NY 10038, USA.
authors.forename: Cho
authors.initials: C
authors.lastname: Tan
authors.affiliation: Department of Parasitology, Charles University, Prague, Czech Republic.
authors.forename: Jan
authors.initials: J
authors.lastname: Tachezy
authors.affiliation: Department of Biomedical Sciences, Division of Experimental and Clinical Microbiology, University of Sassari, 07100 Sassari, Italy.
authors.forename: Paola
authors.initials: P
authors.lastname: Rappelli
authors.affiliation: Department of Biomedical Sciences, Division of Experimental and Clinical Microbiology, University of Sassari, 07100 Sassari, Italy.
authors.forename: Daniele
authors.initials: D
authors.lastname: Dessì
authors.affiliation: Department of Biomedical Sciences, Division of Experimental and Clinical Microbiology, University of Sassari, 07100 Sassari, Italy.
authors.forename: Pier L
authors.initials: PL
authors.lastname: Fiori
authors.affiliation: The Department of Chemistry and Physical Sciences, Pace University, NY 10038, USA.|Haskins Laboratories, Pace University, NY 10038, USA.
authors.forename: Nigel
authors.initials: N
authors.lastname: Yarlett
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000378:metabolism*; D006867:Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D019535:Mycoplasma hominis / Q000378:metabolism*; D009955:Ornithine Decarboxylase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D014246:Trichomonas vaginalis / Q000201:enzymology / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology*
chemical_list: D015800:Protozoan Proteins; D001120:Arginine; D006867:Hydrolases; C019723:arginine deiminase; D009955:Ornithine Decarboxylase