title: Five putative nucleoside triphosphate diphosphohydrolase genes are expressed in Trichomonas vaginalis.
abstract: Trichomonas vaginalis is a protozoan that parasitizes the human urogenital tract causing trichomoniasis, the most common non-viral sexually transmitted disease. The parasite has unique genomic characteristics such as a large genome size and expanded gene families. Ectonucleoside triphosphate diphosphohydrolase (E-NTPDase) is an enzyme responsible for hydrolyzing nucleoside tri- and diphosphates and has already been biochemically characterized in T. vaginalis. Considering the important role of this enzyme in the production of extracellular adenosine for parasite uptake, we evaluated the gene expression of five putative NTPDases in T. vaginalis. We showed that all five putative TvNTPDase genes (TvNTPDase1-5) were expressed by both fresh clinical and long-term grown isolates. The amino acid alignment predicted the presence of the five crucial apyrase conserved regions, transmembrane domains, signal peptides, phosphorylation and catalytic sites. Moreover, a phylogenetic analysis showed that TvNTPDase sequences make up a clade with NTPDases intracellularly located. Biochemical NTPDase activity (ATP and ADP hydrolysis) is responsive to the serum-restrictive conditions and the gene expression of TvNTPDases was mostly increased, mainly TvNTPDase2 and TvNTPDase4, although there was not a clear pattern of expression among them. In summary, the present report demonstrates the gene expression patterns of predicted NTPDases in T. vaginalis.
authors.affiliation: Laboratório de Pesquisa em Parasitologia, Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Av. Ipiranga 2752, 90610-000, Porto Alegre, RS, Brazil.
authors.forename: Amanda Piccoli
authors.initials: AP
authors.lastname: Frasson
authors.affiliation: Laboratório de Pesquisa em Parasitologia, Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Av. Ipiranga 2752, 90610-000, Porto Alegre, RS, Brazil.
authors.forename: Odelta
authors.initials: O
authors.lastname: Dos Santos
authors.affiliation: Laboratório de Pesquisa em Parasitologia, Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Av. Ipiranga 2752, 90610-000, Porto Alegre, RS, Brazil.
authors.forename: Lúcia Collares
authors.initials: LC
authors.lastname: Meirelles
authors.affiliation: Laboratório de Diversidade Microbiana, Faculdade de Farmácia e Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Av. Ipiranga 2752, 90610-000, Porto Alegre, RS, Brazil.
authors.forename: Alexandre José
authors.initials: AJ
authors.lastname: Macedo
authors.affiliation: Laboratório de Pesquisa em Parasitologia, Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Av. Ipiranga 2752, 90610-000, Porto Alegre, RS, Brazil tiana.tasca@ufrgs.br.
authors.forename: Tiana
authors.initials: T
authors.lastname: Tasca
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D011755:Pyrophosphatases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D016415:Sequence Alignment; D014247:Trichomonas Vaginitis / Q000382:microbiology; D014246:Trichomonas vaginalis / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics*
chemical_list: D001426:Bacterial Proteins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D011755:Pyrophosphatases
keywords: Trichomonas vaginalis; gene expression; nucleoside triphosphate diphosphohydrolase; serum limitation