Location of Repository

Analysis of the NTPDase and ecto-5'-nucleotidase profiles in serum-limited Trichomonas vaginalis

By Amanda Piccoli Frasson, Mariele Feiffer Charão, Denis Broock Rosemberg, Ana Paula de Souza, Solange Cristina Garcia, Cristina Bonorino, Maurício Reis Bogo, Geraldo Attilio De Carli and Tiana Tasca

Abstract

Trichomonas vaginalis is a parasite of the human urogenital tract that causes trichomonosis, the most prevalent non-viral sexually transmitted disease. Ectonucleoside triphosphate diphosphohydrolase (NTPDase) family members, which hydrolyse extracellular ATP and ADP and ecto-5′-nucleotidase, which hydrolyses AMP, have been characterised in T. vaginalis. For trichomonad culture, the growth medium is supplemented with 10% serum, which is an important source of nutrients, such as adenosine. Here, we investigated the ATP metabolism of T. vaginalis trophozoites from long-term cultures and clinical isolates under limited bovine serum conditions (1% serum). The specific enzymatic activities were expressed as nmol inorganic phosphate (Pi) released/min/mg protein, the gene expression patterns were determined by reverse transcriptase-polymerase chain reaction, the extracellular adenine nucleotide hydrolysis was analysed by high performance liquid chromatography and the cell cycle analysis was assessed by flow cytometry. Serum limitation led to the profound activation of NTPDase and ecto-5'-nucleotidase activities. Furthermore, the levels of NTPDase A and B transcripts increased and extracellular ATP metabolism was activated, which led to enhanced ATP hydrolysis and the formation of ADP and AMP. Moreover, the cell cycle was arrested at the G0/G1 stage, which suggested adenosine uptake. Our data suggest that under conditions of serum limitation, NTPDase and ecto-5'-nucleotidase play a role in providing the adenosine required for T. vaginalis growth and that this process contributes to the establishment of parasitism

Topics: Trichomonas vaginalis, serum limitation, ectonucleoside triphosphate diphosphohydrolase, ecto-5'-nucleotidase, adenosine, Microbiology, QR1-502, Science, Q, Arctic medicine. Tropical medicine, RC955-962, Special situations and conditions, RC952-1245, Internal medicine, RC31-1245, Medicine, R
Publisher: Instituto Oswaldo Cruz, Ministério da Saúde
Year: 2012
DOI identifier: 10.1590/S0074-02762012000200004
OAI identifier: oai:doaj.org/article:17a8e9c257eb483d82ef3b036f520368
Journal:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • https://doaj.org/toc/1678-8060 (external link)
  • http://www.scielo.br/scielo.ph... (external link)
  • https://doaj.org/article/17a8e... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.