A New MAP Kinase Protein Involved in Estradiol-Stimulated Reproduction of the Helminth Parasite Taenia crassiceps

• Published in: BioMed research international 2010-01, Vol.2010 (2010), p.1-11
• Main Authors: Escobedo, Galileo, Soldevila, Gloria, Ortega-Pierres, Guadalupe, Chávez-Ríos, Jesús Ramsés, Nava, Karen, Fonseca-Liñán, Rocío, López-Griego, Lorena, Hallal-Calleros, Claudia, Ostoa-Saloma, Pedro, Morales-Montor, Jorge
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animal reproduction; Animals; Cysticercus - cytology; Cysticercus - enzymology; Cysticercus - physiology; Dose-Response Relationship, Drug; Electrophoresis, Gel, Two-Dimensional; Estradiol - metabolism; Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors; Extracellular Signal-Regulated MAP Kinases - chemistry; Extracellular Signal-Regulated MAP Kinases - genetics; Extracellular Signal-Regulated MAP Kinases - metabolism; Female; Flow Cytometry; Helminth Proteins - chemistry; Helminth Proteins - genetics; Helminth Proteins - metabolism; Hormones; Immunohistochemistry; Kinases; Male; Molecular Sequence Data; Parasites; Phosphorylation; Phylogeny; Proteins; Reproduction - drug effects; Reproduction - physiology; Sequence Analysis, Protein; Taenia - drug effects; Taenia - enzymology; Taenia - growth & development; Taenia crassiceps
• ISSN: 1110-7243; 2314-6133; 1110-7251; 2314-6141
• DOI: 10.1155/2010/747121

MAP kinases (MAPK) are involved in the regulation of cellular processes such as reproduction and growth. In parasites, the role of MAPK has been scarcely studied. Here, we describe the participation of an ERK-like protein in estrogen-dependent reproduction of the helminth parasite Taenia crassiceps. Our results show that 17β-estradiol induces a concentration-dependent increase in the bud number of in vitro cultured cysticerci. If parasites are also incubated in presence of an ERK-inhibitor, the stimulatory effect of estrogen is blocked. The expression of ERK-like mRNA and its corresponding protein was detected in the parasite. The ERK-like protein was over-expressed by all treatments. Nevertheless, a strong induction of phosphorylation of this protein was observed only in response to 17β-estradiol. Cross-contamination by host cells was discarded by flow cytometry analysis. Parasite cells expressing the ERK-like protein were exclusively located at the subtegument tissue by confocal microscopy. Finally, the ERK-like protein was separated by bidimensional electrophoresis and then sequenced, showing the conserved TEY activation motif, typical of all known ERK 1/2 proteins. Our results show that an ERK-like protein is involved in the molecular signalling during the interaction between the host and T. crassiceps, and may be considered as target for anti-helminth drugs design.