The heat shock protein 90 of Eimeria tenella is essential for invasion of host cell and schizont growth

• Published in: International journal for parasitology 2006-09, Vol.36 (10), p.1205-1215
• Main Authors: Péroval, M, Pery, P, Labbe, M
• Format: Article
• Language: English
• Subjects: 90-kDa heat shock protein; Amino Acid Sequence; Animals; antibiotics; antibodies; Apicomplexa; Biological and medical sciences; biological development; cell invasion; Cloning, Molecular; coccidiosis; Coccidiosis - metabolism; Coccidiosis - transmission; Eimeria tenella; Eimeria tenella - physiology; Fundamental and applied biological sciences. Psychology; Geldanamicin; gene expression; heat shock proteins; Host-Parasite Interactions; HSP90 Heat-Shock Proteins - analysis; HSP90 Heat-Shock Proteins - genetics; HSP90 Heat-Shock Proteins - physiology; Immunoblotting; Immunoprecipitation; infection; Intracellular Membranes - metabolism; Life cycle. Host-agent relationship. Pathogenesis; Microscopy, Fluorescence; Molecular Sequence Data; Parasitology - methods; Plasmodium falciparum; Poultry Diseases - metabolism; Poultry Diseases - transmission; protein secretion; Protozoa; Protozoan Proteins - genetics; schizogony; schizonts; Secretion; sporozoites; Toxoplasma gondii; Vacuoles
• ISSN: 0020-7519; 1879-0135
• DOI: 10.1016/j.ijpara.2006.04.006

The 90-kDa heat shock proteins (Hsp90) are important for stress tolerance, for newly synthesised protein folding and for the growth of various organisms. Participation of Hsp90 in the development of Apicomplexa, notably in Plasmodium falciparum and Toxoplasma gondii, has been proven. In this work, the importance of Hsp90 for Eimeria tenella, which is responsible for avian caecal coccidiosis, was studied. Our results show that E. tenella Hsp90 (EtHsp90) expression increases during infection. Immunofluorescence microscopy studies reveal a dispersed localisation of EtHsp90 during the first schizogony. Moreover, EtHsp90 is secreted by sporozoites as early as 5 min after addition of FCS in a temperature-dependent manner. By using staurosporine, we invalidated the hypothesis that EtHsp90 might be a micronemal protein. Then, EtHsp90 was detected in a parasitophorous vacuole membrane. This result suggests the importance of EtHsp90 for intracellular growth of the parasite. Inhibition of EtHsp90 function using specific antibodies and geldanamicin attenuates the capacity of E. tenella to invade and grow in the host cell.