TY - JOUR
T1 - Characterization of a novel organelle in Toxoplasma gondii with similar composition and function to the plant vacuole
AU - Miranda, Kildare
AU - Pace, Douglas A.
AU - Cintron, Roxana
AU - Rodrigues, Juliany C.F.
AU - Fang, Jianmin
AU - Smith, Alyssa
AU - Rohloff, Peter
AU - Coelho, Elvis
AU - De Haas, Felix
AU - De Souza, Wanderley
AU - Coppens, Isabelle
AU - Sibley, L. David
AU - Moreno, Silvia N.J.
PY - 2010/6
Y1 - 2010/6
N2 - Summary Toxoplasma gondii belongs to the phylum Apicomplexa and is an important cause of congenital disease and infection in immunocompromised patients. Like most apicomplexans, T. gondii possesses several plant-like features, such as the chloroplast-like organelle, the apicoplast. We describe and characterize a novel organelle in T. gondii tachyzoites, which is visible by light microscopy and possesses a broad similarity to the plant vacuole. Electron tomography shows the interaction of this vacuole with other organelles. The presence of a plant-like vacuolar proton pyrophosphatase (TgVP1), a vacuolar proton ATPase, a cathepsin L-like protease (TgCPL), an aquaporin (TgAQP1), as well as Ca2+/H+ and Na+/H + exchange activities, supports similarity to the plant vacuole. Biochemical characterization of TgVP1 in enriched fractions shows a functional similarity to the respective plant enzyme. The organelle is a Ca2+ store and appears to have protective effects against salt stress potentially linked to its sodium transport activity. In intracellular parasites, the organelle fragments, with some markers colocalizing with the late endosomal marker, Rab7, suggesting its involvement with the endocytic pathway. Studies on the characterization of this novel organelle will be relevant to the identification of novel targets for chemotherapy against T. gondii and other apicomplexan parasites as well.
AB - Summary Toxoplasma gondii belongs to the phylum Apicomplexa and is an important cause of congenital disease and infection in immunocompromised patients. Like most apicomplexans, T. gondii possesses several plant-like features, such as the chloroplast-like organelle, the apicoplast. We describe and characterize a novel organelle in T. gondii tachyzoites, which is visible by light microscopy and possesses a broad similarity to the plant vacuole. Electron tomography shows the interaction of this vacuole with other organelles. The presence of a plant-like vacuolar proton pyrophosphatase (TgVP1), a vacuolar proton ATPase, a cathepsin L-like protease (TgCPL), an aquaporin (TgAQP1), as well as Ca2+/H+ and Na+/H + exchange activities, supports similarity to the plant vacuole. Biochemical characterization of TgVP1 in enriched fractions shows a functional similarity to the respective plant enzyme. The organelle is a Ca2+ store and appears to have protective effects against salt stress potentially linked to its sodium transport activity. In intracellular parasites, the organelle fragments, with some markers colocalizing with the late endosomal marker, Rab7, suggesting its involvement with the endocytic pathway. Studies on the characterization of this novel organelle will be relevant to the identification of novel targets for chemotherapy against T. gondii and other apicomplexan parasites as well.
UR - http://www.scopus.com/inward/record.url?scp=77953484215&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2958.2010.07165.x
DO - 10.1111/j.1365-2958.2010.07165.x
M3 - Article
C2 - 20398214
AN - SCOPUS:77953484215
SN - 0950-382X
VL - 76
SP - 1358
EP - 1375
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 6
ER -