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Título : Trypanosoma cruzi calmodulin: Cloning, expression and characterization
Autor : Garcia-Marchan, Y
Sojo, F
Rodriguez, E
Zerpa, N
Malave, C
Galindo-Castro, I
Salerno, M
Benaím, Gustavo
Palabras clave : Calmodulin
Trypanosomatids
Cloning
Calcium
Antibody
Trypanosoma cruzi
Fecha de publicación : 2009
Editorial : Experimental Parasitology
Citación : Vol.123, Nº 4,pp. 326–333
Resumen : We have cloned and expressed calmodulin (CaM) from Trypanosoma cruzi, for the first time, to obtain large amounts of protein. CaM is a very well conserved protein throughout evolution, sharing 100% amino acid sequence identity between different vertebrates and 99% between trypanosomatids. However, there is 89% amino acid sequence identity between T. cruzi and vertebrate CaMs. The results demonstrate significant differences between calmodulin from T. cruzi and mammals. First, a polyclonal antibody developed in an egg-yolk system to the T. cruzi CaM recognizes the autologous CaM but not the CaM from rat. Second, it undergoes a larger increase in the a-helix content upon binding with Ca2+, when compared to CaM from vertebrates. Finally, two classic CaM antagonists, calmidazolium and trifluoperazine, capable of inhibiting the action of CaM in mammals when assayed on the plasma membrane Ca2+ pump, showed a significant loss of activity when assayed upon stimulation with the T. cruzi CaM.
URI : http://saber.ucv.ve/jspui/handle/123456789/4625
ISSN : doi:10.1016/j.exppara.2009.08.010
0014-4894
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