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Theobroma cacao cystatins impair Moniliophthora perniciosa mycelial growth and are involved in postponing cell death symptoms

Carlos Priminho Pirovani, André da Silva Santiago, Lívia Santana dos Santos, Fabienne Micheli, Rogério Margis, Abelmon da Silva Gesteira, Fátima Cerqueira Alvim, Gonçalo Amarante Guimarães Pereira and Júlio Cézar de Mattos Cascardo
Planta
Vol. 232, No. 6 (November 2010), pp. 1485-1497
Published by: Springer
Stable URL: http://www.jstor.org/stable/23391912
Page Count: 13
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Abstract

Three cystatin open reading frames named TcCys1, TcCys2 and TcCys3 were identified in cDNA libraries from compatible interactions between Theobroma cacao (cacao) and Moniliophthora perniciosa. In addition, an ORF named TcCys4 was identified in the cDNA library of the incompatible interaction. The cDNAs encoded conceptual proteins with 209, 127, 124, and 205 amino acid residues, with a deduced molecular weight of 24.3, 14.1, 14.3 and 22.8 kDa, respectively. His-tagged recombinant proteins were purified from Escherichia coli expression, and showed inhibitory activities against M. perniciosa. The four recombinant cystatins exhibited Ki values against papain in the range of 152—221 nM. Recombinant TcCYS3 and TcCYS4 immobilized in CNBr—Sepharose were efficient to capture M. perniciosa proteases from culture media. Polyclonal antibodies raised against the recombinant TcCYS4 detected that the endogenous protein was more abundant in young cacao tissues, when compared with mature tissues. A ∼85 kDa cacao multicystatin induced by M. perniciosa inoculation, MpNEP (necrosis and ethylene-inducing protein) and M. perniciosa culture supernatant infiltration were detected by anti-TcCYS4 antibodies in cacao young tissues. A direct role of the cacao cystatins in the defense against this phytopathogen was proposed, as well as its involvement in the development of symptoms of programmed cell death.

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