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Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola Inra
Barthe, P.; Pujade-Renaud, V.; Breton, F.; Gargani, D.; Thai, R.; Roumestand, C.; De Lamotte, F..
Cassiicolin is a host-selective toxin (HST) produced by the fungus Corynespora cassiicola (strain CCP). It is responsible for the Corynespora leaf fall (CLF) disease, which is among the main pathologies affecting rubber tree (Hevea brasiliensis). Working on purified cassiicolin and using electron microscopy, we have demonstrated that this 27-residue O-glycosylated protein is able to induce cellular damages identical to those induced by the fungus on rubber tree leaves and displays the same host selectivity. The solution structure and disulfide pairing of cassiicolin have been determined using NMR spectroscopy and simulated annealing calculations. Cassiicolin appears to have an original structure with a prolate ellipsoid shape. It adopts an over-all fold...
Tipo: Journal Article Palavras-chave: STRUCTURE 3D HST; NMR STRUCTURE; POST-TRANSLATIONAL MODIFICATIONS; PATHOGENICITY; HOST SELECTIVE TOXIN.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008998eec19&uri=/notices/prodinra1/2008/08/
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