Ruiz de Escudero Fuentemilla, Íñigo

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https://academica-e.unavarra.es/handle/2454/49921

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Ruiz de Escudero Fuentemilla

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Íñigo

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Agronomía, Biotecnología y Alimentación

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IMAB. Research Institute for Multidisciplinary Applied Biology

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0000-0002-8698-1481

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88564

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2331

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20111
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Subject: Cyt1Aa toxin ×

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    PublicationOpen Access
    The amino- and carboxyl-terminal fragments of the Bacillus thuringensis Cyt1Aa toxin have differential roles on toxin oligomerization and pore formation
    (American Chemical Society, 2011) Rodríguez Almazán, Claudia; Ruiz de Escudero Fuentemilla, Íñigo; Cantón, Pablo Emiliano; Muñoz Garay, Carlos; Pérez, Claudia; Gill, Sarjeet S.; Soberón, Mario; Bravo, Alejandra; IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua; Universidad Pública de Navarra / Nafarroako Unibertsitate Publikoa
    The Cyt toxins produced by the bacteria Bacillus thuringiensis show insecticidal activity against some insects, mainly dipteran larvae, being able to kill mosquitoes and black flies. However, they also possess a general cytolytic activity in vitro showing hemolytic activity in red blood cells. These proteins are composed of two outer layers of α-helix hairpins wrapped around a β-sheet. Regarding to their mode of action, one model proposed that the two outer layers of α-helix hairpins swing away from the β-sheet allowing insertion of β-strands into the membrane forming a pore after toxin oligomerization. The other model suggested a detergent-like mechanism of action of the toxin on the surface of the lipid bilayer. In this work we cloned the N- and C-terminal domains form Cyt1Aa and analyzed their effects in Cyt1Aa toxin action. The N-terminal domain shows a dominant negative phenotype inhibiting the in vitro hemolytic activity of Cyt1Aa in red blood cells and the in vivo insecticidal activity of Cyt1Aa against Aedes aegypti larvae. In addition, N-terminal region is able to induce aggregation of Cyt1Aa toxin in solution. Finally, Cterminal domain composed mainly of β-strands, is able to bind to the SUV liposomes, suggesting that this region of the toxin is involved in membrane interaction. Overall, our data indicate that the two isolated domains of Cyt1Aa have different roles in toxin action. The N-terminal region is involved in toxin aggregation while the C-terminal domain in the interaction of the toxin with the lipid membrane.