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AuthorDammak, Mariam
AuthorTounsi, Slim
AuthorRousis, Souad
AuthorJaoua, Samir
Available date2015-12-22T08:48:15Z
Publication Date2010-05
Publication NameJournal of Invertebrate Pathology
Identifierhttp://dx.doi.org/10.1016/j.jip.2010.01.006
Citation"Comparative study of Bacillus thuringiensis Cry1Ia and Cry1Aa delta-endotoxins: Activation process and toxicity against Prays oleae", Dammak, Mariam; Tounsi, Slim; Rouis, Souad; Jaoua, Samir, (2010), Journal of Invertebrate Pathology, vol. 104 (1) p. 39-43
ISSN0022-2011
URIhttp://hdl.handle.net/10576/3972
AbstractCry1Ia and Cry1Aa proteins exhibited toxicities against Prays oleae with LC(50) of 189 and 116 ng/cm(2), respectively. The ability to process Cry1Ia11 protoxin by trypsin, chymotrypsin and P. oleae larvae proteases was studied and compared to that of Cry1Aa11. After solubilization under high alkaline condition (50mM NaOH), Cry1Aa11 was converted into a major fragment of 65 kDa, whereas Cry1Ia11 protoxin was completely degraded by P. oleae larvae proteases and trypsin and converted into a major fragment of 70 kDa by chymotrypsin. Using less proteases of P. oleae juice, the degradation of Cry1Ia11 was attenuated. When the solubilization (in 50mM Na(2)CO(3) pH 10.5 buffer) and activation were combined, Cry1Ia11 was converted into a proteolytic product of 70 kDa after 3h of incubation with trypsin, chymotrypsin and P. oleae juice. These results suggest that the in vivo solubilization of Cry1Ia11 was assured by larval proteases after a swelling of the corresponding inclusion due to the alkalinity of the larval midgut.
SponsorMinistère de l’Enseignement Supérieur, de la Recherche Scientifique et de la Technologie
Languageen
PublisherElsevier Inc.
SubjectBacillus thuringiensis
P. oleae
Cry1Aa11
Cry1Ia11
Solubilization
Activation
Proteolysis
Toxicity
Trypsin
Chymotrypsin
Larvae juice
TitleComparative study of Bacillus thuringiensis Cry1Ia and Cry1Aa delta-endotoxins : activation process and toxicity against Prays oleae
TypeArticle
Pagination39-43
Issue Number1
Volume Number104


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