Membrane binding and oligomer membrane insertion are necessary but insufficient for Bacillus thuringiensis Cyt1Aa toxicity

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• 作者：Pablo Emiliano Cantó ; n^a ; ^{emiliano@ibt.unam.mx" class="auth_mail} ; Jazmin A. Ló ; pez-Dí ; az^a ; ^{jazald@ibt.unam.mx" class="auth_mail} ; Sarjeet S. Gill^b ; ^{sarjeet.gill@ucr.edu" class="auth_mail} ; Alejandra Bravo^a ; ^{bravo@ibt.unam.mx" class="auth_mail} ; Mario Soberó ; n^a ; ^{mario@ibt.unam.mx" class="auth_mail} ; ^{mario.soberon@yahoo.com" class="auth_mail}
• 关键词：Cry ; crystal proteins ; PFT ; pore forming toxins ; Bt ; Bacillus thuringiensis ; Bti ; Bacillus thuringiensis subs israelensis ; BBMV ; brush border membrane vesicles ; LC50 ; median lethal concentration ; SUV ; small unilamellar vesicles
• 刊名：Peptides
• 出版年：March, 2014
• 年：2014
• 卷：53
• 期：Complete
• 页码：286-291
• 全文大小：857 K

文摘

Bacillus thuringiensis Cyt proteins are pore-forming toxins that have insecticidal activity mainly against dipteran insects. However, certain Cyt proteins have toxicity to some insect orders, but not toxicity of Cyt1Aa against lepidopteran larvae has been found. Insect specificity has been proposed to rely in specific binding to certain lipids on the brush border membrane of midgut cells since no protein receptors have been described so far. To determine the molecular basis of Cyt1Aa insect specificity we compared different steps of Cyt1Aa mode of action in a susceptible insect as the dipteran Aedes aegypti and also in the non-susceptible lepidopteran Manduca sexta. Our data shows that the lack toxicity of Cyt1Aa to M. sexta larvae does not rely on protoxin processing, membrane binding interaction, and oligomerization of Cyt1Aa since these steps were similar in the two insect species analyzed.