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Oligomerization of Cry9Aa in solution without receptor binding, is not related with insecticidal activity
Provedor de dados: 69
Autores: Fang,Longfa; Wang,Bo; Zhou,Zishan; Yang,Sujuan; Shu,Changlong; Song,Fuping; Bravo,Alejandra; Soberón,Mario; Zhang,Jie.
Background: Bacillus thuringiensis Cry toxins bind with different insect midgut proteins leading to toxin oligomerization, membrane insertion and pore formation. However, different Cry toxins had been shown to readily form high molecular weight oligomers or aggregates in solution in the absence of receptor interaction. The role of Cry oligomers formed in solution remains uncertain. The Cry9A proteins show high toxicity against different Lepidoptera, and no-cross resistance with Cry1A. Results: Cry9Aa655 protein formed oligomers easily in solution mediated by disulfide bonds, according to SDS-PAGE analysis under non-reducing and reducing conditions. However, oligomerization is not observed if Cry9Aa655 is activated with trypsin, suggesting that cysteine...
Tipo: Journal article
Palavras-chave: Cry9Aa655; Disulfide bonds; Oligomerization; Insecticidal activity.
Ano: 2016
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300006