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Biochemical characterization of the third domain From Bacillus thuringiensis CRY1A Toxins
Author(s) -
VázquezPadrón Robert I.,
MartínezGil Ariel F.,
AyraPardo Camilo,
GonzálezCabrera Joel,
PrietoSamsonov Dmitri L.,
de la Riva Gustavo A.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.7510450519
Subject(s) - bacillus thuringiensis , cry1ac , polyclonal antibodies , toxin , biology , fragment (logic) , microbial toxins , microbiology and biotechnology , antibody , biochemistry , genetically modified crops , bacteria , gene , genetics , transgene , computer science , programming language
Cry proteins from Bacillus thuringiensis have insecticidal properties. The function of domains I and II has been described but domain III has so far eluded understanding. Domain III from Cry1Ab and Cry1Ac has been cloned, expressed in E. coli and injected to rabbits with the aid of characterizing them immunologically. Interestingly, polyclonal antibodies against Cry1Ab fragment did not recognize either the native Cry1Ab toxin or the Cry1Ac fragment while those against the latter did recognize either the native Cry1Ac toxin or the Cry1Ab protein fragment. A combination of information from sequence comparison and hydrophobicity profile indicates that these protein fragments possibly adopt different spatial dispositions within the respective toxins.