Biochemical characterization of the third domain from Bacillus thuringiensis CRY1A toxins

• Published in: Biochemistry and molecular biology international Vol. 45; no. 5; pp. 1011 - 1020
• Main Authors: Vazquez-Padron, R.I, Martinez-Gil, A.F, Ayra-Pardo, C, Gonzalez-Cabrera, J, Prieto-Samsonov, D.L, Riva, G.A. de la
• Format: Journal Article
• Language: English
• Published: England 01.08.1998
• Subjects: Bacillus thuringiensis - chemistry; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - immunology; Bacterial Toxins - chemistry; Bacterial Toxins - genetics; Bacterial Toxins - immunology; Cloning, Molecular; endotoxins; Endotoxins - chemistry; Endotoxins - genetics; Endotoxins - immunology; Enzyme-Linked Immunosorbent Assay; Hemolysin Proteins; Protein Structure, Secondary; recombinant proteins; Recombinant Proteins - chemistry; Solubility
• ISSN: 1039-9712
• DOI: 10.1002/iub.7510450519

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.