Biochemical characterization of the third domain from Bacillus thuringiensis Cry1A toxins.
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.
Vázquez-Padrón
R I
RI
Department of Environment Biotechnology, Center for Genetic Engineering and Biotechnology (CIGB), Havana, Cuba.
Martínez-Gil
A F
AF
Ayra-Pardo
C
C
González-Cabrera
J
J
Prieto-Samsonov
D L
DL
de la Riva
G A
GA
D001413:Bacillus thuringiensis / Q000737:chemistry*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D001427:Bacterial Toxins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D003001:Cloning, Molecular; D004731:Endotoxins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D006460:Hemolysin Proteins; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D012995:Solubility
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011994:Recombinant Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis