C. Rang et al., Exchange of domain I from Bacillus thuringiensis Cry1 toxins influences protoxin stability and crystal formation, CURR MICROB, 43(1), 2001, pp. 1-6
Influence of domain I exchange on the stability and production of Bacillus
thuringiensis Cry1 protoxins as well as on the shape of inclusion and toxic
ity to Spodoptera exigua and Plutella xylostella larvae was investigated. C
himeric genes were prepared by exchanging the regions coding for domain I b
etween Cry1Aa, Cry1Ab, Cry1Ac, Cry1C, and Cry1E. The AcCC chimera accumulat
ed into bipyramidal inclusion bodies, whereas CEE produced round-shaped inc
lusion bodies, and ECC and AaEE protoxins produced small granules. AbEE and
EAaAa did not produce any inclusion body and were visualized by immunodete
ction only. AcCC, GEE, ECC, and AaEE were stable to trypsin, whereas AbEE a
nd EAaAa were not. Bioassays showed that the chimeras were not toxic in viv
o. However, S. exigua larvae fed with the activated AcCC toxin displayed a
lower growth rate.