The entomocidal δ-endotoxins CytA and CytB produced by () subspecies and respectively showed a similar level of toxicity to mosquito larvae but were not toxic to the larvae of the lepidopteran CytA and CytB are also similar in sequence, predicted secondary structure and α-helical content, the only obvious difference being a C-terminal fifteen residue ‘tail’ on CytB. Investigations of the function, if any, of the CytB C-terminal ‘tail’ showed that this δ-endotoxin is highly expressed and forms inclusions in an acrystalliferous mutant without the aid of the 20 kDa ‘helper’ protein from subspecies which is essential for CytA inclusion formation. After proteinase K treatment, CytA and CytB were processed to virtually the same points in a sequence alignment and were equally haemolytic However, the results suggested that unprocessed CytB differs from unprocessed CytA in that the former is not haemolytic.


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