Cloning and characterization of a novel Bacillus thuringiensis cytolytic delta-endotoxin

Pandelakis Koni, D. J. Ellar

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


A gene encoding a major entomocidal polypeptide from Bacillus thuringiensis subspecies kyushuensis Δ-endotoxin crystals (CytB) was cloned into Escherichia coli and sequenced. The deduced amino acid sequence gave a predicted molecular mass of 29 236 Da and showed 39% identity and 70% similarity with the 27,371 Da CytA protein from Bacillus thuringiensis subspecies israelensis. The larger size of CytB compared to CytA appears to be due to additional sequence in CytB after the CytA C-terminus. Unlike CytA, CytB was freely expressed in Escherichia coli and formed cytoplasmic inclusions without the need for a “helper” protein. Electron microscopic observation of CytB inclusions revealed them to be generally amorphous, but examples possessing some lattice structure were seen.

Original languageEnglish (US)
Pages (from-to)319-327
Number of pages9
JournalJournal of Molecular Biology
Issue number2
StatePublished - Jan 20 1993


  • Bacillus thuringiensis
  • Cloning
  • Expression
  • Sequence
  • Δ-endotoxin

ASJC Scopus subject areas

  • Molecular Biology


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