Insecticidal toxin complex proteins from Xenorhabdus nematophilus: structure and pore formation.

Toxin complexes from Xenorhabdus and Photorhabdus spp. bacteria represent novel insecticidal proteins. We purified a native toxin complex (toxin complex 1) from Xenorhabdus nematophilus.

Purification and characterization of a chimeric Cry1F delta-endotoxin expressed in transgenic cotton plants.

Cotton plants were genetically modified through the introduction of a synthetic gene that encodes a Bacillus thuringiensis insecticidal protoxin referred to as Cry1F(synpro). This protoxin is a chimeric, full-length delta-endotoxin of 130 kDa, comprised of the core toxin of Cry1Fa2 protein and parts of the nontoxic portions of Cry1Ca3 and Cry1Ab1 proteins, all of which originated from Bacillus thuringiensis. The Cry1F(synpro) expressed in cotton plants confers resistance to lepidopteran pests.