Towards novel Cry toxins with enhanced toxicity/broader: a new chimeric Cry4Ba / Cry1Ac toxin
Attempts have been made to express or to merge different Cry proteins in order to enhance toxic effects against various insects. Cry1A proteins of Bacillus thuringiensis form a typical bipyramidal parasporal crystal and their protoxins contain a highly conserved C-terminal region. A chimerical gene,...
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Veröffentlicht in: | Applied microbiology and biotechnology 2017, Vol.101 (1), p.113-122 |
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Sprache: | eng |
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Zusammenfassung: | Attempts have been made to express or to merge different Cry proteins in order to enhance toxic effects against various insects. Cry1A proteins of
Bacillus thuringiensis
form a typical bipyramidal parasporal crystal and their protoxins contain a highly conserved C-terminal region. A chimerical gene, called
cry(4Ba-1Ac),
formed by a fusion of the N-terminus part of
cry4Ba
and the C-terminus part of
cry1Ac
, was constructed. Its transformation to an acrystalliferous
B. thuringiensis
strain showed that it was expressed as a chimerical protein of 116 kDa, assembled in spherical to amorphous parasporal crystals. The chimerical gene
cry(4Ba-1Ac)
was introduced in a
B. thuringiensis kurstaki
strain. In the generated crystals of the recombinant strain, the presence of Cry(4Ba-1Ac) was evidenced by MALDI-TOF. The recombinant strain showed an important increase of the toxicity against
Culex pipiens
larvae (LC
50
= 0.84 mg l
−1
± 0.08) compared to the wild type strain through the synergistic activity of Cry2Aa with Cry(4Ba-1Ac). The enhancement of toxicity of
B. thuringiensis kurstaki
expressing Cry(4Ba-1Ac) compared to that expressing the native toxin Cry4Ba, might be related to its a typical crystallization properties. The developed fusion protein could serve as a potent toxin against different pests of mosquitoes and major crop plants. |
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ISSN: | 0175-7598 1432-0614 |
DOI: | 10.1007/s00253-016-7766-3 |