DELETION BY INVIVO RECOMBINATION SHOWS THAT THE 28-KILODALTON CYTOLYTIC POLYPEPTIDE FROM BACILLUS-THURINGIENSIS SUBSP ISRAELENSIS IS NOT ESSENTIAL FOR MOSQUITOCIDAL ACTIVITY
DELETION BY INVIVO RECOMBINATION SHOWS THAT THE 28-KILODALTON CYTOLYTIC POLYPEPTIDE FROM BACILLUS-THURINGIENSIS SUBSP ISRAELENSIS IS NOT ESSENTIAL FOR MOSQUITOCIDAL ACTIVITY
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DOI：
10.1128/jb.173.11.3374-3381.1991
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发表时间：
1991-06-01
影响因子：
3.2
通讯作者：
RAPOPORT, G
中科院分区：
文献类型：
--
作者：
DELECLUSE, A;CHARLES, JF;RAPOPORT, G
The cytA gene encoding the 28-kDa polypeptide of Bacillus thuringiensis subsp. israelensis crystals was disrupted in the 72-MDa resident plasmid by in vivo recombination, thus indicating that homologous recombination occurs in B. thuringiensis. The absence of the 28-kDa protein in B. thuringiensis did not affect the crystallization of the other toxic components of the parasporal body (68-, 125-, and 135-kDa polypeptides). The absence of the 28-kDa protein abolished the hemolytic activity of B. thuringiensis subsp. israelensis crystals. However, the mosquitocidal activity of the 28-kDa protein-free crystals did not differ significantly from that of the wild-type crystals when tested on Aedes aegypti and Culex pipiens larvae. The 28-kDa protein contributed slightly to the toxicity to Anopheles stephensi larvae. This indicates that the 28-kDa protein is not essential for mosquitocidal activity, at least against the three species tested.
