Vip3Aa from Bacillus thuringiensis subsp. kurstaki HD1 is toxic to Aedes aegypti (Diptera: Culicidae)

Wang, Junhui; Wang, Jiayu; He, Jiali; Wu, Jiangyu; Sun, Jiazhi; Wang, Ruiping; Zhang, Wenfei

doi:10.1016/j.jip.2020.107342

Cited by 9 publications

(1 citation statement)

References 14 publications

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“…Initially, it was shown that Vip3 was lepidopteran specific. However, activity against other insect targets, such as the cockroach species Periplaneta americana and Blattella germanica ( 60 ), and the mosquito species Aedes aegypti ( 61 ), has been reported. Unlike Cry toxins, which accumulate in parasporal bodies inside the bacterial sporangium, Vip3 proteins are secreted by the Bt bacterium during the vegetative growth phase, and their production continues during the sporulation growth phase ( 62 ).…”

Section: Structural Changes Of Vip3 Toxins During Pore Formationmentioning

confidence: 99%

Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced by Bacillus thuringiensis

et al. 2023

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Different Bacillus thuringiensis (Bt) strains produce a broad variety of pore-forming toxins (PFTs) that show toxicity against insects and other invertebrates. Some of these insecticidal PFT proteins have been used successfully worldwide to control diverse insect crop pests. There are several studies focused on describing the mechanism of action of these toxins that have helped to improve their performance and to cope with the resistance evolved by different insects against some of these proteins. However, crucial information that is still missing is the structure of pores formed by some of these PFTs, such as the three-domain crystal (Cry) proteins, which are the most commercially used Bt toxins in the biological control of insect pests. In recent years, progress has been made on the identification of the structural changes that certain Bt insecticidal PFT proteins undergo upon membrane insertion. In this review, we describe the models that have been proposed for the membrane insertion of Cry toxins. We also review the recently published structures of the vegetative insecticidal proteins (Vips; e.g. Vip3) and the insecticidal toxin complex (Tc) in the membrane-inserted state. Although different Bt PFTs show different primary sequences, there are some similarities in the three-dimensional structures of Vips and Cry proteins. In addition, all PFTs described here must undergo major structural rearrangements to pass from a soluble form to a membrane-inserted state. It is proposed that, despite their structural differences, all PFTs undergo major structural rearrangements producing an extended α-helix, which plays a fundamental role in perforating their target membrane, resulting in the formation of the membrane pore required for their insecticidal activity.

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Section: Structural Changes Of Vip3 Toxins During Pore Formationmentioning

confidence: 99%