• BMB Reports
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• v.53 no.5
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• pp.260-265
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• 2020

Scorpion venom comprises a cocktail of toxins that have proven to be useful molecular tools for studying the pharmacological properties of membrane ion channels. HelaTx1, a short peptide neurotoxin isolated recently from the venom of the scorpion Heterometrus laoticus, is a 25 amino acid peptide with two disulfide bonds that shares low sequence homology with other scorpion toxins. HelaTx1 effectively decreases the amplitude of the K⁺ currents of voltage-gated Kv1.1 and Kv1.6 channels expressed in Xenopus oocytes, and was identified as the first toxin member of the κ-KTx5 subfamily, based on a sequence comparison and phylogenetic analysis. In the present study, we report the NMR solution structure of HelaTx1, and the major interaction points for its binding to voltage-gated Kv1.1 channels. The NMR results indicate that HelaTx1 adopts a helix-loop-helix fold linked by two disulfide bonds without any β-sheets, resembling the molecular folding of other cysteine-stabilized helix-loop-helix (Cs α/α) scorpion toxins such as κ-hefutoxin, HeTx, and OmTx, as well as conotoxin pl14a. A series of alanine-scanning analogs revealed a broad surface on the toxin molecule largely comprising positively-charged residues that is crucial for interaction with voltage-gated Kv1.1 channels. Interestingly, the functional dyad, a key molecular determinant for activity against voltage-gated potassium channels in other toxins, is not present in HelaTx1.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2005.04a
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• pp.47-47
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• 2005

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.281-286
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• 2010

A Pseudomonas fluorescens strain was isolated and found to show antagonistic activity against phytopathogenic fungi and to possess a gene responsible for production of antibiotic 2,4-diacetylphloroglucinol. For the extension of biocontrol range, a gene for an Androetonus australis Hector insect toxin 1 (AaHIT1), one of the most known toxic insect-selective peptides, was designed and synthesized according to the preferred codon usage of Pseudomonas fluorescens, cloned, and transformed into the strain by pSUP106 vector, a broad-host-range plasmid. Bioassays indicated that the engineered strain was able to produce AaHIT1 with insecticidal activity, and at the same time retain the activity against plant pathogen. The experiments for nonplanted soil and rhizosphere colonization showed that, similar to the population of the wild-type strain, that of the engineered strain remained relatively constant in the first 10 days, and the subsequent 50 days, suggesting that AaHIT1 expression in the bacterial cell does not substantially impair its long-term colonization. It is first reported that a Pseudomonas fluorescens strain expressing an active scorpion neurotoxin has dual activity against phytopathogenic fungi and insects, making at attractive for agronomic applications.