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Open AccessArticle

Loop Replacement Enhances the Ancestral Antibacterial Function of a Bifunctional Scorpion Toxin

Group of Peptide Biology and Evolution, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, 1 Beichen West Road, Chaoyang District, Beijing 100101, China
Author to whom correspondence should be addressed.
Toxins 2018, 10(6), 227;
Received: 23 May 2018 / Accepted: 31 May 2018 / Published: 4 June 2018
(This article belongs to the Special Issue Scorpion Toxins)
On the basis of the evolutionary relationship between scorpion toxins targeting K+ channels (KTxs) and antibacterial defensins (Zhu S., Peigneur S., Gao B., Umetsu Y., Ohki S., Tytgat J. Experimental conversion of a defensin into a neurotoxin: Implications for origin of toxic function. Mol. Biol. Evol. 2014, 31, 546–559), we performed protein engineering experiments to modify a bifunctional KTx (i.e., weak inhibitory activities on both K+ channels and bacteria) via substituting its carboxyl loop with the structurally equivalent loop of contemporary defensins. As expected, the engineered peptide (named MeuTXKα3-KFGGI) remarkably improved the antibacterial activity, particularly on some Gram-positive bacteria, including several antibiotic-resistant opportunistic pathogens. Compared with the unmodified toxin, its antibacterial spectrum also enlarged. Our work provides a new method to enhance the antibacterial activity of bifunctional scorpion venom peptides, which might be useful in engineering other proteins with an ancestral activity. View Full-Text
Keywords: scorpion K+ channel toxin; MeuTXKα3; defensin; loop; scaffold scorpion K+ channel toxin; MeuTXKα3; defensin; loop; scaffold
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Zhang, S.; Gao, B.; Wang, X.; Zhu, S. Loop Replacement Enhances the Ancestral Antibacterial Function of a Bifunctional Scorpion Toxin. Toxins 2018, 10, 227.

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