Next Article in Journal
Hydrogen-Rich Water and Lactulose Protect Against Growth Suppression and Oxidative Stress in Female Piglets Fed Fusarium Toxins Contaminated Diets
Next Article in Special Issue
Tb II-I, a Fraction Isolated from Tityus bahiensis Scorpion Venom, Alters Cytokines’: Level and Induces Seizures When Intrahippocampally Injected in Rats
Previous Article in Journal
Uremic Toxin Clearance and Cardiovascular Toxicities
Previous Article in Special Issue
Antimicrobial and Chemotactic Activity of Scorpion-Derived Peptide, ToAP2, against Mycobacterium massiliensis
Article Menu
Issue 6 (June) cover image

Export Article

Open AccessArticle
Toxins 2018, 10(6), 227; https://doi.org/10.3390/toxins10060227

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.
Received: 23 May 2018 / Accepted: 31 May 2018 / Published: 4 June 2018
(This article belongs to the Special Issue Scorpion Toxins)
View Full-Text   |   Download PDF [1593 KB, uploaded 4 June 2018]   |  

Abstract

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
Figures

Figure 1a

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Zhang, S.; Gao, B.; Wang, X.; Zhu, S. Loop Replacement Enhances the Ancestral Antibacterial Function of a Bifunctional Scorpion Toxin. Toxins 2018, 10, 227.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top