Next Article in Journal
The Role of Toxins in the Pursuit for Novel Analgesics
Next Article in Special Issue
Evaluation of the Liver Toxicity of Pterocephalus hookeri Extract via Triggering Necrosis
Previous Article in Journal
Evaluation of Mycotoxin Screening Tests in a Verification Study Involving First Time Users
Previous Article in Special Issue
Augmentation of Saporin-Based Immunotoxins for Human Leukaemia and Lymphoma Cells by Triterpenoid Saponins: The Modifying Effects of Small Molecule Pharmacological Agents
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessCommunication

The Inhibitory Effect of Celangulin V on the ATP Hydrolytic Activity of the Complex of V-ATPase Subunits A and B in the Midgut of Mythimna separata

1,†, 1,†, 1, 1, 2 and 1,*
1
College of Chemistry and Pharmacy, Northwest A&F University, Yangling 712100, China
2
College of Life Sciences, Northwest A&F University, Yangling 712100, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Toxins 2019, 11(2), 130; https://doi.org/10.3390/toxins11020130
Received: 17 January 2019 / Revised: 16 February 2019 / Accepted: 18 February 2019 / Published: 22 February 2019
(This article belongs to the Collection Toxic and Pharmacological Effect of Plant Toxins)
  |  
PDF [1549 KB, uploaded 22 February 2019]
  |     |  

Abstract

Celangulin V (CV) is a compound isolated from Celastrus angulatus Max that has a toxic activity against agricultural insect pests. CV can bind to subunits a, H, and B of the vacuolar ATPase (V-ATPase) in the midgut epithelial cells of insects. However, the mechanism of action of CV is still unclear. In this study, the soluble complex of the V-ATPase A subunit mutant TSCA which avoids the feedback inhibition by the hydrolysate ADP and V-ATPase B subunit were obtained and then purified using affinity chromatography. The H+K+-ATPase activity of the complex and the inhibitory activity of CV on ATP hydrolysis were determined. The results suggest that CV inhibits the ATP hydrolysis, resulting in an insecticidal effect. Additionally, the homology modeling of the AB complex and molecular docking results indicate that CV can competitively bind to the AB complex at the ATP binding site, which inhibits ATP hydrolysis. These findings suggest that the AB subunits complex is one of the potential targets for CV and is important for understanding the mechanism of interaction between CV and V-ATPase. View Full-Text
Keywords: Celangulin V; Mythimna separata Walker; V-ATPase AB subunits complex; ATP hydrolysis Celangulin V; Mythimna separata Walker; V-ATPase AB subunits complex; ATP hydrolysis
Figures

Figure 1

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

Ding, L.; Guo, Z.; Xu, H.; Li, T.; Wang, Y.; Tao, H. The Inhibitory Effect of Celangulin V on the ATP Hydrolytic Activity of the Complex of V-ATPase Subunits A and B in the Midgut of Mythimna separata. Toxins 2019, 11, 130.

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