Next Article in Journal
Bee Venom Suppresses the Differentiation of Preadipocytes and High Fat Diet-Induced Obesity by Inhibiting Adipogenesis
Previous Article in Journal
Cellular and Molecular Aspects of the β-N-Methylamino-l-alanine (BMAA) Mode of Action within the Neurodegenerative Pathway: Facts and Controversy
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle

Comparative Proteomic Analysis of the Effect of Periplocoside P from Periploca sepium on Brush Border Membrane Vesicles in Midgut Epithelium of Mythimna separata Larvae

1
Institute of Pesticide Science, College of Plant Protection, Northwest A&F University, Yangling, Shaanxi 712100, China
2
Provincial Key Laboratory for Botanical Pesticide R&D of Shaanxi, Yangling, Shaanxi 712100, China
3
Key Laboratory of Crop Pest Integrated Management on the Loess Plateau, Ministry of Agriculture, Yangling, Shaanxi 712100, China
*
Author to whom correspondence should be addressed.
Received: 21 November 2017 / Revised: 19 December 2017 / Accepted: 19 December 2017 / Published: 22 December 2017
(This article belongs to the Section Plant Toxins)
View Full-Text   |   Download PDF [2171 KB, uploaded 22 December 2017]   |  

Abstract

Periplocoside P (PSP), a novel compound isolated from Periploca sepium Bunge, possesses insecticidal activity against some lepidopterans, such as Mythimna separata. In M. separata, the brush border membrane vesicles of the midgut epithelium are the initial site of action of periplocosides. We conducted two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight/time of flight mass spectrometry analysis to analyze differentially expressed proteins (DEPs) from periplocoside P (PSP)-treated M. separata. We successfully isolated seven up-regulated and three down-regulated DEPs that have been previously identified, as well as a novel DEP. The DEPs are implicated in protein degradation, transporter, folding, and synthesis, and in juvenile hormone biosynthesis. DEPs involved in the oxidative phosphorylation energy metabolism pathway are enriched. Through real-time polymerase chain reaction assay, we confirmed that vma1 expression is significantly up-regulated expression levels in PSP-treated M. separata larvae. Enzymology validation further indicated that PSP can significantly inhibit V-type ATPase activity in a concentration-dependent manner. Given these results, we speculate that in M. separata, the V-type ATPase A subunit in the midgut epithelium is the putative target binding site of periplocosides. This finding provides preliminary evidence for the mode of action of periplocosides. View Full-Text
Keywords: botanical pesticide; periplocoside P; proteomics; brush border membrane vesicles (BBMVs); V-type ATPase A subunit botanical pesticide; periplocoside P; proteomics; brush border membrane vesicles (BBMVs); V-type ATPase A subunit
Figures

Graphical abstract

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).

Share & Cite This Article

MDPI and ACS Style

Feng, M.; Li, Y.; Chen, X.; Wei, Q.; Wu, W.; Hu, Z. Comparative Proteomic Analysis of the Effect of Periplocoside P from Periploca sepium on Brush Border Membrane Vesicles in Midgut Epithelium of Mythimna separata Larvae. Toxins 2018, 10, 7.

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