Next Article in Journal
Bioactive Polycyclic Quinones from Marine Streptomyces sp. 182SMLY
Previous Article in Journal
Specific Metabolites in a Phaeodactylum tricornutum Strain Isolated from Western Norwegian Fjord Water
Article Menu

Export Article

Open AccessArticle
Mar. Drugs 2016, 14(1), 11; doi:10.3390/md14010011

Recombinant Expression and Characterization of α-Conotoxin LvIA in Escherichia coli

Key Laboratory of Tropical Biological Resources, Ministry of Education, Key Laboratory for Marine Drugs of Haikou, Hainan University, Haikou 570228, China
College of Horticulture and Landscapes, Hainan University, Haikou 570228, China
College of Marine Science, Hainan University, Haikou 570228, China
Author to whom correspondence should be addressed.
Academic Editor: Paul Long
Received: 13 October 2015 / Revised: 11 December 2015 / Accepted: 28 December 2015 / Published: 5 January 2016
View Full-Text   |   Download PDF [2957 KB, uploaded 5 January 2016]   |  


α-Conotoxin LvIA is derived from Conus lividus, native to Hainan, and is the most selective inhibitor of α3β2 nicotinic acetylcholine receptors (nAChRs) known to date. In this study, an efficient approach for the production of recombinant α-Conotoxin LvIA is described. Tandem repeats of a LvIA gene fragment were constructed and fused with a KSI gene and a His6 tag in a Escherichia coli (E. coli) expression vector pET-31b(+). The recombinant plasmids were transformed into E. coli and were found to express well. The KSI-(LvIA)n-His6 fusion protein was purified by metal affinity chromatography and then cleaved with CNBr to release recombinant LvIA (rLvIA). High yields of fusion protein ranging from 100 to 500 mg/L culture were obtained. The pharmacological profile of rLvIA was determined by two-electrode voltage-clamp electrophysiology in Xenopus laevis oocytes expressing rat nAChR subtypes. The rLvIA antagonized the α3β2 nAChR subtype selectively with a nano-molar IC50. The rLvIA was analgesic in a mouse hot-plate test model of pain. Overall, this study provides an effective method to synthesize α-conotoxin LvIA in an E. coli recombinant expression system, and this approach could be useful to obtain active conopeptides in large quantity and at low cost. View Full-Text
Keywords: α-conotoxin LvIA; recombinant expression; fusion protein; nAChRs; electrophysiology; pain assay α-conotoxin LvIA; recombinant expression; fusion protein; nAChRs; electrophysiology; pain assay

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 alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Zhu, X.; Bi, J.; Yu, J.; Li, X.; Zhang, Y.; Zhangsun, D.; Luo, S. Recombinant Expression and Characterization of α-Conotoxin LvIA in Escherichia coli. Mar. Drugs 2016, 14, 11.

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



[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top