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Identification and characterization of a novel O‐superfamily conotoxin from Conus litteratus
Author(s) -
Wang Lei,
Pi Canhui,
Liu Junliang,
Chen Shangwu,
Peng Can,
Sun Dandan,
Zhou Maojun,
Xiang Hui,
Ren Zhenghua,
Xu Anlong
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1044
Subject(s) - conotoxin , conus , signal peptide , peptide , complementary dna , cdna library , peptide sequence , biochemistry , open reading frame , biology , microbiology and biotechnology , chemistry , anatomy , gene
A novel conotoxin named lt6c, an O‐superfamily conotoxin, was identified from the cDNA library of venom duct of Conus litteratus . The full‐length cDNA contains an open reading frame encoding a predicted 22‐residue signal peptide, a 22‐residue proregion and a mature peptide of 28 amino acids. The signal peptide sequence of lt6c is highly conserved in O‐superfamily conotoxins and the mature peptide consists of six cysteines arranged in the pattern of CCCCCC that is defined the O‐superfamily of conotoxins. The mature peptide fused with thioredoxin, 6‐His tag, and a Factor Xa cleavage site was successfully expressed in Escherichia coli . About 12 mg lt6c was purified from 1L culture. Under whole‐cell patch‐clamp mode, lt6c inhibited sodium currents on adult rat dorsal root ganglion neurons. Therefore, lt6c is a novel O‐superfamily conotoxin that is able to block sodium channels. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.