Cloning and purification of the first termicin-like peptide from the cockroach Eupolyphaga sinensis

The Journal of Venomous Animals and Toxins Including Tropical Diseases
Zichao LiuDingkang Wang

Abstract

Termicin is an antimicrobial peptide with six cysteines forming three disulfide bridges that was firstly isolated from the salivary glands and hemocytes of the termite Pseudacanthotermes spiniger. In contrast to many broad-spectrum antimicrobial peptides, termicin is most active against filamentous fungi. Although more than one hundred complementary DNAs (cDNAs) encoding termicin-like peptides have been reported to date, all these termicin-like peptides were obtained from Isoptera insects. The cDNA was cloned by combination of cDNA library construction kit and DNA sequencing. The polypeptide was purified by gel filtration and reversed-phase high performance liquid chromatography (RP-HPLC). Its amino acid sequence was determined by Edman degradation and mass spectrometry. Antimicrobial activity was tested against several bacterial and fungal strains. The minimum inhibitory concentration (MIC) was determined by microdilution tests. A novel termicin-like peptide with primary structure ACDFQQCWVTCQRQYSINFISARCNGDSCVCTFRT was purified from extracts of the cockroach Eupolyphaga sinensis (Insecta: Blattodea). The cDNA encoding Es-termicin was cloned by cDNA library screening. This cDNA encoded a 60 amino acid precursor which included ...Continue Reading

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Citations

Aug 10, 2016·Future Medicinal Chemistry·Tecla CiociolaLuciano Polonelli
Nov 8, 2017·Toxins·Michal LinialDan Ofer

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Datasets Mentioned

BETA
KR014250

Methods Mentioned

BETA
gel filtration
PCR

Software Mentioned

MEGA
SignalP
ExPASy MW /
ClustalW2

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