Cloning, prokaryotic expression and antibacterial assay of Tenecin gene encoding an antibacterial peptide from Tenebrio molitor / 南方医科大学学报
Journal of Southern Medical University
;
(12): 2002-2005, 2011.
Artigo
em Chinês
| WPRIM
| ID: wpr-265731
ABSTRACT
<p><b>OBJECTIVE</b>To clone tenecin gene, an antibacterial peptide gene, from Tenebrio molitor for its prokaryotic expression and explore the molecular mechanism for regulating the expression of antibacterial peptide in Tenebrio molitor larvae.</p><p><b>METHODS</b>The antibacterial peptide was induced from the larvae of Tenebrio molitor by intraperitoneal injection of Escherichia coli DH-5α (1×10(8)/ml). RT-PCR was performed 72 h after the injection to clone Tenecin gene followed by sequencing and bioinformatic analysis. The recombinant expression vector pET-28a(+)-Tenecin was constructed and transformed into E. coli BL21(DE3) cells and the expression of tenecin protein was observed after IPTG induction.</p><p><b>RESULTS</b>Tenecin expression was detected in transformed E.coli using SDS-PAGE after 1 mmol/L IPTG induction. Tenecin gene, which was about 255 bp in length, encoded Tenecin protein with a relative molecular mass of 9 kD. Incubation of E.coli with 80, 60, 40, and 20 µg/ml tenecin for 18 h resulted in a diameter of the inhibition zone of 25.1∓0.03, 20.7∓0.06, 17.2∓0.11 and 9.3∓0.04 mm, respectively.</p><p><b>CONCLUSIONS</b>Tenecin protein possesses strong antibacterial activity against E. coli DH-5α, which warrants further study of this protein for its potential as an antibacterial agent in clinical application.</p>
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Farmacologia
/
Tenebrio
/
Proteínas Recombinantes de Fusão
/
Dados de Sequência Molecular
/
Testes de Sensibilidade Microbiana
/
Química
/
Sequência de Aminoácidos
/
Clonagem Molecular
/
Proteínas de Insetos
/
Peptídeos Catiônicos Antimicrobianos
Limite:
Animais
Idioma:
Chinês
Revista:
Journal of Southern Medical University
Ano de publicação:
2011
Tipo de documento:
Artigo
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