| Registro completo |
| Provedor de dados: |
Electron. J. Biotechnol.
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| País: |
Chile
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| Título: |
High-level soluble expression of the functional peptide derived from the C-terminal domain of the sea cucumber lysozyme and analysis of its antimicrobial activity
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| Autores: |
Cong,Lina
Liang,Wenjing
Wu,Yao
Li,Cheng
Chang,Yihai
Dong,Liang
Song,Wanlin
Ma,Jun
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| Data: |
2014-11-01
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| Ano: |
2014
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| Palavras-chave: |
Affinity purification
Lysozyme peptide
Molecular modeling
Recombinant protein
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| Resumo: |
Background The sea cucumber lysozyme belongs to the family of invertebrate lysozymes and is thought to be a key defense factor in protecting aquaculture animals against bacterial infection. Recently, evidence was found that the sea cucumber lysozyme exerts broad spectrum antimicrobial action in vitro against Gram-negative and Gram-positive bacteria, and it also has more potent antimicrobial activity independent of its enzymatic activity. To explore the antimicrobial role of this non-enzymatic lysozyme and model its structure to novel antimicrobial peptides, the peptide from the C-terminal amino acid residues 70-146 of the sea cucumber lysozyme in Stichopus japonicus (SjLys-C) was heterologously expressed in Escherichia coli Rosetta(DE3)pLysS. Results The fusion protein system led to over-expression of the soluble and highly stable product, an approximate 26 kDa recombinant SjLys-C protein (rSjLys-C). The present study showed that rSjLys-C displayed strong antimicrobial activity against the tested Gram-positive and Gram-negative bacteria. In particular, the heat-treated rSjLys-C exhibited more inhibitive activity than the native rSjLys-C. The structural analysis of SjLys-C showed that it is a typical hydrophilic peptide and contains a helix-loop-helix motif. The modeling of SjLys-C molecular structures at different temperatures revealed that the tertiary structure of SjLys-C at 100°C underwent a conformational change which is favorable for enhancing antimicrobial activity. Conclusion These results indicate that the expressed rSjLys-C is a highly soluble product and has a strong antimicrobial activity. Therefore, gaining a large quantity of biologically active rSjLys-C will be used for further biochemical and structural studies and provide a potential use in aquaculture and medicine.
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| Tipo: |
Journal article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005
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| Editor: |
Pontificia Universidad Católica de Valparaíso
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| Formato: |
text/html
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| Fonte: |
Electronic Journal of Biotechnology v.17 n.6 2014
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