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

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 vitr...

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Autores principales:	Cong,Lina, Liang,Wenjing, Wu,Yao, Li,Cheng, Chang,Yihai, Dong,Liang, Song,Wanlin, Ma,Jun
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2014
Materias:	Affinity purification Lysozyme peptide Molecular modeling Recombinant protein
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005
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spelling	oai:scielo:S0717-345820140006000052014-12-10High-level soluble expression of the functional peptide derived from the C-terminal domain of the sea cucumber lysozyme and analysis of its antimicrobial activityCong,LinaLiang,WenjingWu,YaoLi,ChengChang,YihaiDong,LiangSong,WanlinMa,Jun Affinity purification Lysozyme peptide Molecular modeling Recombinant protein 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.17 n.6 20142014-11-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005en10.1016/j.ejbt.2014.09.001
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Affinity purification Lysozyme peptide Molecular modeling Recombinant protein
spellingShingle	Affinity purification Lysozyme peptide Molecular modeling Recombinant protein Cong,Lina Liang,Wenjing Wu,Yao Li,Cheng Chang,Yihai Dong,Liang Song,Wanlin Ma,Jun 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
description	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.
author	Cong,Lina Liang,Wenjing Wu,Yao Li,Cheng Chang,Yihai Dong,Liang Song,Wanlin Ma,Jun
author_facet	Cong,Lina Liang,Wenjing Wu,Yao Li,Cheng Chang,Yihai Dong,Liang Song,Wanlin Ma,Jun
author_sort	Cong,Lina
title	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
title_short	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
title_full	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
title_fullStr	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
title_full_unstemmed	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
title_sort	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
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2014
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005
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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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