Molecular Characterization of a Novel Big Defensin from Clam Venerupis philippinarum
Zhao, Jianmin1; Li, Chenghua1,2; Chen, Aiqin1; Li, Lingyun3; Su, Xiurong2; Li, Taiwu2
2010-10-20
Source PublicationPLOS ONE
ISSN1932-6203
Volume5Issue:10Pages:e13480-
Contribution Rank[Zhao, Jianmin; Li, Chenghua; Chen, Aiqin] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai, Peoples R China; [Li, Chenghua; Su, Xiurong; Li, Taiwu] Ningbo Univ, Fac Life Sci & Biotechnol, Ningbo, Peoples R China; [Li, Lingyun] NE Agr Univ, Coll Anim Sci & Technol, Harbin, Peoples R China
AbstractAntimicrobial peptides (AMPs) are important mediators of the primary defense mechanism against microbial invasion. In the present study, a big defensin was identified from Venerupis philippinarum haemocytes (denoted as VpBD) by RACE and EST approaches. The VpBD cDNA contained an open reading frame (ORF) of 285 bp encoding a polypeptide of 94 amino acids. The deduce amino acid sequence of VpBD shared the common features of big defensin including disulfide array organization and helix structure, indicating that VpBD should be a new member of the big defensin family. The mRNA transcript of VpBD was up-regulated significantly during the first 24 hr after Vibrio anguillarum challenge, which was 7.4-fold increase compared to that of the control group. Then the expression decreased gradually from 24 hr to 96 hr, and the lowest expression level was detected at 96 hr post-infection, which was still 3.9-fold higher than that of control. The mature peptide of VpBD was recombined in Escherichia coli and purified for minimum inhibitory concentration (MIC) determination. The rVpBD displayed broad-spectrum inhibitory activity towards all tested bacteria with the highest activity against Staphyloccocus aureus and Pseudomonas putida. These results indicated that VpBD was involved in the host immune response against bacterial infection and might contribute to the clearance of invading bacteria.; Antimicrobial peptides (AMPs) are important mediators of the primary defense mechanism against microbial invasion. In the present study, a big defensin was identified from Venerupis philippinarum haemocytes (denoted as VpBD) by RACE and EST approaches. The VpBD cDNA contained an open reading frame (ORF) of 285 bp encoding a polypeptide of 94 amino acids. The deduce amino acid sequence of VpBD shared the common features of big defensin including disulfide array organization and helix structure, indicating that VpBD should be a new member of the big defensin family. The mRNA transcript of VpBD was up-regulated significantly during the first 24 hr after Vibrio anguillarum challenge, which was 7.4-fold increase compared to that of the control group. Then the expression decreased gradually from 24 hr to 96 hr, and the lowest expression level was detected at 96 hr post-infection, which was still 3.9-fold higher than that of control. The mature peptide of VpBD was recombined in Escherichia coli and purified for minimum inhibitory concentration (MIC) determination. The rVpBD displayed broad-spectrum inhibitory activity towards all tested bacteria with the highest activity against Staphyloccocus aureus and Pseudomonas putida. These results indicated that VpBD was involved in the host immune response against bacterial infection and might contribute to the clearance of invading bacteria.
Corresponding AuthorZhao, JM, Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai, Peoples R China
KeywordOyster Crassostrea-gigas Antimicrobial Peptides Expression Gene Shrimp Family Penaeidins Proteins Mussels Crab
Department污染过程与控制实验室 
Subject AreaBiology ; Multidisciplinary Sciences
Funding OrganizationChinese Academy of Sciences [kzcx2-yw-225]; NSFC [30901115]
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Indexed BySCI
WOS KeywordOYSTER CRASSOSTREA-GIGAS ; ANTIMICROBIAL PEPTIDES ; EXPRESSION ; GENE ; SHRIMP ; FAMILY ; PENAEIDINS ; PROTEINS ; MUSSELS ; CRAB
SubtypeArticle
Language英语
WOS Research AreaScience & Technology - Other Topics
WOS IDWOS:000283216400009
Citation statistics
Document Type期刊论文
Identifierhttp://ir.yic.ac.cn/handle/133337/3795
Collection中科院海岸带环境过程与生态修复重点实验室_污染过程与控制实验室
Affiliation1.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai, Peoples R China
2.Ningbo Univ, Fac Life Sci & Biotechnol, Ningbo, Peoples R China
3.NE Agr Univ, Coll Anim Sci & Technol, Harbin, Peoples R China
First Author AffilicationYantai Institute of Coastal Zone Research, Chinese Academy of Sciences
Recommended Citation
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Zhao, Jianmin,Li, Chenghua,Chen, Aiqin,et al. Molecular Characterization of a Novel Big Defensin from Clam Venerupis philippinarum[J]. PLOS ONE,2010,5(10):e13480-.
APA Zhao, Jianmin,Li, Chenghua,Chen, Aiqin,Li, Lingyun,Su, Xiurong,&Li, Taiwu.(2010).Molecular Characterization of a Novel Big Defensin from Clam Venerupis philippinarum.PLOS ONE,5(10),e13480-.
MLA Zhao, Jianmin,et al."Molecular Characterization of a Novel Big Defensin from Clam Venerupis philippinarum".PLOS ONE 5.10(2010):e13480-.
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