First molluscan antimicrobial peptide hydramacin in Manila clam: molecular characterization and expression analysis OTHER

DC Field Value Language
dc.contributor.author 이영득 -
dc.contributor.author Saranya Revathy K -
dc.contributor.author 이숙경 -
dc.contributor.author 황일선 -
dc.contributor.author 오철홍 -
dc.contributor.author 강도형 -
dc.contributor.author 신기욱 -
dc.contributor.author 이제히 -
dc.contributor.author Mahanama De Zoysa -
dc.date.accessioned 2020-04-20T05:32:46Z -
dc.date.available 2020-04-20T05:32:46Z -
dc.date.created 2020-01-16 -
dc.date.issued 2014 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/3004 -
dc.description.abstract Objective: To investigate molecular characterization and the immune responses of Manila clam hydramacin (Rp-hdmc).Methods: cDNA sequence of hydramacin was isolated from Manila clam transcriptome database. Molecular characterization of hydramacin cDNA was performed by BLAST and SWISS-MODEL bioinformatics programs. Tissue-specific expression and transcriptional regulation after Vibrio tapetis challenge was done by quantitative real time PCR. Results: Rp-hdmc has 291 bp open reading frame (ORF), encoding 97 amino acids with a mature hydramacin consisting of 77 amino acid residues. In un-challenged clam, Rp-hdmc was constitutively expressed in all tested tissues and the highest expression level was detected in gill. After pathogenic bacteria Vibrio tapetis challenge, Rp-hdmc mRNA was up-regulated in gill and hemocytes.Conclusions: We identified hydramacin cDNA (Rp-hdmc) from mollusk Manila clam that shows the characteristic features of hydramacin sequence. It has eight cysteine residues with four disulfide linkages, three helices and two β-strands in secondary structure. Expression results after V. tapetis challenges suggest that Rp-hdmc is involved in immune response against pathogenic bacteria. hydramacin cDNA was performed by BLAST and SWISS-MODEL bioinformatics programs. Tissue-specific expression and transcriptional regulation after Vibrio tapetis challenge was done by quantitative real time PCR. Results: Rp-hdmc has 291 bp open reading frame (ORF), encoding 97 amino acids with a mature hydramacin consisting of 77 amino acid residues. In un-challenged clam, Rp-hdmc was constitutively expressed in all tested tissues and the highest expression level was detected in gill. After pathogenic bacteria Vibrio tapetis challenge, Rp-hdmc mRNA was up-regulated in gill and hemocytes.Conclusions: We identified hydramacin cDNA (Rp-hdmc) from mollusk Manila clam that shows the characteristic features of hydramacin sequence. It has eight cysteine residues with four disulfide linkages, three helices and two β-strands in secondary structure. Expression results after V. tapetis challenges suggest that Rp-hdmc is involved in immune response against pathogenic bacteria. -
dc.description.uri 1 -
dc.language English -
dc.title First molluscan antimicrobial peptide hydramacin in Manila clam: molecular characterization and expression analysis -
dc.title.alternative First molluscan antimicrobial peptide hydramacin in Manila clam: molecular characterization and expression analysis -
dc.type Article -
dc.citation.endPage 465 -
dc.citation.startPage 460 -
dc.citation.title Journal of Coastal Life Medicine -
dc.citation.volume 2 -
dc.citation.number 6 -
dc.contributor.alternativeName 이영득 -
dc.contributor.alternativeName 오철홍 -
dc.contributor.alternativeName 강도형 -
dc.identifier.bibliographicCitation Journal of Coastal Life Medicine, v.2, no.6, pp.460 - 465 -
dc.description.journalClass 1 -
dc.description.journalRegisteredClass other -
Appears in Collections:
Jeju Research Institute > Jeju Bio Research Center > 1. Journal Articles
Jeju Research Institute > Tropical & Subtropical Research Center > 1. Journal Articles
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