Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning

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dc.contributor.authorSang Woon Shin-
dc.contributor.authorSoon Sik Park-
dc.contributor.authorDoo Sang Park-
dc.contributor.authorMi Gwang Kim-
dc.contributor.authorSun Chang Kim-
dc.contributor.authorPaul T Brey-
dc.contributor.authorHo Yong Park-
dc.date.accessioned2017-04-19T08:55:37Z-
dc.date.available2017-04-19T08:55:37Z-
dc.date.issued1998-
dc.identifier.issn09651748-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4523-
dc.description.abstractFollowing injection of bacteria into the hemocoel of the fall webworm, Hyphantria cunea, several inducible genes were identified and characterized using PCR-based differential display (DD-PCR) and subtractive cloning. Ten immune-related cDNA clones (Hdd1, Hdd2, Hdd3, Hdd11, Hdd13, Hdd15, Hdd17, Hdd23, Hs106, Hs302) were isolated and characterized. The deduced amino acid sequence of Hdd2 was shown to be a member of the copper, zinc superoxide dismutase (Cu-Zn SOD) family. The H. cunea Cu-Zn SOD is novel in that it is up-regulated following a bacterial challenge and has a putative signal peptide suggesting its secretion and involvement in the insect immune response. Hdd3 was found to encode a new member of the serpin (serine protease inhibitor) family. The putative lectin corresponding to Hdd15 is of a different kind in that it has two lectin C domains in a single molecule. These two lectin C domains show significant homology to the lectin C domain of Periplaneta lipopolysaccharide binding protein (LPS-BP). Three cloned genes, Hdd17, Hs106 and Hs302, encode a homologue to Bombyx mori Gram negative binding protein, a hemolin-like protein and a attacin-like protein, respectively. The deduced amino acid sequences from Hdd11 showed weak homology with a Locusta migratoria hemolymph protein. On the contrary, Hdd1, Hdd13 and Hdd23 did not reveal any significant homology with known proteins. All of the 10 genes were clearly inducible by E. coli and M. luteus injection. Injection of distilled water only slightly induced mRNA levels. Comparison of temporal mRNA expression following E. coli injection showed three types of expression patterns.-
dc.publisherElsevier-
dc.titleIsolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning-
dc.title.alternativeIsolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning-
dc.typeArticle-
dc.citation.titleInsect Biochemistry and Molecular Biology-
dc.citation.number0-
dc.citation.endPage837-
dc.citation.startPage827-
dc.citation.volume28-
dc.contributor.affiliatedAuthorDoo Sang Park-
dc.contributor.affiliatedAuthorHo Yong Park-
dc.contributor.alternativeName신상운-
dc.contributor.alternativeName박순식-
dc.contributor.alternativeName박두상-
dc.contributor.alternativeName김미광-
dc.contributor.alternativeName김선창-
dc.contributor.alternativeNameBrey-
dc.contributor.alternativeName박호용-
dc.identifier.bibliographicCitationInsect Biochemistry and Molecular Biology, vol. 28, pp. 827-837-
dc.identifier.doi10.1016/S0965-1748(98)00077-0-
dc.subject.keywordExtracellular copper-
dc.subject.keywordZinc superoxide dismutase (Cu-Zn SOD)-
dc.subject.keywordSerine protease inhibitor (serpin)-
dc.subject.keywordLectin-
dc.subject.keywordGram negative binding protein (GNBP)-
dc.subject.keywordHemolin-
dc.subject.keywordAttacin-
dc.subject.localExtracellular copper-
dc.subject.localZinc superoxide dismutase (Cu-Zn SOD)-
dc.subject.localSerine protease inhibitor (serpin)-
dc.subject.localserine protease inhibitor-
dc.subject.localLectin-
dc.subject.localGram negative binding protein (GNBP)-
dc.subject.localHemolin-
dc.subject.localAttacin-
dc.description.journalClassY-
Appears in Collections:
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Division of Biomaterials Research > Industrial Bio-materials Research Center > 1. Journal Articles
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