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Potential Use of Genetically Engineered Variable Lymphocyte Receptor B Specific to Avian Influenza Virus H9N2

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dc.contributor.authorIm, Se Pyeong-
dc.contributor.authorKim, Jaesung-
dc.contributor.authorLee, Jung Seok-
dc.contributor.authorKim, Si Won-
dc.contributor.authorJung, Jae Wook-
dc.contributor.authorLazarte, Jassy Mary S.-
dc.contributor.authorKim, Jong Yong-
dc.contributor.authorKim, Young Rim-
dc.contributor.authorLee, Jeong Ho-
dc.contributor.authorChong, Roger S. M.-
dc.contributor.authorJung, Tae Sung-
dc.date.accessioned2022-12-26T16:32:16Z-
dc.date.available2022-12-26T16:32:16Z-
dc.date.issued2018-11-
dc.identifier.issn0022-1767-
dc.identifier.issn1550-6606-
dc.identifier.urihttps://scholarworks.gnu.ac.kr/handle/sw.gnu/11067-
dc.description.abstractThe variable lymphocyte receptor (VLR) B of jawless vertebrates functions as a secreted Ab of jawed vertebrates and has emerged as an alternative Ab with a single polypeptide chain. After observing an upregulated VLRB response in hagfish immunized with avian influenza virus (AIV) subtype H9N2, we screened AIV H9N2-specific VLRB using a mammalian expression system. To improve the binding avidity of the Ag-specific VLRB to the Ag, we enabled multimerization of the VLRB by conjugating it with C-terminal domain of human C4b-binding protein. To dramatically enhance the expression and secretion of the Ag-specific VLRB, we introduced a glycine-serine linker and the murine Ig kappa leader sequence. The practical use of the Ag-specific VLRB was also demonstrated through various immunoassays, detected by anti-VLRB Ab (11G5). Finally, we found that the Ag-specific VLRB decreased the infectivity of AIV H9N2. Together, our findings suggest that the generated Ag-specific VLRB could be used for various immunoapplications.-
dc.format.extent10-
dc.language영어-
dc.language.isoENG-
dc.publisherAmerican Association of Immunologists-
dc.titlePotential Use of Genetically Engineered Variable Lymphocyte Receptor B Specific to Avian Influenza Virus H9N2-
dc.typeArticle-
dc.publisher.location미국-
dc.identifier.doi10.4049/jimmunol.1800981-
dc.identifier.scopusid2-s2.0-85056003272-
dc.identifier.wosid000449433800025-
dc.identifier.bibliographicCitationJournal of Immunology, v.201, no.10, pp 3119 - 3128-
dc.citation.titleJournal of Immunology-
dc.citation.volume201-
dc.citation.number10-
dc.citation.startPage3119-
dc.citation.endPage3128-
dc.type.docTypeArticle-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClasssci-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaImmunology-
dc.relation.journalWebOfScienceCategoryImmunology-
dc.subject.keywordPlusIMMUNE-RESPONSE-
dc.subject.keywordPlusIMMUNOLOGICAL RESPONSES-
dc.subject.keywordPlusMONOCLONAL-ANTIBODIES-
dc.subject.keywordPlusSTRUCTURAL INSIGHTS-
dc.subject.keywordPlusJAWLESS VERTEBRATES-
dc.subject.keywordPlusANTIGEN RECEPTORS-
dc.subject.keywordPlusSEA LAMPREY-
dc.subject.keywordPlusHAGFISH-
dc.subject.keywordPlusEVOLUTION-
dc.subject.keywordPlusGLYCOSYLATION-
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