Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display

Cited 28 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorSang Jick Kim-
dc.contributor.authorMyeong Hee Jang-
dc.contributor.authorJ T Stapleton-
dc.contributor.authorSun Ok Yoon-
dc.contributor.authorK S Kim-
dc.contributor.authorE S Jeon-
dc.contributor.authorHyo Jeong Hong-
dc.date.accessioned2017-04-19T09:00:51Z-
dc.date.available2017-04-19T09:00:51Z-
dc.date.issued2004-
dc.identifier.issn0042-6822-
dc.identifier.uri10.1016/j.virol.2003.10.014ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6424-
dc.description.abstractFour human monoclonal antibodies (MAbs) to hepatitis A virus (HAV) were isolated from a phage-displayed antibody library constructed from the peripheral blood lymphocytes (PBLs) of HAV-immune donors. The four MAbs showed differences in their affinity: two (HA6, HA9) of them were dominant after four rounds of panning, and showed higher affinity than the other two (HA1, HA12). All four MAbs showed HAV-neutralizing activity in radioimmunofocus inhibition assay and their neutralizing activity was positively correlated with their affinities. Analysis of their epitope specificity by cross-competition binding assays suggested that HA6 and HA9 recognize extensively overlapping epitopes, which overlap with those of HA1 and HA12, although HA1 and HA12 recognize distinct epitopes. In addition, competition assays with known neutralizing murine MAbs suggested that the epitopes of four human MAbs extensively overlap with those of B5B3 and K34C8 which are distinct but reside within the single, immunodominant neutralization site on the HAV capsid. The human MAbs (HA6 and HA9) with highest affinity may be useful in the immunoprophylaxis of HAV infection.-
dc.publisherElsevier-
dc.titleNeutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display-
dc.title.alternativeNeutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display-
dc.typeArticle-
dc.citation.titleVirology-
dc.citation.number2-
dc.citation.endPage607-
dc.citation.startPage598-
dc.citation.volume318-
dc.contributor.affiliatedAuthorSang Jick Kim-
dc.contributor.affiliatedAuthorMyeong Hee Jang-
dc.contributor.affiliatedAuthorSun Ok Yoon-
dc.contributor.affiliatedAuthorHyo Jeong Hong-
dc.contributor.alternativeName김상직-
dc.contributor.alternativeName장명희-
dc.contributor.alternativeNameStapleton-
dc.contributor.alternativeName윤선옥-
dc.contributor.alternativeName김근수-
dc.contributor.alternativeName전은석-
dc.contributor.alternativeName홍효정-
dc.identifier.bibliographicCitationVirology, vol. 318, no. 2, pp. 598-607-
dc.identifier.doi10.1016/j.virol.2003.10.014-
dc.subject.keywordFab-
dc.subject.keywordHAV-
dc.subject.keywordHuman antibody library-
dc.subject.keywordNeutralization epitope-
dc.subject.keywordPhage display-
dc.subject.localFab-
dc.subject.localHAV-
dc.subject.localHuman antibody library-
dc.subject.localNeutralization epitope-
dc.subject.localPhage display-
dc.subject.localphage display-
dc.description.journalClassY-
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.