Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism

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dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorC Y Maeng-
dc.contributor.authorSeung Jun Kim-
dc.contributor.authorM S Oh-
dc.contributor.authorC J Ryu-
dc.contributor.authorSang Jick Kim-
dc.contributor.authorKyou Hoon Han-
dc.contributor.authorHyo Jeong Hong-
dc.contributor.authorSeong Eon Ryu-
dc.date.accessioned2017-04-19T09:07:45Z-
dc.date.available2017-04-19T09:07:45Z-
dc.date.issued2007-
dc.identifier.issn0027-8424-
dc.identifier.uri10.1073/pnas.0701279104ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8006-
dc.description.abstractThe humanized monoclonal antibody HzKR127 recognizes the preS1 domain of the human hepatitis B virus surface proteins with a broadly neutralizing activity in vivo. We present the crystal structures of HzKR127 Fab and its complex with a major epitope peptide. In the complex structure, the bound peptide forms a type IV β-turn followed by 310 helical turn, the looped-out conformation of which provides a structural basis for broad neutralization. Upon peptide binding, the antibody undergoes a dramatic complementarity determining region H3 lid opening. To understand the structural implication of the virus neutralization, we carried out comprehensive alanine-scanning mutagenesis of all complementarity determining region residues in HzKR127 Fab. The functional mapping of the antigen-combining site demonstrates the specific roles of major binding determinants in antigen binding, contributing to the rational design for maximal humanization and affinity maturation of the antibody.-
dc.publisherNatl Acad Sciences-
dc.titleBroadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism-
dc.title.alternativeBroadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism-
dc.typeArticle-
dc.citation.titleProceedings of National Academy of Sciences of United States of America-
dc.citation.number22-
dc.citation.endPage9235-
dc.citation.startPage9230-
dc.citation.volume104-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorSeung Jun Kim-
dc.contributor.affiliatedAuthorSang Jick Kim-
dc.contributor.affiliatedAuthorKyou Hoon Han-
dc.contributor.affiliatedAuthorHyo Jeong Hong-
dc.contributor.affiliatedAuthorSeong Eon Ryu-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName맹철영-
dc.contributor.alternativeName김승준-
dc.contributor.alternativeName오미숙-
dc.contributor.alternativeName류춘제-
dc.contributor.alternativeName김상직-
dc.contributor.alternativeName한규훈-
dc.contributor.alternativeName홍효정-
dc.contributor.alternativeName류성언-
dc.identifier.bibliographicCitationProceedings of National Academy of Sciences of United States of America, vol. 104, no. 22, pp. 9230-9235-
dc.identifier.doi10.1073/pnas.0701279104-
dc.subject.keywordAlanine-scanning mutagenesis-
dc.subject.keywordCrystal structure-
dc.subject.keywordHumanized antibody-
dc.subject.keywordVirus neutralization-
dc.subject.localAlanine-scanning mutagenesis-
dc.subject.localcrystal structure-
dc.subject.localCrystal structure-
dc.subject.localHumanized antibody-
dc.subject.localhumanized antibodies-
dc.subject.localhumanized antibody-
dc.subject.localVirus neutralization-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
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