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<publisher>HAL CCSD</publisher>
<title lang=en>Enhanced humanization and affinity maturation of neutralizing anti-hepatitis B virus preS1 antibody based on antigen–antibody complex structure</title>
<creator>Kim, Jin Hong</creator>
<creator>Gripon, Philippe</creator>
<creator>Bouezzedine, Fidaa</creator>
<creator>Jeong, Mun Sik</creator>
<creator>Chi, Seung-Wook</creator>
<creator>Ryu, Seong-Eon</creator>
<creator>Hong, Hyo Jeong</creator>
<contributor>Kangwon National University</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Daejeon University</contributor>
<contributor>Hanyang University</contributor>
<contributor>This work was supported by Ministry of Health and Welfare grant A050260 and by a 2014 research grant from Kangwon National University (No. 120140400). This work was also financially supported by ANRS (Agence nationale de recherche contre le sida et les hépatites virales).</contributor>
<description>International audience</description>
<source>ISSN: 1873-3468</source>
<source>FEBS Letters</source>
<publisher>Wiley</publisher>
<identifier>hal-01110668</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01110668</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01110668/document</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01110668/file/Enhanced%20humanization_accepted.pdf</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01110668</source>
<source>FEBS Letters, Wiley, 2015, 589 (2), pp.193 - 200. 〈10.1016/j.febslet.2014.11.046〉</source>
<identifier>DOI : 10.1016/j.febslet.2014.11.046</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.febslet.2014.11.046</relation>
<identifier>PUBMED : 25481411</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/25481411</relation>
<language>en</language>
<subject>[SDV.BC] Life Sciences [q-bio]/Cellular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>To improve a previously constructed broadly neutralizing hepatitis B virus (HBV)-specific preS1 humanized antibody (HzKR127), we further humanized it through specificitydetermining residue (SDR) grafting. Moreover, we improved affinity by mutating two residues in heavy-chain complementarity-determining regions (CDR), on the basis of the crystal structure of the antigen–antibody complex. HzKR127-3.2 exhibited 2.5-fold higher affinity and enhanced virus-neutralizing activity compared to the original KR127 antibody and showed less immunogenic potential than HzKR127. Enhanced virus-neutralizing activity was achieved by the increased association rate, providing insights into engineering potent antibody therapeutics for HBV immunoprophylaxis. HzKR127-3.2 may be a good candidate for HBV immunoprophylaxis.</description>
<date>2015-01</date>
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