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Enhanced humanization and affinity maturation of neutralizing anti-hepatitis B virus preS1 antibody based on antigen–antibody complex structure

Abstract : 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.
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https://hal-univ-rennes1.archives-ouvertes.fr/hal-01110668
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Submitted on : Wednesday, January 28, 2015 - 4:17:58 PM
Last modification on : Wednesday, March 4, 2020 - 9:53:24 AM
Long-term archiving on: : Wednesday, April 29, 2015 - 11:15:28 AM

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Jin Hong Kim, Philippe Gripon, Fidaa Bouezzedine, Mun Sik Jeong, Seung-Wook Chi, et al.. Enhanced humanization and affinity maturation of neutralizing anti-hepatitis B virus preS1 antibody based on antigen–antibody complex structure. FEBS Letters, Wiley, 2015, 589 (2), pp.193 - 200. ⟨10.1016/j.febslet.2014.11.046⟩. ⟨hal-01110668⟩

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