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Biophysical characterization and single-chain Fv construction of a neutralizing antibody to measles virus

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/78836

Title: Biophysical characterization and single-chain Fv construction of a neutralizing antibody to measles virus
Authors: Tadokoro, Takashi Browse this author →KAKEN DB
Jahan, Lubna Browse this author
Ito, Yuri Browse this author
Tahara, Maino Browse this author
Chen, Surui Browse this author
Imai, Atsutoshi Browse this author
Sugimura, Natsumi Browse this author
Yoshida, Koki Browse this author
Saito, Mizuki Browse this author
Ose, Toyoyuki Browse this author
Hashiguchi, Takao Browse this author
Takeda, Makoto Browse this author
Fukuhara, Hideo Browse this author
Maenaka, Katsumi Browse this author →KAKEN DB
Keywords: hemagglutinin
Measles virus
Nectin-4
neutralizing antibody
single-chain fragment variables
SLAM
surface plasmon resonance
Issue Date: 9-Jul-2019
Publisher: John Wiley & Sons
Journal Title: FEBS Journal
Publisher DOI: 10.1111/febs.14991
Abstract: The measles virus (MV) is a major cause of childhood morbidity and mortality worldwide. We previously established a mouse monoclonal antibody, 2F4, which shows high neutralizing titers against eight different genotypes of MV. However, the molecular basis for the neutralizing activity of the 2F4 antibody remains incompletely understood. Here, we have evaluated the binding characteristics of a Fab fragment of the 2F4 antibody. Using the MV infectious assay, we demonstrated that 2F4 Fab inhibits viral entry via either of two cellular receptors, SLAM and Nectin4. Surface plasmon resonance (SPR) analysis of recombinant proteins indicated that 2F4 Fab interacts with MV hemagglutinin (MV-H) with a K-D value at the nm level. Furthermore, we designed a single-chain Fv fragment of 2F4 antibody as another potential biopharmaceutical to target measles. The stable 2F4 scFv was successfully prepared by the refolding method and shown to interact with MV-H at the mu m level. Like 2F4 Fab, scFv inhibited receptor binding and viral entry. This indicates that 2F4 mAb uses the receptor-binding site and/or a neighboring region as an epitope with high affinity. These results provide insight into the neutralizing activity and potential therapeutic use of antibody fragments for MV infection.
Rights: This is the peer reviewed version of the following article: T.Tadokoro, et al. / Biophysical characterization and single‐chain Fv construction of a neutralizing antibody to measles virus. FEBS Journal, First published: 09 July 2019, which has been published in final form at https://doi.org/10.1111/febs.14991. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
Type: article (author version)
URI: http://hdl.handle.net/2115/78836
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田所 高志

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