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Occludin (OCLN) is a tetraspan membrane component of epithelial tight junctions and a known receptor for hepatitis C virus (HCV). Previously, we established functional monoclonal antibodies (mAbs) that bind to each extracellular loop of OCLN and showed their ability to prevent in vitro and in vivo HCV infection. In this study, we converted these mAbs to corresponding monovalent antigen-binding fragments (Fabs) and single-chain variable fragment (scFv) antibodies. These Fab fragments and scFv antibodies demonstrate similar binding specificity and affinity to parental anti-OCLN mAbs. Moreover, Fab fragments and scFv antibodies inhibit in vitro HCV infection. The small functional monovalent OCLN-binding probes reported in our study have high potential as drug candidates and tools for biological and pharmaceutical studies of OCLN. © 2020 Federation of European Biochemical Societies.

Citation

Yoshimi Shimizu, Takehiro Shinoda, Yoshitaka Shirasago, Masuo Kondoh, Naoko Shinya, Kentaro Hanada, Kiyohito Yagi, Tetsuro Suzuki, Takaji Wakita, Tomomi Kimura-Someya, Mikako Shirouzu, Masayoshi Fukasawa. Occludin-binding single-chain variable fragment and antigen-binding fragment antibodies prevent hepatitis C virus infection. FEBS letters. 2021 Jan;595(2):220-229

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PMID: 33113151

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