Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus

Emi Hifumi, Mitsue Arakawa, Shingo Matsumoto, Tatsuhiro Yamamoto, Yoshiki Katayama, Taizo Uda

    Research output: Contribution to journalArticlepeer-review

    7 Citations (Scopus)

    Abstract

    Catalytic antibodies have exhibited interesting functions against some infectious viruses such as HIV, rabies virus, and influenza virus in vitro as well as in vivo. In some cases, a catalytic antibody light chain takes on several structures from the standpoint of molecular size (monomer, dimer, etc.) and/or isoelectronic point. In this study, we prepared a monomeric 23D4 light chain by mutating the C-terminal Cys to Ala of the wild-type. The mutated 23D4 molecule took a simple monomeric form, which could hydrolyze synthetic 4-methyl-coumaryl-7-amide substrates and a plasmid DNA. Because the monomeric 23D4 light chain suppressed the infection of influenza virus A/Hiroshima/37/2001 in an in vitro assay, the corresponding experiments were conducted in vivo, after the virus strain (which was taken from a human patient) was successfully adapted into BALB/cN Seamice. In the experiments, a mixture of the monomeric 23D4 and the virus was nasally administered 1) with preincubation and 2) without preincubation. As a result, the monomeric 23D4 clearly exhibited the ability to suppress the influenza virus infection in both cases, indicating a potential drug for preventing infection of the influenza A virus.

    Original languageEnglish
    Pages (from-to)2347-2358
    Number of pages12
    JournalFASEB Journal
    Volume29
    Issue number6
    DOIs
    Publication statusPublished - Jun 1 2015

    All Science Journal Classification (ASJC) codes

    • Biotechnology
    • Biochemistry
    • Molecular Biology
    • Genetics

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