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

Catalytic antibodies have exhibited interesting functions against some infections 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 Sea mice. 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.— Hifumi, E., Arakawa, M., Matsumoto, S., Yamamoto, T., Katayama, Y., Uda, T. Biochemical features and antiviral activity of a monomeric catalytic antibody light‐chain 23D4 against influenzaAvirus. FASEB J. 29, 2347‐2358 (2015). www.fasebj.org