TY - JOUR
T1 - Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus
AU - Hifumi, Emi
AU - Arakawa, Mitsue
AU - Matsumoto, Shingo
AU - Yamamoto, Tatsuhiro
AU - Katayama, Yoshiki
AU - Uda, Taizo
PY - 2015/6/1
Y1 - 2015/6/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84933575479&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84933575479&partnerID=8YFLogxK
U2 - 10.1096/fj.14-264275
DO - 10.1096/fj.14-264275
M3 - Article
C2 - 25713031
AN - SCOPUS:84933575479
VL - 29
SP - 2347
EP - 2358
JO - FASEB Journal
JF - FASEB Journal
SN - 0892-6638
IS - 6
ER -