tetano
Editor, Senior Moderator
FASEB J. 2015 Feb 20. pii: fj.14-264275. [Epub ahead of print]
[h=1]Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus.[/h] Hifumi E[SUP]1[/SUP], Arakawa M[SUP]2[/SUP], Matsumoto S[SUP]2[/SUP], Yamamoto T[SUP]2[/SUP], Katayama Y[SUP]2[/SUP], Uda T[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 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., and Uda, T. Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus.
? FASEB.
[h=4]KEYWORDS:[/h] AFM image; catalytic antibody; hydrolysis; infection; suppression
PMID: 25713031 [PubMed - as supplied by publisher]
[h=1]Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus.[/h] Hifumi E[SUP]1[/SUP], Arakawa M[SUP]2[/SUP], Matsumoto S[SUP]2[/SUP], Yamamoto T[SUP]2[/SUP], Katayama Y[SUP]2[/SUP], Uda T[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 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., and Uda, T. Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus.
? FASEB.
[h=4]KEYWORDS:[/h] AFM image; catalytic antibody; hydrolysis; infection; suppression
PMID: 25713031 [PubMed - as supplied by publisher]