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 journalArticle

3 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

Fingerprint

Catalytic Antibodies
Influenza A virus
Viruses
Antiviral Agents
Orthomyxoviridae
Light
Rabies virus
Virus Diseases
Infection
Molecular Structure
Plasmids
HIV
DNA
Pharmaceutical Preparations
Dimers
Assays
In Vitro Techniques
Monomers
Experiments

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus. / Hifumi, Emi; Arakawa, Mitsue; Matsumoto, Shingo; Yamamoto, Tatsuhiro; Katayama, Yoshiki; Uda, Taizo.

In: FASEB Journal, Vol. 29, No. 6, 01.06.2015, p. 2347-2358.

Research output: Contribution to journalArticle

Hifumi, Emi ; Arakawa, Mitsue ; Matsumoto, Shingo ; Yamamoto, Tatsuhiro ; Katayama, Yoshiki ; Uda, Taizo. / Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus. In: FASEB Journal. 2015 ; Vol. 29, No. 6. pp. 2347-2358.
@article{9c3a626822074cb88b194e706d00ba94,
title = "Biochemical features and antiviral activity of a monomeric catalytic antibody light-chain 23D4 against influenza A virus",
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.",
author = "Emi Hifumi and Mitsue Arakawa and Shingo Matsumoto and Tatsuhiro Yamamoto and Yoshiki Katayama and Taizo Uda",
year = "2015",
month = "6",
day = "1",
doi = "10.1096/fj.14-264275",
language = "English",
volume = "29",
pages = "2347--2358",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "6",

}

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

VL - 29

SP - 2347

EP - 2358

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 6

ER -