Production and characterization of monoclonal antibody to botulinum neurotoxin type B light chain by phage display

Myung Shin Lee, Ji Chul Lee, Cha Yong Choi, Junho Chung

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)

Abstract

A monoclonal antibody to the light chain of botulinum neurotoxin type B (BoNT/B) was generated and its protective activity was evaluated in vivo. A chimeric rabbit/human Fab library was generated using bone marrow and spleen cDNAs of rabbits immunized with the BoNT/B light chain, and three monoclonal antibodies specific to the catalytic domain of BoNT/B were isolated. One of these clones, BCXRH1, was specific to a conformation-dependent epitope, and partially neutralized the BoNT/B complex in vivo.

Original languageEnglish
Pages (from-to)18-24
Number of pages7
JournalHybridoma
Volume27
Issue number1
DOIs
StatePublished - 1 Feb 2008

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Bacteriophages
Monoclonal Antibodies
Light
Rabbits
Libraries
Epitopes
Catalytic Domain
Spleen
Complementary DNA
Clone Cells
Bone Marrow
rimabotulinumtoxinB

Cite this

Lee, Myung Shin ; Lee, Ji Chul ; Choi, Cha Yong ; Chung, Junho. / Production and characterization of monoclonal antibody to botulinum neurotoxin type B light chain by phage display. In: Hybridoma. 2008 ; Vol. 27, No. 1. pp. 18-24.
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Production and characterization of monoclonal antibody to botulinum neurotoxin type B light chain by phage display. / Lee, Myung Shin; Lee, Ji Chul; Choi, Cha Yong; Chung, Junho.

In: Hybridoma, Vol. 27, No. 1, 01.02.2008, p. 18-24.

Research output: Contribution to journalArticleResearchpeer-review

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AB - A monoclonal antibody to the light chain of botulinum neurotoxin type B (BoNT/B) was generated and its protective activity was evaluated in vivo. A chimeric rabbit/human Fab library was generated using bone marrow and spleen cDNAs of rabbits immunized with the BoNT/B light chain, and three monoclonal antibodies specific to the catalytic domain of BoNT/B were isolated. One of these clones, BCXRH1, was specific to a conformation-dependent epitope, and partially neutralized the BoNT/B complex in vivo.

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