Neutralization of<i>Burkholderia pseudomallei</i>Protease by Fabs Generated through Phage Display
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- NATHAN Sheila
- School of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia
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- RADER Christoph
- Department of Molecular Biology, Scripps Research Institute
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- BARBAS Carlos F.
- Department of Molecular Biology, Scripps Research Institute
書誌事項
- タイトル別名
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- Neutralization of Burkholderia pseudomallei Protease by Fabs Generated through Phage Display
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説明
The isolation of therapeutic and functional protease inhibitors in vitro via combinatorial chemistry and phage display technology has been described previously. Here we report the construction of a combinatorial mouse-human chimeric antibody fragment (Fab) antibody library targeted against the protease of the tropical pathogen, Burkholderia pseudomallei. The resulting library was biopanned against the protease, and selected clones were analyzed for their ability to function as protease inhibitors. Three families of Fabs were identified by restriction fingerprinting, all of which demonstrated high specificity towards the protease of B. pseudomallei. Purified Fabs also demonstrated the capacity to inhibit B. pseudomallei protease activity in vitro, and this inhibitory property was exclusive to the pathogenic protease. Thus these recombinant antibodies are candidates for immunotherapy and tools to aid in further elucidation of the mechanism of action of the B. pseudomallei protease.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 69 (12), 2302-2311, 2005
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681451727488
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- NII論文ID
- 130000030444
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 7755876
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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