Catalytic Features and Eradication Ability of Antibody Light-chain UA15-L against Helicobacter pylori*
- Emi Hifumi‡§,
- Fumiko Morihara¶,
- Kenji Hatiuchi§,
- Takuro Okuda§,
- Akira Nishizono∥ and
- Taizo Uda§,**,1
- ‡Research Center for Applied Medical Engineering, Oita University, Dan-noharu 700, Oita-shi, Oita 870-1192, the **Department of Applied Biochemistry, Faculty of Engineering, Oita University, Dan-noharu 700, Oita-shi, Oita 870-1192, ¶Fukuyama Medical Laboratory Co., Fukuyama-city, Hiroshima 720-8510, the ∥Faculty of Medicine, Department of Infectious Diseases, Oita University, Oita 879-5593, and §JST-CREST (Japan Science and Technology Corporation), Kawaguchi City 332-0012, Japan
- ↵1 To whom correspondence should be addressed: Tel./Fax: 81-97-554-7892; E-mail: uda{at}cc.oita-u.ac.jp.
Abstract
We have successfully developed a catalytic antibody capable of degrading the active site of the urease of Helicobacter pylori and eradicating the bacterial infection in a mouse stomach. This monoclonal antibody UA15 was generated using a designed recombinant protein UreB, which contained the crucial region of the H. pylori urease β-subunit active site, for immunization. The light chain of this antibody (UA15-L) by itself showed a proteolytic activity to substantially degrade both UreB and the intact urease. Oral administration of UA15-L also significantly reduced the number of H. pylori in a mouse stomach. This is the first example of a monoclonal catalytic antibody capable of functioning in vivo, and such an antibody may have a therapeutic utility in the future.
- Received July 11, 2007.
- Revision received November 6, 2007.
- The American Society for Biochemistry and Molecular Biology, Inc.
