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. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Hifumi, E., Morihara, F., Hatiuchi, K., Okuda, T., Nishizono, A., & Uda, T. (2008). Catalytic features and eradication ability of antibody light-chain UA15-L against Helicobacter pylori. Journal of Biological Chemistry, 283(2), 899–907. https://doi.org/10.1074/jbc.M705674200
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