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Science 21 June 2002:
Vol. 296. no. 5576, pp. 2247 - 2249
DOI: 10.1126/science.296.5576.2247
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CATALYTIC ANTIBODIES:
Antibody Design by Man and Nature

Paul Wentworth, Jr.

Catalytic antibodies have emerged as being without peer as rationally designed biocatalysts. They have been shown to catalyze an ever-increasing array of chemical reactions with both high substrate specificity and selectivity. Probing the immune repertoire, via an expanding number of techniques, has lead to the production of proteins that can catalyze chemistry that is both difficult to perform using existing chemical methods and that is not catalyzed by endogenous enzymes. Remarkably, recent evidence has pointed to a hitherto unknown catalytic function of all antibodies that seems to be intrinsic to their immunoglobulin structure, the conversion of 1O2* into H2O2. This new catalytic potential of antibodies points to a new 'chemical arm' of the immune system and reveals that the evolution of catalytic antibodies significantly predates their rational design.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Evidence for Antibody-Catalyzed Ozone Formation in Bacterial Killing and Inflammation.
P. Wentworth Jr., J. E. McDunn, A. D. Wentworth, C. Takeuchi, J. Nieva, T. Jones, C. Bautista, J. M. Ruedi, A. Gutierrez, K. D. Janda, et al. (2002)
Science 298, 2195-2199
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Science. ISSN 0036-8075 (print), 1095-9203 (online)