| Literature DB >> 15627620 |
Anne Jokilammi1, Pauli Ollikka, Miikka Korja, Elina Jakobsson, Vuokko Loimaranta, Sauli Haataja, Harri Hirvonen, Jukka Finne.
Abstract
We have used a conceptually novel way to construct antibody mimics based on the binding of a noncatalytic enzyme to its substrate. Bacteriophage-derived endosialidase cleaves polysialic acid (polySia), an important oncofetal and bacterial antigen, which is poorly immunogenic. We fused to green fluorescent protein (GFP) a catalytically inactive endosialidase known to bind but not degrade polysialic acid. The fusion protein is a convenient single-step reagent in fluorescence microscopy, binding assays and immunoblots. It efficiently and specifically detected polysialic acid in developing brain, neuroblastoma cells and bacteria causing meningitis. Enzyme-substrate interactions represent an unexploited source of molecular recognition events. Some of these could be used in designing well-defined substitute antibodies for the study of target molecules which are difficult to purify, available in low quantities, are unstable or have poor immunogenity.Entities:
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Year: 2004 PMID： 15627620 DOI： 10.1016/j.jim.2004.10.006
Source DB: PubMed Journal: J Immunol Methods ISSN： 0022-1759 Impact factor: 2.303