Construction of antibody mimics from a noncatalytic enzyme-detection of polysialic acid

Anne Jokilammi*, Pauli Ollikka, Miikka Korja, Elina Jakobsson, Vuokko Loimaranta, Sauli Haataja, Harri Hirvonen, Jukka Finne

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    11 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)149-160
    Number of pages12
    JournalJournal of Immunological Methods
    Issue number1-2
    Publication statusPublished - Dec 2004


    • Antibody mimics
    • Endosialidase
    • Enzyme engineering
    • Molecular probes
    • Neural plasticity
    • Oncofetal antigen
    • Polysialic acid
    • Substitute antibodies


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