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Endosialidases: Versatile Tools for the Study of Polysialic Acid

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SialoGlyco Chemistry and Biology II

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 367))

Abstract

Polysialic acid is an α2,8-linked N-acetylneuraminic acid polymer found on the surface of both bacterial and eukaryotic cells. Endosialidases are bacteriophage-borne glycosyl hydrolases that specifically cleave polysialic acid. The crystal structure of an endosialidase reveals a trimeric mushroom-shaped molecule which, in addition to the active site, harbors two additional polysialic acid binding sites. Folding of the protein crucially depends on an intramolecular C-terminal chaperone domain that is proteolytically released in an intramolecular reaction. Based on structural data and previous considerations, an updated catalytic mechanism is discussed. Endosialidases degrade polysialic acid in a processive mode of action, and a model for its mechanism is suggested. The review summarizes the structural and biochemical elucidations of the last decade and the importance of endosialidases in biochemical and medical applications. Active endosialidases are important tools in studies on the biological roles of polysialic acid, such as the pathogenesis of septicemia and meningitis by polysialic acid-encapsulated bacteria, or its role as a modulator of the adhesion and interactions of neural and other cells. Endosialidase mutants that have lost their polysialic acid cleaving activity while retaining their polysialic acid binding capability have been fused to green fluorescent protein to provide an efficient tool for the specific detection of polysialic acid.

This work has been supported by grants from the Academy of Finland and the Deutsche Forschungsgemeinschaft.

Elina Jakobsson and David Schwarzer have contributed equally to this review.

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Abbreviations

CTD:

C-terminal chaperone domain

endoN:

Endosialidase (endo-N-acylneuraminidase)

NCAM:

Neural cell adhesion molecule

Neu5Ac:

N-Acetylneuraminic acid

Neu5Gc:

N-Glycolylneuraminic acid

Sia:

Sialic acid

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Authors and Affiliations

  1. Department of Medical Biochemistry and Genetics, University of Turku, Kiinamyllynkatu 10, 20520, Turku, Finland

    Elina Jakobsson & Anne Jokilammi

  2. Institute for Cellular Chemistry (OE 4330), Hannover Medical School, Carl-Neuberg-Street 1, 30625, Hannover, Germany

    David Schwarzer

  3. Department of Biosciences, Division of Biochemistry and Biotechnology, University of Helsinki, 56, 00014, Helsinki, Finland

    Jukka Finne

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  1. Institute for Cellular Chemistry, Hannover, Germany

    Rita Gerardy-Schahn

  2. Lille University of Science and Technology, Villeneuve d'Ascq Cedex, France

    Philippe Delannoy

  3. Institute for Glycomics, Griffith University, Southport, Queensland, Australia

    Mark von Itzstein

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Jakobsson, E., Schwarzer, D., Jokilammi, A., Finne, J. (2012). Endosialidases: Versatile Tools for the Study of Polysialic Acid. In: Gerardy-Schahn, R., Delannoy, P., von Itzstein, M. (eds) SialoGlyco Chemistry and Biology II. Topics in Current Chemistry, vol 367. Springer, Cham. https://doi.org/10.1007/128_2012_349

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