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    Solution structure of the novel dispersin protein of enteroaggregative Escherichia coli

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    Publication date
    2007-12
    Author
    Velarde, J.J.
    Varney, K.M.
    Inman, K.G.
    Farfan, M.
    Dudley, E.
    Weber, D.J.
    Nataro, J.P.
    Fletcher, Jonathan N.
    Keyword
    Dispersin
    Structure
    Escherichia coli
    Enteroaggregative Escherichia coli (EAEC)
    Diarrhoea
    Adherence
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Enteroaggregative Escherichia coli (EAEC), increasingly recognized as an important cause of infant and travelers' diarrhoea, exhibits an aggregative, stacked-brick pattern of adherence to epithelial cells. Adherence is mediated by aggregative adherence fimbriae (AAFs), which are encoded on the pAA virulence plasmid. We recently described a highly prevalent pAA plasmid-borne gene, aap, which encodes a protein (nicknamed dispersin) that is secreted to the bacterial cell surface. Dispersin-null mutants display a unique hyper-aggregating phenotype, accompanied by collapse of AAF pili onto the bacterial cell surface. To study the mechanism of this effect, we solved the structure of dispersin from EAEC strain 042 using solution NMR, revealing a stable beta-sandwich with a conserved net positive surface charge of +3 to +4 among 23 dispersin alleles. Experimental data suggest that dispersin binds non-covalently to lipopolysaccharide on the surface of the bacterium. We also show that the AAF organelles contribute positive charge to the bacterial surface, suggesting that dispersin's role in fimbrial function is to overcome electrostatic attraction between AAF and the bacterial surface
    URI
    http://hdl.handle.net/10454/4777
    Version
    No full-text available in the repository
    Citation
    Velarde, J. J., Varney, K. M., Inman, K. G., Farfan, M., Dudley, E., Fletcher, J., Weber, D. J. and Nataro, J. P. (2007). Solution structure of the novel dispersin protein of enteroaggregative Escherichia coli. Molecular Microbiology, Vol. 66, No. 5, pp. 1123¿1135.
    Link to publisher’s version
    http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2007.05985.x/pdf
    Type
    Article
    Collections
    Life Sciences Publications

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