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    P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells.

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    Authors
    Burnett, Tracey A
    Dinkla, Katrin
    Rohde, Manfred
    Chhatwal, Gursharan S
    Uphoff, Cord
    Srivastava, Mukesh
    Cordwell, Stuart J
    Geary, Steven
    Liao, Xiaofen
    Minion, F Chris
    Walker, Mark J
    Djordjevic, Steven P
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    Issue Date
    2006-05-01
    
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    Abstract
    Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparin-binding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages. Following purification of four recombinant proteins spanning P159 (F1P159, F2P159, F3P159 and F4P159), only F3P159 and F4P159 bound heparin in a dose-dependent manner (K(d) values 142.37 +/- 22.01 nM; 75.37 +/- 7.34 nM respectively). Scanning electron microscopic studies showed M. hyopneumoniae bound intimately to porcine kidney epithelial-like cells (PK15 cells) but these processes were inhibited by excess heparin and F4P159. Similarly, latex beads coated with F2P159 and F4P159 adhered to and entered PK15 cells, but heparin, F2P159 and F4P159 was inhibitory. These findings indicate that P159 is a post-translationally cleaved, glycosaminoglycan-binding adhesin of M. hyopneumoniae.
    Citation
    Mol. Microbiol. 2006, 60(3):669-86
    URI
    http://hdl.handle.net/10033/14550
    DOI
    10.1111/j.1365-2958.2006.05139.x
    PubMed ID
    16629669
    Type
    Article
    Language
    en
    ISSN
    0950-382X
    ae974a485f413a2113503eed53cd6c53
    10.1111/j.1365-2958.2006.05139.x
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