2006
DOI: 10.1111/j.1365-2958.2006.05139.x
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P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

Abstract: SummaryMycoplasma 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 heparinbinding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins repre… Show more

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Cited by 90 publications
(188 citation statements)
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“…Within these multi-factorial processes, proteins on the mycoplasma surface play a central role in the host-pathogen interaction. In this context, binding to host ECM components is mediated by different mycoplasma molecules, such as adhesins and proteins of unknown function in Mycoplasma gallisepticum (Jenkins et al, 2007;May et al, 2006) and Mycoplasma hyopneumoniae (Burnett et al, 2006;Seymour et al, 2010), as well as proteins involved in protein synthesis and housekeeping enzymes in other species (Chen et al, 2011;Dallo et al, 2002;Dumke et al, 2011;Hoelzle et al, 2007). In addition to the described association of PDHB and elongation factor Tu of M. pneumoniae with human fibronectin (Dallo et al, 2002) and of GAPDH with human fibrinogen (Dumke et al, 2011), here we show that PDHB and enolase are binding partners of human plasminogen.…”
Section: Discussionmentioning
confidence: 99%
“…Within these multi-factorial processes, proteins on the mycoplasma surface play a central role in the host-pathogen interaction. In this context, binding to host ECM components is mediated by different mycoplasma molecules, such as adhesins and proteins of unknown function in Mycoplasma gallisepticum (Jenkins et al, 2007;May et al, 2006) and Mycoplasma hyopneumoniae (Burnett et al, 2006;Seymour et al, 2010), as well as proteins involved in protein synthesis and housekeeping enzymes in other species (Chen et al, 2011;Dallo et al, 2002;Dumke et al, 2011;Hoelzle et al, 2007). In addition to the described association of PDHB and elongation factor Tu of M. pneumoniae with human fibronectin (Dallo et al, 2002) and of GAPDH with human fibrinogen (Dumke et al, 2011), here we show that PDHB and enolase are binding partners of human plasminogen.…”
Section: Discussionmentioning
confidence: 99%
“…The cytosolic L7/L12 protein remained intact (Fig. 1F) (14) and P116 fragments were not recognized by pre-immune sera (supplemental Fig. S6).…”
Section: Proteomic and Molecular Analyses Of P116-p116mentioning
confidence: 99%
“…Given that PK15 cells have been used as a model for M. hyopneumoniae binding to eukaryotic cells (13,14), we explored the interaction of P116 fragments with PK15 cells. Adherence to PK15 cells was determined using fluorescent microspheres coated with purified P116 fragments.…”
Section: C-terminal Lysine Of P116 Facilitates Binding To Porcinementioning
confidence: 99%
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