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

Burnett, Tracey A; Dinkla, Katrin; Rohde, Manfred; Chhatwal, Gursharan S.; Uphoff, Cord C.; Srivastava, Mukesh; Cordwell, Stuart J.; Geary, Steven J.; Liao, X.; Minion, F. Chris; Walker, Mark J.; Djordjevic, Steven P.

doi:10.1111/j.1365-2958.2006.05139.x

Cited by 89 publications

(188 citation statements)

References 45 publications

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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%

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

2013

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The obligate pathogenic mycoplasma species Mycoplasma pneumoniae uses a limited but effective repertoire of virulence factors to infect and colonize the human respiratory tract. Besides the development of a unique adhesion complex and the expression of tissue-damaging factors, surface-located glycolytic enzymes and their capacity to bind to components of the human extracellular matrix (ECM) support pathogen-host interactions. Here, we demonstrated that the glycolytic enzymes enolase (Mpn606) and pyruvate dehydrogenase subunit B (Mpn392; PDHB) of M. pneumoniae show concentration-dependent binding to human plasminogen. Monospecific polyclonal antisera against both recombinant proteins reduced the binding to plasminogen significantly. The surface location of PDHB but not of enolase was demonstrated using Triton X fractionation of M. pneumoniae total protein content, membrane fractionation, colony blotting, mild proteolysis of mycoplasma cells, and immunofluorescence tests. To characterize the binding site of plasminogen in surface-displaced PDHB, the mycoplasmal protein was separated into four recombinant proteins followed by investigation of the binding behaviour of peptides that overlap the protein part interacting with plasminogen. Spot analysis resulted in a novel region of 12 amino acids (FPAMFQIFTHAA, position 91 to 102 of PDHB), which is responsible exclusively for binding of human plasminogen and also interacts in a dose-dependent manner with this host protein. The data indicate that the plasminogen-binding enzymes enolase and especially the surface-associated PDHB may contribute to the pathogenesis of M. pneumoniae infections.

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Section: Discussionmentioning

confidence: 99%

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

2013

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“…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%

“…Prevention of the interactions between the host and M. hyopneumoniae prior to colonization would result in a more efficacious vaccine (8,10). Although research into this area is focusing on proteins specific to these interactions (11)(12)(13)(14)(15), M. hyopneumoniae pathogenicity and adherence mechanisms remain poorly characterized (7,12).…”

mentioning

confidence: 99%

“…Despite the role of P97 in adherence, additional surface proteins also contribute to this process including P159 and P216 (5,(11)(12)(13)(14). A 126 kDa preprotein is proteolytically processed to form P97 (5,16); the gene encoding P97 (mhp183) is located in a two gene operon with that encoding P102 (mhp182) (5).…”

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A Processed Multidomain Mycoplasma hyopneumoniae Adhesin Binds Fibronectin, Plasminogen, and Swine Respiratory Cilia

Seymour¹,

Deutscher

Jenkins

et al. 2010

Journal of Biological Chemistry

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134

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Porcine enzootic pneumonia is a chronic respiratory disease that affects swine. The etiological agent of the disease, Mycoplasma hyopneumoniae, is a bacterium that adheres to cilia of the swine respiratory tract, resulting in loss of cilia and epithelial cell damage. A M. hyopneumoniae protein P116, encoded by mhp108, was investigated as a potential adhesin. Examination of P116 expression using proteomic analyses observed P116 as a full-length protein and also as fragments, ranging from 17 to 70 kDa in size. A variety of pathogenic bacterial species have been shown to bind the extracellular matrix component fibronectin as an adherence mechanism. M. hyopneumoniae cells were found to bind fibronectin in a dose-dependent and saturable manner. Surface plasmon resonance was used to show that a recombinant C-terminal domain of P116 bound fibronectin at physiologically relevant concentrations (K D 24 ؎ 6 nM). Plasmin(ogen)-binding proteins are also expressed by many bacterial pathogens, facilitating extracellular matrix degradation. M. hyopneumoniae cells were found to also bind plasminogen in a dose-dependent and saturable manner; the C-terminal domain of P116 binds to plasminogen (K D 44 ؎ 5 nM). Plasminogen binding was abolished when the C-terminal lysine of P116 was deleted, implicating this residue as part of the plasminogen binding site. P116 fragments adhere to the PK15 porcine kidney epithelial-like cell line and swine respiratory cilia. Collectively these data suggest that P116 is an important adhesin and virulence factor of M. hyopneumoniae.

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Mycoplasma

Browning

Marenda

Markham

et al. 2010

Pathogenesis of Bacterial Infections in Animals

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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

Cited by 89 publications

References 45 publications

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

A Processed Multidomain Mycoplasma hyopneumoniae Adhesin Binds Fibronectin, Plasminogen, and Swine Respiratory Cilia

Mycoplasma

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