Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of<i>Mycoplasma hyopneumoniae</i>

Wilton, Jody L.; Jenkins, Cheryl; Cordwell, Stuart J.; Falconer, Linda; Minion, F. Chris; Oneal, David; Djordjevic, Michael A.; Connolly, Angela; Barchia, I.; Walker, Mark J.; Djordjevic, Steven P.

doi:10.1111/j.1365-2958.2008.06546.x

Cited by 64 publications

(154 citation statements)

References 51 publications

(106 reference statements)

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“…Cilia Binding Assay-Cilia binding was performed with recombinant P116 proteins, as described by Wilton et al (13) based on the assay developed by Zhang et al (29). Cilium adhesin protein P97 (F2 P97 ) (12) was used as the positive control, and the non cilia-binding N-terminal 64-kDa fragment of P120 (a M. hyopneumoniae protein encoded by mhp107), another P97 paralog, was used as a negative control.…”

Section: Methodsmentioning

confidence: 99%

“…An in vitro assay of M. hyopneumoniae binding to cilia was developed by Zhang et al (29) to investigate potential receptors of the bacterium. A similar assay has been used to determine the cilial-binding region of P97 (39) and demonstrate that P216 is a cilium adhesin (13). As this assay has previously been successfully employed to identify cilium adhesins, it was utilized to investigate the ability of P116 fragments to bind purified swine respiratory cilia.…”

Section: C-terminal Lysine Of P116 Facilitates Binding To Porcinementioning

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%

“…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).…”

mentioning

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%

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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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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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Section: Methodsmentioning

confidence: 99%

Section: C-terminal Lysine Of P116 Facilitates Binding To Porcinementioning

confidence: 99%

Section: C-terminal Lysine Of P116 Facilitates Binding To Porcinementioning

confidence: 99%