ArticleThe Journal of biological chemistry2010
A processed multidomain mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Rethinking Mycoplasma hyopneumoniae adhesion: a glycocalyx-mediated infectious niche model in porcine respiratory infection.Veterinary research · 2026Review
- Research Progress on Immune Evasion ofMicroorganisms · 2024Review
- Chimeric proteins of Mycoplasma hyopneumoniae as vaccine and preclinical model for immunological evaluation.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Hijacking of Host Plasminogen byMicrobiology spectrum · 2023Article
- Differential domains and endoproteolytic processing in dominant surface proteins of unknown function fromHeliyon · 2023Article
- Development of a Multi-Epitope Vaccine forInternational journal of molecular sciences · 2022Article
- Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae.BMC microbiology · 2022Article
- NADH oxidase of Mycoplasma hyopneumoniae functions as a potential mediator of virulence.BMC veterinary research · 2022Article
- Review
- Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.Scientific reports · 2021Article
- Review
- Construction ofFrontiers in microbiology · 2021Article
- Pathogenicity & virulence ofVirulence · 2020Review
- Article
- Mycoplasma hyopneumoniae Inhibits Porcine Beta-Defensin 2 Production by Blocking the Unfolded Protein Response To Facilitate Epithelial Adhesion and Infection.Infection and immunity · 2020Article
- Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules.Scientific reports · 2020Article
- Genomic Variability and Post-translational Protein Processing Enhance the Immune Evasion ofFrontiers in immunology · 2020Review
- Combined Transcriptome Sequencing ofFrontiers in microbiology · 2020Article
- Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y.Scientific reports · 2019Article
- Terminomics Methodologies and the Completeness of Reductive Dimethylation: A Meta-Analysis of Publicly Available Datasets.Proteomes · 2019Article
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11 authors.
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Abstract
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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