ArticleThe Journal of biological chemistry2011
Mhp107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 55 citations in OpenAlex.
- Rethinking Mycoplasma hyopneumoniae adhesion: a glycocalyx-mediated infectious niche model in porcine respiratory infection.Veterinary research · 2026Review
- Mesomycoplasma hyopneumoniae lipoprotein Mhp390 serves as a plasminogen receptor mediating extracellular matrix degradation and respiratory epithelial cells injury.Veterinary research · 2025Article
- Research Progress on Immune Evasion ofMicroorganisms · 2024Review
- A genetic and virulence characterization of Brazilian strains ofFrontiers in microbiology · 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
- Review
- Incomplete autophagy promotes the replication of Mycoplasma hyopneumoniae.Journal of microbiology (Seoul, Korea) · 2021Article
- Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.Scientific reports · 2021Article
- Construction ofFrontiers in microbiology · 2021Article
- Pathogenicity & virulence ofVirulence · 2020Review
- 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
- Mycoplasma hyopneumoniae resides intracellularly within porcine epithelial cells.Scientific reports · 2018Article
- Fructose-1,6-bisphosphate aldolase encoded by a core gene of Mycoplasma hyopneumoniae contributes to host cell adhesion.Veterinary research · 2018Article
- Extracellular DNA release from the genome-reduced pathogen Mycoplasma hyopneumoniae is essential for biofilm formation on abiotic surfaces.Scientific reports · 2018Article
- Elongation Factor Thermo Unstable (EF-Tu) Moonlights as an Adhesin on the Surface ofFrontiers in microbiology · 2018Article
- Extracellular Actin Is a Receptor forFrontiers in cellular and infection microbiology · 2018Article
- N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen.Scientific reports · 2017Article
- Elongation factor Tu is a multifunctional and processed moonlighting protein.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma hyopneumoniae is the causative pathogen of porcine enzootic pneumonia, an economically significant disease that disrupts the mucociliary escalator in the swine respiratory tract. Expression of Mhp107, a P97 paralog encoded by the gene mhp107, was confirmed using ESI-MS/MS. To investigate the function of Mhp107, three recombinant proteins, F1(Mhp107), F2(Mhp107), and F3(Mhp107), spanning the N-terminal, central, and C-terminal regions of Mhp107 were constructed. Colonization of swine by M. hyopneumoniae requires adherence of the bacterium to ciliated cells of the respiratory tract. Recent studies have identified a number of M. hyopneumoniae adhesins that bind heparin, fibronectin, and plasminogen. F1(Mhp107) was found to bind porcine heparin (K(D) ∼90 nM) in a dose-dependent and saturable manner, whereas F3(Mhp107) bound fibronectin (K(D) ∼180 nM) at physiologically relevant concentrations. F1(Mhp107) also bound porcine plasminogen (K(D) = 24 nM) in a dose-dependent and physiologically relevant manner. Microspheres coated with F3(Mhp107) mediate adherence to porcine kidney epithelial-like (PK15) cells, and all three recombinant proteins (F1(Mhp107)-F3(Mhp107)) bound swine respiratory cilia. Together, these findings indicate that Mhp107 is a member of the multifunctional M. hyopneumoniae adhesin family of surface proteins and contributes to both adherence to the host and pathogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.