ArticleInfection and immunity2006
Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 65 citations in OpenAlex.
- Rethinking Mycoplasma hyopneumoniae adhesion: a glycocalyx-mediated infectious niche model in porcine respiratory infection.Veterinary research · 2026Review
- Research Progress on Immune Evasion ofMicroorganisms · 2024Review
- Marine-Derived Sulfated Glycans Inhibit the Interaction of Heparin with Adhesion Proteins ofMarine drugs · 2024Article
- Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection.Molecular microbiology · 2022Article
- Perspectives for improvement of Mycoplasma hyopneumoniae vaccines in pigs.Veterinary research · 2021Review
- Construction ofFrontiers in microbiology · 2021Article
- Mycoplasma bovis Membrane Protein MilA Is a Multifunctional Lipase with Novel Lipid and Glycosaminoglycan Binding Activity.Infection and immunity · 2020Article
- Featured Species-Specific Loops Are Found in the Crystal Structure ofFrontiers in cellular and infection microbiology · 2019Article
- Extracellular DNA release from the genome-reduced pathogen Mycoplasma hyopneumoniae is essential for biofilm formation on abiotic surfaces.Scientific reports · 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
- TrmFO, a Fibronectin-Binding Adhesin of Mycoplasma bovis.International journal of molecular sciences · 2017Article
- Factors associated with seroconversion to the major piroplasm surface protein of the bovine haemoparasite Theileria orientalis.Parasites & vectors · 2016Article
- Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae.Open biology · 2016Article
- Mechanical transfer of Theileria orientalis: possible roles of biting arthropods, colostrum and husbandry practices in disease transmission.Parasites & vectors · 2016Article
- MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae.Open biology · 2015Article
- A recombinant chimera comprising the R1 and R2 repeat regions of M. hyopneumoniae P97 and the N-terminal region of A. pleuropneumoniae ApxIII elicits immune responses.BMC veterinary research · 2014Article
- Article
- Factors influencing the cell adhesion and invasion capacity of Mycoplasma gallisepticum.Acta veterinaria Scandinavica · 2013Article
- MHJ_0125 is an M42 glutamyl aminopeptidase that moonlights as a multifunctional adhesin on the surface of Mycoplasma hyopneumoniae.Open biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma hyopneumoniae is the causative agent of porcine enzootic pneumonia, a chronic and economically significant respiratory disease that affects swine production worldwide. M. hyopneumoniae adheres to and adversely affects the function of ciliated epithelial cells of the respiratory tract, and the cilium adhesin (Mhp183, P97) is intricately but not exclusively involved in this process. Although binding of pathogenic bacteria to glycosaminoglycans is a recognized step in pathogenesis, knowledge of glycosaminoglycan-binding proteins in M. hyopneumoniae is lacking. However, heparin and other sulfated polysaccharides are known to block the binding of M. hyopneumoniae to purified swine respiratory cilia. In this study, four regions within the cilium adhesin were examined for the ability to bind heparin. Cilium adhesin fragments comprising 653 amino acids of the N terminus and 301 amino acids of the C terminus (containing two repeat regions, R1 and R2) were cloned and expressed. These fragments bound heparin in a dose-dependent and saturable manner with physiologically significant binding affinities of 0.27 +/- 0.02 microM and 1.89 +/- 0.33 microM, respectively. Heparin binding of both fragments was strongly inhibited by the sulfated polysaccharides fucoidan and mucin but not by chondroitin sulfate B. When the C-terminal repeat regions R1 and R2 were cloned separately and expressed, heparin-binding activity was lost, suggesting that both regions are required for heparin binding. The ability of the cilium adhesin to bind heparin indicates that this molecule plays a multifunctional role in the adherence of M. hyopneumoniae to host respiratory surfaces and therefore has important implications with respect to the pathogenesis of this organism.
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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.