ArticleThe Journal of biological chemistry2011
Sequence TTKF ↓ QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin 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 30 papers.
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Who cites it
30 citing papers in PubMed, 56 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
- Differential domains and endoproteolytic processing in dominant surface proteins of unknown function fromHeliyon · 2023Article
- Mycoplasma hyopneumoniae membrane protein Mhp271 interacts with host UPR protein GRP78 to facilitate infection.Molecular microbiology · 2022Article
- Incomplete autophagy promotes the proliferation of Mycoplasma hyopneumoniae through the JNK and Akt pathways in porcine alveolar macrophages.Veterinary research · 2022Article
- Characterization and Evaluation of a Novel Conserved Membrane Antigen P35 ofFrontiers in veterinary science · 2022Article
- Review
- 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 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
- 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
- Elongation factor Tu is a multifunctional and processed moonlighting protein.Scientific reports · 2017Article
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Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma hyopneumoniae colonizes the ciliated respiratory epithelium of swine, disrupting mucociliary function and inducing chronic inflammation. P97 and P102 family members are major surface proteins of M. hyopneumoniae and play key roles in colonizing cilia via interactions with glycosaminoglycans and mucin. The p102 paralog, mhp683, and homologs in strains from different geographic origins encode a 135-kDa pre-protein (P135) that is cleaved into three fragments identified here as P45(683), P48(683), and P50(683). A peptide sequence (TTKF↓QE) was identified surrounding both cleavage sites in Mhp683. N-terminal sequences of P48(683) and P50(683), determined by Edman degradation and mass spectrometry, confirmed cleavage after the phenylalanine residue. A similar proteolytic cleavage site was identified by mass spectrometry in another paralog of the P97/P102 family. Trypsin digestion and surface biotinylation studies showed that P45(683), P48(683), and P50(683) reside on the M. hyopneumoniae cell surface. Binding assays of recombinant proteins F1(683)-F5(683), spanning Mhp683, showed saturable and dose-dependent binding to biotinylated heparin that was inhibited by unlabeled heparin, fucoidan, and mucin. F1(683)-F5(683) also bound porcine epithelial cilia, and antisera to F2(683) and F5(683) significantly inhibited cilium binding by M. hyopneumoniae cells. These data suggest that P45(683), P48(683), and P50(683) each display cilium- and proteoglycan-binding sites. Mhp683 is the first characterized glycosaminoglycan-binding member of the P102 family.
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