ArticleVirulence2018
Comparative proteomics of two Mycoplasma hyopneumoniae strains and Mycoplasma flocculare identified potential porcine enzootic pneumonia determinants.
Article in Virulence, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- CD40 Ligand Potentiates Immunogenecity ofCurrent issues in molecular biology · 2025Article
- Comparative Proteomic Analysis of Secretory Proteins ofVeterinary sciences · 2023Article
- Differential domains and endoproteolytic processing in dominant surface proteins of unknown function fromHeliyon · 2023Article
- NADH oxidase of Mycoplasma hyopneumoniae functions as a potential mediator of virulence.BMC veterinary research · 2022Article
- Characteristics ofFrontiers in veterinary science · 2022Article
- Using a Relative Quantitative Proteomic Method to Identify Differentially Abundant Proteins inFrontiers in immunology · 2022Article
- Review
- Perspectives for improvement of Mycoplasma hyopneumoniae vaccines in pigs.Veterinary research · 2021Review
- Pathogenicity & virulence ofVirulence · 2020Review
- Mycoplasmas-Host Interaction: Mechanisms of Inflammation and Association with Cellular Transformation.Microorganisms · 2020Review
- Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y.Scientific reports · 2019Article
- Quantitative Proteomic Analyses of a Pathogenic Strain and Its Highly Passaged Attenuated Strain ofBioMed research international · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma hyopneumoniae and Mycoplasma flocculare are genetically similar bacteria, which coinhabit the porcine respiratory tract. These mycoplasmas share most of the known virulence factors, but, while M. hyopneumoniae causes porcine enzootic pneumonia (PEP), M. flocculare is a commensal species. To identify potential PEP determinants and provide novel insights on mycoplasma-host interactions, the whole cell proteomes of two M. hyopneumoniae strains, one pathogenic (7448) and other non-pathogenic (J), and M. flocculare were compared. A cell fractioning approach combined with mass spectrometry (LC-MS/MS) proteomics was used to analyze cytoplasmic and surface-enriched protein fractions. Average detection of ~ 50% of the predicted proteomes of M. hyopneumoniae 7448 and J, and M. flocculare was achieved. Many of the identified proteins were differentially represented in M. hyopneumoniae 7448 in comparison to M. hyopneumoniae J and M. flocculare, including potential PEP determinants, such as adhesins, proteases, and redox-balancing proteins, among others. The LC-MS/MS data also provided experimental validation for several genes previously regarded as hypothetical for all analyzed mycoplasmas, including some coding for proteins bearing virulence-related functional domains. The comprehensive proteome profiling of two M. hyopneumoniae strains and M. flocculare provided tens of novel candidates to PEP determinants or virulence factors, beyond those classically described.
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