Differential responses to stress of two Mycoplasma hyopneumoniae strains

• Published in: Journal of proteomics Vol. 199; pp. 67 - 76
• Main Authors: Paes, Jéssica Andrade, Leal Zimmer, Fernanda M.A., Moura, Hercules, Barr, John R., Ferreira, Henrique Bunselmeyer
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 15.05.2019
• Subjects: Animals; Bacterial Proteins - analysis; Bacterial Proteins - genetics; Chromatography, Liquid; Heat stress; Heat-Shock Response; LC-MS/MS; Mycoplasma hyopneumoniae; Mycoplasma hyopneumoniae - genetics; Mycoplasma hyopneumoniae - pathogenicity; Mycoplasma hyopneumoniae - physiology; Oxidative Stress; Proteome - analysis; Proteome - genetics; Species Specificity; Stress, Physiological; Swine; Tandem Mass Spectrometry; Virulence; Oxidative stress; LC-MS/MS; Heat stress; Mycoplasma hyopneumoniae; Virulence
• ISSN: 1874-3919; 1876-7737
• DOI: 10.1016/j.jprot.2019.03.006

Mycoplasma hyopneumoniae is a respiratory pathogen, causing porcine enzootic pneumonia. To survive in the porcine respiratory tract, M. hyopneumoniae must cope with both oxidative and heat stress imposed by the host. To get insights into M. hyopneumoniae stress responses and pathogenicity mechanisms, the protein profiles of two M. hyopneumoniae strains, pathogenic 7448 strain and non-pathogenic strain J, were surveyed under oxidative (OS) or heat (HS) stress. M. hyopneumoniae strains were submitted to OS (0.5% hydrogen peroxide) or HS (temperature shifts to 42 °C) conditions and protein profiling was carried out by LC-MS/MS and label-free quantitative analyses. Data are available via ProteomeXchange with identifier PXD012742. Qualitative and quantitative differences involving 40–60 M. hyopneumoniae proteins were observed for both strains when comparing bacteria exposed to OS or HS to non-treated controls. However, no differences in abundance were found in proteins classically related to stress responses, as peroxidases and chaperones, suggesting that these proteins would be constitutively present in both strains in the tested conditions. Interestingly, under stress conditions, more virulence-related proteins were detected in M. hyopneumoniae 7448 differentially represented proteins than in M. hyopneumoniae J, suggesting that stress may trigger a differential response of the corresponding genes, shared by both strains. [Display omitted] •Protein profiles of two M. hyopneumoniae strains under oxidative or heat stress.•Comparison between pathogenic and non-pathogenic M. hyopneumoniae strains.•No differences in the proteins classically related to stress responses.•Virulence-related proteins detected in pathogenic M. hyopneumoniae under stress.