P27 (MBOV_RS03440) is a novel fibronectin binding adhesin of Mycoplasma bovis

Mycoplasma bovis, one of the major pathogens of bovine respiratory disease, binds to respiratory epithelial cells resulting in severe pneumonia and tissue damage. This study was designed to identify the adhesive function of a putative 27-kDa M. bovis lipoprotein, encoded by the gene MBOV_RS03440 and...

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Bibliographic Details
Published in:International journal of medical microbiology 2018-10, Vol.308 (7), p.848-857
Main Authors: Chen, Xi, Huang, Jing, Zhu, Hongmei, Guo, Yongpeng, Khan, Farhan Anwar, Menghwar, Harish, Zhao, Gang, Guo, Aizhen
Format: Article
Language:English
Subjects:
Adhesin
Adhesins, Bacterial - genetics
Adhesins, Bacterial - metabolism
Animals
Antibodies, Bacterial - immunology
Bacterial Adhesion - physiology
Bind
Cattle
Cattle Diseases - microbiology
Cells, Cultured
Fibronectin
Fibronectins - metabolism
Lipoproteins - genetics
Lipoproteins - immunology
Lipoproteins - metabolism
MBOV_RS03440
Mycoplasma bovis
Mycoplasma bovis - genetics
Mycoplasma bovis - pathogenicity
P27
Pneumonia - microbiology
Pneumonia - veterinary
Protein Binding
Respiratory Mucosa - microbiology
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Summary:Mycoplasma bovis, one of the major pathogens of bovine respiratory disease, binds to respiratory epithelial cells resulting in severe pneumonia and tissue damage. This study was designed to identify the adhesive function of a putative 27-kDa M. bovis lipoprotein, encoded by the gene MBOV_RS03440 and designated as P27. The gene was cloned and overexpressed to produce antibodies against the recombinant P27 (rP27). The western blot and flow cytometry assay confirmed P27 to be a surface-localized protein, while ELISA confirmed it to be an immunogenic protein. Confocal immunofluorescence microscopy demonstrated that rP27 bound to embryonic bovine lung (EBL) cell monolayers in a dose-dependent manner. Furthermore, anti-rP27 antiserum inhibited the attachment of M. bovis to EBL cells demonstrating the binding specificity of P27 to EBL cells. The attachment of rP27 to EBL cells was mediated by fibronectin (Fn), an extracellular matrix component. The interaction between rP27 and Fn was qualitatively and quantitatively monitored by ligand immunoblot assay, ELISA, and biolayer interferometry. Collectively, these results indicate that P27 is a novel Fn-binding, immunogenic adhesive protein of M. bovis, thereby contributing to the further understanding of the molecular pathogenesis of M. bovis.
ISSN:1438-4221
1618-0607
DOI:10.1016/j.ijmm.2018.07.006