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Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
Molecular cloning and characterization of a surface-localized adhesion protein in Mycoplasma bovis Hubei-1 strain
Xiaohui Zou1, Yuan Li, Yang Wang
1National Contagious Bovine Pleuropneumonia Reference Laboratory, Division of Bacterial Diseases, Harbin Veterinary Research Institute, CAAS, Harbin, China.
Abstract:
Mycoplasma bovis (M. bovis) is an important pathogen that causes various bovine diseases, such as mastitis in cows and pneumonia in calves. The surface proteins are generally thought to play a central role in the pathogenesis of this organism. We screened the entire genome of M. bovis Hubei-1 and discovered a gene named vpmaX that encodes the 25 kDa variable surface lipoprotein A (VpmaX). Sequence analysis revealed that VpmaX contains several repetitive units and a typical bacterial lipoprotein signal sequence. The vpmaX gene was cloned and expressed in E. coli to obtain recombinant VpmaX (rVpmaX). Western blot analysis using a rabbit antibody against rVpmaX demonstrated that VpmaX is a membrane protein. Immunostaining visualized via confocal laser scanning microscopy showed that rVpmaX was able to adhere to embryonic bovine lung cells (EBL), and this was also confirmed by a sandwich ELISA. In summary, a surface-localized adhesion protein was identified in M. bovis Hubei-1.
Insights
Researchers identified a novel surface protein, variable surface lipoprotein A (VpmaX), in Mycoplasma bovis. This protein is crucial for the pathogen
Area of Science:
- Veterinary Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Mycoplasma bovis is a significant bovine pathogen responsible for diseases like mastitis and pneumonia.
- Surface proteins are critical for the pathogenesis of M. bovis.
Purpose of the Study:
- To identify and characterize novel surface proteins involved in Mycoplasma bovis pathogenesis.
- To investigate the role of a newly discovered gene, vpmaX, and its encoded protein, VpmaX.
Main Methods:
- Genome screening of M. bovis Hubei-1 to identify the vpmaX gene.
- Gene cloning and expression in E. coli to produce recombinant VpmaX (rVpmaX).
- Western blot, confocal laser scanning microscopy, and sandwich ELISA to confirm protein localization and function.
Main Results:
- The vpmaX gene was identified, encoding a 25 kDa variable surface lipoprotein A (VpmaX) with repetitive units and a signal sequence.
- Western blot confirmed VpmaX as a membrane protein.
- Immunostaining and ELISA demonstrated that rVpmaX adheres to embryonic bovine lung cells (EBL).
Conclusions:
- A novel surface-localized adhesion protein, VpmaX, has been identified in Mycoplasma bovis Hubei-1.
- VpmaX likely plays a role in the adhesion of M. bovis to host cells, contributing to its pathogenesis.
