1. Proteomic Analysis of the Interactions between Mycoplasma hyopneumoniae and Porcine Tracheal Ciliated Cells
- Author
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Shui-Tein Chen, Yen-Peng Ho, David Shiuan, and Yuan-Zuo Li
- Subjects
Proteome ,Sus scrofa ,Bioengineering ,Biology ,Blotting, Far-Western ,Proteomics ,Applied Microbiology and Biotechnology ,Biochemistry ,Bacterial Adhesion ,Microbiology ,Bacterial Proteins ,Mycoplasma hyopneumoniae ,Animals ,Humans ,Electrophoresis, Gel, Two-Dimensional ,Mycoplasma Infections ,Cilia ,Receptor ,Molecular Biology ,Cells, Cultured ,Cell adhesion molecule ,Epithelial Cells ,General Medicine ,biology.organism_classification ,Trachea ,Blot ,Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ,Host-Pathogen Interactions ,Peroxiredoxin ,Lamin ,Biotechnology - Abstract
Mycoplasma hyopneumoniae colonizes at the porcine respiratory-ciliated epithelial cells and causes the enzootic pneumonia of swine. The adhesion step is crucial in the colonization process. A few adhesion molecules have been characterized, and the concurrent receptors from the porcine ciliated cells have also been suggested to recognize the adhesion molecules. In the present study, the interactions between M. hyopneumoniae and porcine tracheal ciliated cells were investigated by employing the Far-Western blotting method. The results indicate that aconitase, lamin A/C, and peroxiredoxin of the porcine tracheal ciliated cell may interact specifically with the mycoplasmal proteins. We speculate that these mycoplasmal proteins could be secreted cleavage products, and their relative small size may enable them to penetrate into ciliated cells interfering with important metabolic pathways and other critical cellular processes.
- Published
- 2009