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Proteomic Comparative Analysis of Pathogenic Strain 232 and Avirulent Strain J of Mycoplasma hyopneumoniae

Yuan-Zuo Li1, Yen-Peng Ho2, Shui-Tein Chen3, Tzyy-Wen Chiou1, Zong-Sian Li2, and David Shiuan1*

1Department of Life Science and Institute of Biotechnology, National Dong Hwa University, Hualien, 974 Taiwan, ROC; fax: (8863) 863-3630; E-mail: shiuan@mail.ndhu.edu.tw

2Department of Chemistry, National Dong Hwa University, Hualien, Taiwan, ROC

3Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, ROC

* To whom correspondence should be addressed.

Received March 7, 2008; Revision received April 2, 2008
Mycoplasma hyopneumoniae is an important pathogen of pigs causing enzootic pneumonia of swine. The pathogen remains largely enigmatic as far as the host–pathogen interactions are concerned. In the present study, the protein profiles of two strains of M. hyopneumoniae were compared by two-dimensional gel electrophoresis and mass spectrometry. The results indicate that the major adhesin P97, the 50-kDa protein derived from P159 adhesin, and the 43-kDa cleavage product of P102 are expressed at much higher levels in the pathogenic strain 232. In contrast, the avirulent strain J switches its focus to metabolism and expresses more glyceraldehyde 3-phosphate dehydrogenase in gluconeogenesis and lactate dehydrogenase, pyruvate dehydrogenase, and phosphate acetyltransferase in the pyruvate metabolism pathway. We speculate that the avirulent strain may have developed better capabilities to cope with the rich environment during repeated inoculations. Simultaneously, the capability to infect host cells may become less important so that the adhesion-related protein genes are down-regulated.
KEY WORDS: Mycoplasma hyopneumoniae, proteomics, virulence factors

DOI: 10.1134/S0006297909020138