Identification of novel post-translationally modified and antigenic proteins from the pathogenic Mycoplasma hyopneumoniae strain 7448
Paulo Marcos Pintoa, Gustavo Chemalea, Luiza Amaral de Castroa, Ana Paula Metz Costaa, Arnaldo Zahaa, Henrique Bunselmeyer Ferreiraa
aLaboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, UFRGS, Porto Alegre.
Mycoplasma hyopneumoniae is an important pathogen for pigs, being the causative agent of enzootic pneumonia (EP). Recently the genome sequences of three strains, J, 7448 and 232 have been reported. Here we present a proteomic study of M. hyopneumoniae pathogenic strain 7448. Two-dimensional gel electrophoresis of soluble protein extracts was carried out and a total of 73 protein spots were identified by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF-MS), allowing the elaboration of reference M. hyopneumoniae proteome maps in two pH ranges (3-10 and 4-7). Proteins from many different protein families were identified, including some related to cytoadherence and possibly involved in pathogenicity. Thirty one M. hyopneumoniae genes, including three hypothetical ones, were experimentally validated with the identification of the corresponding protein products. Putative post-translational modifications were found for 15 proteins (in a total of 41 spots). Moreover, at least five highly antigenic proteins of M. hyopneumoniae were identified by western blots, including four novel ones. This proteome map of M. hyopneumoniae is a useful reference for comparative analyses of pathogenic and non-pathogenic strains and of M. hyopneumoniae cells grown under modified conditions.
Support: MCT/CNPq, FAPERGS and CAPES.
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