1887

Abstract

is one of the most extensively studied bacterial species in terms of physiology, genetics, cell culture and development. As a very diverse group, the serovars of display a spectrum of host specificities ranging from a broad host range to strictly host-adapted variants. This study utilized a classic proteomic approach combining 2D gel electrophoresis and mass spectrometry for the comparative analysis of the proteomes of serovars Typhimurium, Enteritidis, Choleraesuis, Pullorum and Dublin. The comparative analysis revealed species-specific protein factors with no significant change in expression amongst all isolates, as well as proteins with fluctuating expression levels between serovars and strains. Examples include an isoform of SodA specific for serovar Typhimurium, the third isoform of the lysine arginine ornithine (LAO)-binding amino acid transporter specific for serovar Pullorum, and the enzyme GabD found to be unique to serovar Choleraesuis. Overall the study demonstrated the importance of using multiple isolates when characterizing the expression patterns of bacteria in order to account for the intrinsic diversity of a bacterial population and revealed several factors with potential roles in host adaptation and pathogenicity of the serovars of .

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2007-12-01
2019-10-14
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vol. , part 12, pp. 4183 - 4193

All identified proteins with the average intensity values measured using Proteome Weaver in two replicate gels. The table includes differentially expressed proteins as well as stable protein factors with uniform expression amongst all isolates. In several cases a protein was not detected in any of the isolates representing a serovar. The presence of the gene encoding such protein in the genome of the serovar is indicated where appropriate (e.g ). [ PDF] (15 kb)



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