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Haemophilus parasuis is the causative agent of Glässer’s disease, a respiratory illness in swine, which causes significant economic loss in the industry. To date, there is no commercially available cross-protective vaccine or diagnostic for this disease. Because of this, identification and characterization of putative virulence factors is crucial. In order to understand the mechanism of infection of H. parasuis, it is imperative to not only identify proteins traditionally associated with virulence but to also recognize differences that exist for those proteins at a molecular and/or expression level. Using a combination of bottom-up and isobaric-tagging for relative and absolute quantification (iTRAQ) proteomic strategies, Nterminal sequencing, molecular modeling and antigenic characterization techniques, putative virulence factors have been identified and characterized. In attempt to identify the P2 and P5 colonization factors of H. parasuis, tandem mass spectrometry was performed following 2-D SDS-PAGE immunoblots with a monoclonal antibody to OMP P5 of H. influenzae. While OMP P2 was identified using this method, OMP P5 was not. Additional proteins identified include: TRAP solute transporter, glucose-specific PTS system enzyme IIA, acetyl-CoA carboxylase biotin carboxylase subunit, purine nucleoside phosphorylase, chelated iron ABC transporter, probable sugar isomerase, Mn-dependent superoxide dismutase, putative iron ABC transporter, D-ribose transporter, alanine aminotransferase, phosphoribosylglycinamide formyltransferase, FbpA, and hypothetical proteins HPS 06844 and HPS 10240. Sequence and structural alignment of identified proteins with H. influenzae OMP P5 were used in order to elucidate common epitopes for antibody 4BF8 with no success. Molecular modeling and

Identification and characterization of the major outer membrane proteins of &lt;em&gt;Haemophilus parasuis&lt;/em&gt; for the rational development of a vaccine candidate and diagnostic for Glässer's disease