Submitted to: Protein Society Symposium
Publication Type: Abstract Only
Publication Acceptance Date: 5/5/2006
Publication Date: 7/7/2006
Citation: Zimmerli, M.K., Tabatabai, L.B. 2006. Identification and characteriazation of haemophilus parasuis p2 and p5 adhesin proteins [abstract]. Protein Society Symposium. Paper No. 134-588.
Technical Abstract: Haemophilus parasuis is the causative agent of Glässer’s disease and is a re-emerging pathogen of swine reared in segregated early weaning facilities. Symptoms include meningitis, pleuritis, swollen joints and polyserositis with or without death. Since there is no current vaccine nor diagnostic for this disease, identification of proteins involved in virulence is critical. Previously, P2 and P5, homologues of H. influenzae adhesin proteins, were identified in H. parasuis using Western blot and N-terminal sequencing analysis (McVicker and Tabatabai, Prep. Biochem. Biotechnol, 2006). We used 2-D electrophoresis followed by mass/peptide fingerprint analysis using MALDI-TOF MS to identify P2 and P5 peptides from virulent and avirulent strains of H. parasuis. Amino acid sequences of these proteins were determined by electrospray tandem MS (ESI-MS/MS) analysis of protein of trypsin digests of the P2 and P5 proteins, and the data were analyzed by using MASCOT. The results of these studies revealed that the 32kDa P5 protein has a pI of 5.5 for all serovars and the sequence is homologous to the P5 protein of H. influenzae. The P2 protein in H. parasuis, however, has a pI of 6.0 for virulent serovars and a pI of 9.0 for non-virulent serovars. Also, the molecular weight of the P2 protein differs among the serovars. Together, these results will permit us to design peptide-based vaccines and diagnostics for Glässer’s disease of pigs.