|Van Schilfgaarde, Muriel|
Submitted to: Federation of American Societies for Experimental Biology Conference
Publication Type: Abstract Only
Publication Acceptance Date: 3/4/2005
Publication Date: 4/4/2005
Citation: Tabatabai, L.B., Mcvicker, J.K., Zimmert, M.K., Zehr, E.S., Van Schilfgaarde, M. 2005. Identification and properties of haemophilus parasuis adhesion proteins. Federation of American Societies for Experimental Biology Conference. Abstract #11885. Interpretive Summary:
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 pleuritis, meningitis, swollen joints and polyserositis with or without death. Commercial vaccines and autogenous vaccines are available, but are not completely effective. To develop improved vaccines, a study was undertaken to examine proteins that may play a role in colonization. P2 and P5 outer membrane proteins, homologues of Haemophilus influenzae, were investigated. Monoclonal antibody (Mab) to H. influenzae P5 protein was used to identify the P2 and P5 proteins H. parasuis serovars 2 and 3, virulent and avirulent strains, respectively. The N-terminal sequence of H. parasuis 32 kDa P5 protein was homologous to the H. influenzae 32 and 48 kDa proteins. The Mab also identified a conserved epitope in the H. influenzae 55 kDa P2 protein and the H. parasuis 48 and 55 kDa proteins from virulent strain 2 and avirulent strain 3, respectively in 1-D and 2-D gels. H. influenzae P2 and P5 proteins bind human CEACAM1, a member of the carcinoembryonic antigen family of proteins. H. parasuis P2 protein, but not the P5 protein, bound the CEA antigen. Provided human CEA is similar to porcine CEA, CEA-binding could play a role in Glässer's disease, and play a role in immunosuppression often observed in Glässer's disease.