Submitted to: Research Workers in Animal Diseases Conference Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 9/21/2001
Publication Date: 11/11/2001
Citation: OSMUNDSON, R.S., TABATABAI, L.B. IDENTIFICATION, ISOLATION AND CHARACTERIZATION OF AN IMMUNOGLOBULIN BINDING PROTEIN EXPRESSED BY MANNHEIMIA HAEMOLYTICA (POSTER PRESENTATION FOR THE 82ND CONFERENCE OF RESEARCH WORKERS IN ANIMAL DISEASE). RESEARCH WORKERS IN ANIMAL DISEASES CONFERENCE PROCEEDINGS. 2001. Abstract #100P.
Technical Abstract: Mannheimia haemolytica is the known causative agent of bovine pasteurellosis or "shipping fever." Bacterial immunoglobulin binding protein (IBP) expression is known to play a role in the pathogenesis of a variety of organisms. This study demonstrates the presence of an IBP in a whole cell sonicate (WCS) preparation and a culture supernatant from an M. haemolytica A1 culture. The IBP was isolated by affinity chromatography using bovine Fc fragments bound to Sepharose. The 57,000 Da protein was found to have a pI of 5.7. Immune sera from convalescent cattle showed an increased antibody response to IBP when compared to sera from naive or actively infected cattle. Although M. haemolytica serotype A1 is most frequently associated with pasteurellosis in cattle, it was demonstrated that all 12 serotypes (1, 2, 5, 6, 7, 8, 9, 11, 13, 14, and 16) bound both bovine Fc and sheep Fc. These results suggest that an immune response to the 57,000 Da IBP may play a role in protection from M. haemolytica infection and may be an important component in vaccine preparations. However, species-specific Fc binding does not appear to play a role in species-specific infection by different serotypes of M. haemolytica.