Submitted to: Protein Society Symposium
Publication Type: Abstract Only
Publication Acceptance Date: 5/5/2006
Publication Date: 7/7/2006
Citation: Tabatabai, L.B., Zimmerli, M.K., Briggs, R.E., Tatum, F.M. 2006. The pasteurella multocida outer membrane proteome [abstract]. Protein Society Symposium. Paper No. 293-588.
Technical Abstract: Fowl cholera continues to be of major concern to the poultry industry, especially for turkey growers. This disease costs the turkey industry millions of dollars annually. Fowl cholera is caused primarily by three serotypes of Pasteurella multocida serotypes A:1, A:3, and A:4. a live attenuated vaccine strain, strain M-9 (serotype 3,4) has been implicated in outbreaks associated with vaccination. Recently, Rimler (2001) identified an outer membrane-associated protein with a molecular mass of 39,000 that was believed to be one of the cross protective factor and was later characterized by Tabatabai and Zehr (2004), using 1-D gels, peptide mass finger printing and C-18 HPLC purification of two tryptic peptides we identified the protein as Pasteurella lipoprotein B (Accession no.15603595). We used similar methods to identify the remainder of the 11 bands in the 1-D gel of the Sarkosyl-extracted insoluble residue that was solubilized in sodium dodecyl sulfate before electrophoresis. Only four additional proteins could be identified. The bands included a putative virulence factor (Accession no. 15603684), LipA (Accession no. 15602638), HemY (Accession no. 15603680), and Unknown lipoprotein (Accession No. 15602915). The recombinant form of the PlpB was cloned and the T10 fusion protein produced an immune response in turkey poults. These results suggest that it may be possible to design a recombinant vaccine to control fowl cholera.