| Haemophilus parasuis is the etiologic agent of Gl?sser's disease in pigs, which causes highmorbidity and mortality in naive swine populations and is pathologicallycharacterized by serofibrinousto fibrino-purulent polyserositis, arthritis and meningitis. H. parasuis additionally causes pneumonia inthe absence of systemic disease but is also often carried in the nasal passages of seemingly healthy.Monoclonal antibody (MAb) 2D2 against H.parasuis were obtained by the fusion of SP2/0 murinemyeloma cells and spleen cells from BALB/c mice immunized with a whole-bacterial-cell suspension(WC) of H. parasuis filed isolated strain HLJ-018. The bacterial clearance assay showed that Mab 2D2was also able to reduce prevalence of H.parasuis colonization comparing to the control group in vivo.Then we used random heptapeptide library displayed by bacteriophage 12-mer to characterizemimotope from Mab 2D2. After three rounds of panning, 12 phages were selected and identified byELISA and sequenced. The alignment analysis revealed that amino acid homology in that all 12 clonescontained a continues sequence of G-A-P-M-H-M-A-T-L, BLASTp analysis reveals that highamino-acid sequence homology to Ferrous iron transport protein(FeoB), FeoB is a G-protein coupledmembrane protein essential for Fe (II) uptake in prokaryotes and is the major component of the ferrousiron transporter (Feo) system. The ferrous iron acquisition system has been experimentally identified infive additional microbes: Porphyromonas gingivalis, Leptospira biflexa , Shigella flexneri, Legionellapneumophila, and the cyanobacterium Synechocystis sp. In our study we got a Mab can eliminate thebacteria from the blood. Using the technology of phage display to map the epitope of H.parasuis MAb,an epitope homology to FeoB was obtained.Our results were helpful for further structural and functional research on H. parasuis protein anddevelopment of vaccine and drugs of H. parasuis. |
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