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A native strain of Pasteurella multocida wasisolated from pigs suffering from severe atrophic rhinitis atdomestic farms in Gyeonggi Province, Korea, and was identifiedas capsular serogroup "D" and somatic serotype "4" by discdiffusion decapsulation and gel diffusion precipitation tests,respectively. The P. multocida (D:4) induced atrophic rhinitisin healthy pigs by the secondary infection. The gene for outermembrane protein H (ompH) of P. multocida (D:4) wascloned in Escherichia coli DH5α by PCR. The open readingframe of the ompH was composed of 1,023 bp, possiblyencoding a protein with 341 amino acid residues containing asignal peptide of 20 amino acids at N-terminus, and the geneproduct with molecular mass of ca. 38 kDa was identified bySDS-PAGE. Hydropathy profiles indicated that there are twovariable domains in the OmpH. To express the ompH in E.coli, the gene was manipulated in various ways. Expression ofthe truncated as well as full-length forms of the recombinantOmpH was fatal to the host E. coli BL21 (DE3). However, thetruncated OmpH fused with GST was consecutively expressedin E. coli DH5α. A large quantity of the fused polypeptidewas purified through GST-affinity chromatography.

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