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anatipestifer localizes to the outer membrane. In this study, we confirmed that B739_0832 protein in R. Although OmpH in some pathogenic bacteria, such as Pasteurella, has been reported as a virulence factor, it is still not clear whether B739_0832 protein contributes to the virulence of R. anatipestifer infection using B739_0832 protein, a putative outer membrane protein H (OmpH) that is conserved among different serotypes of R. In a previous study, we developed an indirect ELISA method for detecting R. anatipestifer is still poorly understood for its pathogenesis mechanisms. However, as a harmful pathogen causing significant economic losses in the poultry industry, R. Riemerella anatipestifer causes serious contagious disease in ducks, geese, and other fowl. Instead, our analysis reveals a highly conserved salt-bridge network, which likely has a role for Skp function.Ĭopyright © 2015 Biophysical Society. Bioinformatic analysis of amino acid conservation, structural analysis of LPS-binding proteins, and MD simulations further confirm the absence of a specific LPS binding site on Skp, making a biological relevance of the interaction unlikely. High-resolution NMR spectroscopy measurements indicate that LPS interacts with Skp nonspecifically, accompanied by destabilization of the Skp trimer and similar to denaturation by the nonnatural detergent lauryldimethylamine-N-oxide (LDAO). In this study, we revisit the specificity of the chaperone-lipid interaction of Skp and LPS. These nonsoluble compounds are conveyed across the aqueous periplasm along specific molecular transport routes: the lipid lipopolysaccharide (LPS) is shuttled by the Lpt system, whereas outer membrane proteins (Omps) are transported by chaperones, including the periplasmic Skp. The bacterial outer membrane comprises two main classes of components, lipids and membrane proteins. It consists of 141 amino acids, possesses regions very rich in basic amino acids, and has a molecular mass of 15,862 kDa. By combining protein and nucleotide sequence data, we determined the primary structure of the entire OmpH protein. Furthermore, we isolated by molecular cloning the corresponding gene, named it ompH, and determined its nucleotide sequence. 72% of the total amino acid sequence was determined by sequencing several HPLC-purified proteolytic fragments and 55 amino acids from the NH2 terminus. It had a molecular mass of 16 kDa, a pI above 10.0, and was rich in arginine and lysine. The most abundant (OMB2) was purified in preparative acid-urea polyacrylamide gel electrophoresis and reversed-phase high pressure liquid chromatography (HPLC).

typhimurium, one strain of Salmonella minnesota, and three strains of Escherichia coli K12) had those proteins. Also, all the other enterobacterial strains studied (five additional strains of S.

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