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O-antigen chain length

Larue, K., Kimber, M.S., Ford, R., Whitfield, C. Biochemical and structural analysis of bacterial O-antigen chain length regulator proteins reveals a conserved quaternary structure. J Biol Chem 284 (2009) 7395-7403. [Pg.23]

Delgado, M., Mouslim, C., Groisman, E. The PmrA/PmrB and RcsC/YojN/RcsB systems control expression of the Salmonella O-antigen chain length determinant. Mol Microbiol 60 (2006) 39-50. [Pg.116]

Morona, R., van den Bosch, L., Manning, P. Molecular, genetic, and topological characterization of O-antigen chain length regulation in Shigella flexneri. J Bacteriol 177 (1995) 1059-1068. [Pg.119]

The O Antigen Chain Lengths is Important for the Full Virulence... [Pg.144]

Franco, V.A., Liu, D., Reeves, P.R. The Wzz (Cld) protein in Escherichia coli amino acid sequence variation determines O antigen chain length specificity. J Bacteriol 180 (1998) 2670-2675. [Pg.147]

Like Escherichia coli, clinical isolates of H. pylori produce high-molecular-mass (smooth-form) lipopolysaccharide (LPS) composed of an outermost saccharide moiety, divided into the O-polysaccharide or O-specific chain (O-antigen) and core oligosaccharide (OS) regions, covalently linked to lipid A (Fig. 10.1). H. pylori smooth-form LPS possesses O-polysaccharide chains of relatively constant chain length compared with those of enterobacterial LPS (Moran et al., 1992a Moran, 1999). Their length is determined by an enzymatic molecular ruler mechanism... [Pg.211]

Figure 2 Pathways for O antigen assembly, (a) Wzy-dependent pathway. After the initiation reaction, glycosyltransferases extend the O antigen until the completion of the repeating unit, which is translocated across the membrane by Wzz. In the periplasmic side of the membrane nascent units are polymerized by Wzy and the control of the chain length distribution is carried out by Wzz. (b) ABC transporter-dependent pathway. In this pathway the polymer is formed intracellular and terminated by the addition of a termination signal (black square), which also couples the polymer to the Wzt protein. ATP hydrolysis is required for export across the membrane, (c) Synthase-dependent pathway. After initiation, one more adaptor sugar is added (black circle) and the WbbF bifunctional enzyme that is also responsible for its vectorial translocation across the inner membrane extends the rest of the polymer. Figure 2 Pathways for O antigen assembly, (a) Wzy-dependent pathway. After the initiation reaction, glycosyltransferases extend the O antigen until the completion of the repeating unit, which is translocated across the membrane by Wzz. In the periplasmic side of the membrane nascent units are polymerized by Wzy and the control of the chain length distribution is carried out by Wzz. (b) ABC transporter-dependent pathway. In this pathway the polymer is formed intracellular and terminated by the addition of a termination signal (black square), which also couples the polymer to the Wzt protein. ATP hydrolysis is required for export across the membrane, (c) Synthase-dependent pathway. After initiation, one more adaptor sugar is added (black circle) and the WbbF bifunctional enzyme that is also responsible for its vectorial translocation across the inner membrane extends the rest of the polymer.
Leinonen A, Netzer K-O, Boutourd A, et al. Goodpasture antigen expression of fidl length a3(IV) chain of type IV coUagen and locahzation of epitopes exclusively to the noncoUagenous (NCI) domain. Kidney Int 1999 55 926 35. [Pg.687]


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See also in sourсe #XX -- [ Pg.10 , Pg.108 ]




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