The immunochemistry of Shigella flexneri O-antigens. The biochemical basis of smooth to rough mutation.

1. Smooth to rough mutation has the same biochemical basis in Shigella as in Salmonella. It is the result of enzyme defects blocking the incorporation of the O-specific side chains that characterize the smooth lipopolysaccharide with the consequent exposure of the underlying basal structures that determine ;rough'-specificity. 2. The Shigella flexneri basal structure resembles its Salmonella analogue in that it has the same qualitative sugar composition, and enzyme defects in its biosynthetic pathway give rise to ;rough'-lipopolysaccharides that are indistinguishable from those of Salmonella chemotypes Ra, Rb, Rc and Rd. However, the Salmonella and Shigella basal structures are not identical as judged by quantitative analysis and the absence of serological cross-reaction. 3. The Sh. flexneri basal structure side chain has been isolated and characterized as an alpha-N-acetylglucosaminyl-(1-->4)-galactosyl-(1-->3)-glucose sequence with alpha-glucosyl radicals substituted on the 3- and 4-positions of the galactose and glucose respectively. The different sugar types in this side chain are incorporated into the growing molecule in the same order as in Salmonella, which explains why the enzyme defects associated with smooth to rough mutation produce the same series of R-chemotypes from both genera. The terminal alpha-glucosyl and alpha-N-acetylglucosaminyl-(1-->4)-galactosyl residues of the Sh. flexneri basal structure are sufficiently different from the terminal alpha-galactosyl and alpha-N-acetylglucosaminylglucosyl residues of the Salmonella analogue that they offer an explanation for the absence of serological cross-reaction between these two basal structures.