title: Nutritionally variant streptococcal serotype I antigen. Characterization as a lipid-substituted poly(ribitol phosphate).
abstract: Initial characterization of the nutritionally variant streptococcal serotype I amphipathic polymer indicated an estimated m.w. of 360,000 for the aggregated form of the molecule, whereas the dissociated form had an estimated m.w. of 38,000 based on dextran m.w. standards. In addition, SDS-PAGE indicated an amphiphile with a stepladder appearance made up of several components with m.w. larger than the major electrophoresis components of LPS or lipoteichoic acid. Chemically, the serotype I amphiphile appeared to be a lipid-substituted poly(ribitol phosphate) with galactose and alanine substitution on the ribitol phosphate backbone. This report represents the first characterization of a bacterial amphiphile with a chemical composition and structure as proposed here. As is the case with other bacterial amphiphiles, the nutritionally variant streptococcal serotype I amphiphile was found both intra- and extracellularly. Finally, immunofluorescence studies demonstrated that the amphiphile was expressed on the cell surface.
authors.affiliation: Wake Forest University Medical Center, Winston-Salem, NC 27103.
authors.forename: M
authors.initials: M
authors.lastname: George
authors.forename: I
authors.initials: I
authors.lastname: van de Rijn
mesh_terms: D000409:Alanine / Q000032:analysis; D000942:Antigens, Bacterial / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D005690:Galactose / Q000032:analysis; D006385:Hemagglutination Inhibition Tests; D008055:Lipids / Q000032:analysis; D008970:Molecular Weight; D011134:Polysaccharides / Q000276:immunology / Q000302:isolation & purification*; D013291:Streptococcus / Q000032:analysis / Q000276:immunology*
chemical_list: D000942:Antigens, Bacterial; D008055:Lipids; D011134:Polysaccharides; C008984:polyribitol phosphate; D000409:Alanine; D005690:Galactose