Immunochemical and structural characterization of the antigenic polysaccharide from Eubacterium saburreum T18

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Abstract
An antigenic surface polysaccharide produced by Eubacterium saburreum strain T18, isolated from human dental plaque, was purified from formamide extract of whole cells. Methylation analysis, Smith degradation, optical rotation data and nuclear magnetic resonance spectra demonstrated that the purified antigen was a homopolysaccharide composed of D‐glycero‐D‐galacto‐heptose (Hep.) residues. The structure of the repealing unit in the polysaccharide was: ‐(→6)‐[α‐Hep.furanosyl‐(1→4)]‐β‐Hep.pyranosyl‐(1→6)‐[α‐Hep.furanosyl‐(1→2), α‐Hep.furanosyl‐(l→4)]‐β‐Hep.pyranosyl‐(1‐)4→6)‐β‐Hep.pyranosyl‐(l→. No heptose residues were acetylated. Immunodiffusion reactions in agar gel suggested that the immunodeterminant of the antigenic polysaccharide was D‐glycero‐D‐galacto‐heptofuranosyl residues as branched nonreducing terminals.