Recognition factors of Dolichos biflorus agglutinin (DBA) and their accommodation sites

In this study, many importnat recognition factors of DBA-glycan binding were characterized by our established enzyme-linked lectinosorbent (ELLSA) and inhibition assays. The results of these assays showed that the intensity profile of the recognition factors for the major combining site of DBA wa s expressed byMass relative potency (Mass R.P.) and shown by decreasing order of high density of polyvalent GalNAc α1 → (super glycotopes, 3.7 × 103)  >>  the corresponding β anomers >>  monomeric GalNAcα1 → related glycotopes (GalNAc as 1.0) >>  their GalNAc β-anomers >>  Gal (absence of NHCH3CO at carbon-2 of GAlNAc) and GlcNAc (different epimer of Carbon-4 in GalNAc). From the all data available, it is proposed that the combining site of DBA should consist of a small cavity shape as major site and most complementary to monomeric GalNAc α → located at both terminal reducing end (Tn) and nonreducing end of glycan chains, and with a wide and broad area as subsite to accomodate from mono- to tetra-saccharides (GalNAcβ, Galβ1 → 3/4GlcNAc, lFuc1 → 2Galβ1 → 3/4GlcNAc, GalNAcβ1 → 3Galα1 → 4Galβ1  → 4Glc) at the nonreducing side. In this study, it has provided the most (comprehensive) recognition knowledge of DBA-glycan interactions at the factors of glycotope, super glycotope/sub-monosaccharide levels. Thus, it should expand and upgrade the conventional concept of the combining (...

Source: Glycoconjugate Journal - June 2, 2023 Category: Biochemistry Source Type: research