TY - JOUR
T1 - Observation of Unique Cross-Linked Lattices between Multiantennary Carbohydrates and Soybean Lectin. Presence of Pseudo-2-fold Axes of Symmetry in Complex Type Carbohydrates
AU - Gupta, Dipti
AU - Bhattacharyya, Lokesh
AU - Brewer, C. Fred
AU - Fant, Jane
AU - Macaluso, Frank
AU - Sabesan, Subramaniam
PY - 1994/5/1
Y1 - 1994/5/1
N2 - The tetrameric lectin from Glycine max (soybean) (SBA) has been shown to cross-link and precipitate with N-linked multiantennary complex type oligosaccharides containing nonreducing terminal Gal residues (Bhattacharyya, L., Haraldsson, M., & Brewer, C. F. (1988) Biochemistry 27, 1034–1041). In the present study, negative stain electron micrographs of the precipitates of SBA with a series of naturally occurring and synthetic multiantennary carbohydrates with terminal Gal or GalNAc residues show the presence of highly ordered cross-linked lattices for many of the complexes. The precipitates of SBA with a “bisected” and “nonbisected” N-linked biantennary complex type oligosaccharide containing Gal residues at the nonreducing termini show similar two-dimensional patterns. However, the pattern observed for the precipitates of a tetraantennary complex type oligosaccharide with SBA is distinct from those of the two biantennary carbohydrates. Furthermore, the precipitates formed between the lectin and a synthetic O-linked biantennary (“cluster”) glycoside with terminal GalNAc residues show a pattern that is different from those above. Four biantennary pentasaccharide analogs of the blood group I antigen containing β-LacNAc moieties at the 2,3-, 2,4-, 2,6-, and 3,6-positions of the core Gal also showed ordered patterns in their precipitates with SBA. X-ray crystallographic data and mixed quantitative precipitation profiles of binary mixtures of the four analogs demonstrate that each analog possesses a unique cross-linked lattice with the protein. A common structural feature of the naturally occurring and synthetic carbohydrates that show highly organized cross-linked lattices with SBA is the presence of a pseudo-2-fold axis of symmetry in each oligosaccharide relating the terminal binding epitopes on each arm. This suggests that the symmetry features of certain naturally occurring branch chain oligosaccharides facilitate formation of highly ordered, homogeneous cross-linked complexes with specific lectins.
AB - The tetrameric lectin from Glycine max (soybean) (SBA) has been shown to cross-link and precipitate with N-linked multiantennary complex type oligosaccharides containing nonreducing terminal Gal residues (Bhattacharyya, L., Haraldsson, M., & Brewer, C. F. (1988) Biochemistry 27, 1034–1041). In the present study, negative stain electron micrographs of the precipitates of SBA with a series of naturally occurring and synthetic multiantennary carbohydrates with terminal Gal or GalNAc residues show the presence of highly ordered cross-linked lattices for many of the complexes. The precipitates of SBA with a “bisected” and “nonbisected” N-linked biantennary complex type oligosaccharide containing Gal residues at the nonreducing termini show similar two-dimensional patterns. However, the pattern observed for the precipitates of a tetraantennary complex type oligosaccharide with SBA is distinct from those of the two biantennary carbohydrates. Furthermore, the precipitates formed between the lectin and a synthetic O-linked biantennary (“cluster”) glycoside with terminal GalNAc residues show a pattern that is different from those above. Four biantennary pentasaccharide analogs of the blood group I antigen containing β-LacNAc moieties at the 2,3-, 2,4-, 2,6-, and 3,6-positions of the core Gal also showed ordered patterns in their precipitates with SBA. X-ray crystallographic data and mixed quantitative precipitation profiles of binary mixtures of the four analogs demonstrate that each analog possesses a unique cross-linked lattice with the protein. A common structural feature of the naturally occurring and synthetic carbohydrates that show highly organized cross-linked lattices with SBA is the presence of a pseudo-2-fold axis of symmetry in each oligosaccharide relating the terminal binding epitopes on each arm. This suggests that the symmetry features of certain naturally occurring branch chain oligosaccharides facilitate formation of highly ordered, homogeneous cross-linked complexes with specific lectins.
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U2 - 10.1021/bi00184a600
DO - 10.1021/bi00184a600
M3 - Article
C2 - 8180186
AN - SCOPUS:0028234894
SN - 0006-2960
VL - 33
SP - 5614
EP - 5622
JO - Biochemistry
JF - Biochemistry
IS - 18
ER -