TY - JOUR
T1 - Loci and motifs of the GalNAcα1 → 3/O related glycotopes in the mammalian glycoconjugates and their lectin recognition roles
AU - Wu, Albert M.
N1 - Publisher Copyright:
© 2022, The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
PY - 2022/10
Y1 - 2022/10
N2 - Galα1 → and GalNAcα1 → are the two essential key sugars in human blood group AB active glycotopes, in which GalNAcα1 → related sequences are located at both sides of the nonreducing and the reducing ends of human blood group A active O-glycans. It is also found at the nonreducing ends of GlcNAc N-glycans and glycosphingolipid(GSL) of human blood group A active glycotopes (Ah) and Forssman antigen (Fp). When monosaccharides and their α, β anomers are involved in basic units to express the complex size of the combining sites of the GalNAcα1 → specific lectins, they can be divided into a cavity site to accommodate the GalNAcα → key sugar and a subsite with a wide and broad range of recognition area to adopt the rest part of sugar sequences or glycotopes. The function of the subsite is assumed to act as an enhancement factor to increase its affinity power. The following three points are the theme of this mini review: (1) the loci and distribution of the GalNAcα1 → related glycotopes in mammalian glycoconjugates are illustrated and their chemical structures are advanced by the expression of the disaccharide units and code system; (2) the sizes and motifs of GalNAcα1 → specific lectin-glycan interactions are given and (3) the role of the polyvalent blood group Ah and Bh glycotopes as blood group AB antigens are proposed. These three highlights should provide an essential background required for the advances in this field.
AB - Galα1 → and GalNAcα1 → are the two essential key sugars in human blood group AB active glycotopes, in which GalNAcα1 → related sequences are located at both sides of the nonreducing and the reducing ends of human blood group A active O-glycans. It is also found at the nonreducing ends of GlcNAc N-glycans and glycosphingolipid(GSL) of human blood group A active glycotopes (Ah) and Forssman antigen (Fp). When monosaccharides and their α, β anomers are involved in basic units to express the complex size of the combining sites of the GalNAcα1 → specific lectins, they can be divided into a cavity site to accommodate the GalNAcα → key sugar and a subsite with a wide and broad range of recognition area to adopt the rest part of sugar sequences or glycotopes. The function of the subsite is assumed to act as an enhancement factor to increase its affinity power. The following three points are the theme of this mini review: (1) the loci and distribution of the GalNAcα1 → related glycotopes in mammalian glycoconjugates are illustrated and their chemical structures are advanced by the expression of the disaccharide units and code system; (2) the sizes and motifs of GalNAcα1 → specific lectin-glycan interactions are given and (3) the role of the polyvalent blood group Ah and Bh glycotopes as blood group AB antigens are proposed. These three highlights should provide an essential background required for the advances in this field.
KW - Carbohydrate specificities and
KW - Combining size and site
KW - GalNAcα1 → 3/O related glycotopes and lectins, Super-glycotopes
KW - Glycoconjugate binding
KW - Glycotopes
KW - Polyvalency of glycotopes
KW - Recognition Factors
UR - http://www.scopus.com/inward/record.url?scp=85136926694&partnerID=8YFLogxK
U2 - 10.1007/s10719-022-10068-6
DO - 10.1007/s10719-022-10068-6
M3 - 文献综述
C2 - 35962217
AN - SCOPUS:85136926694
SN - 0282-0080
VL - 39
SP - 633
EP - 651
JO - Glycoconjugate Journal
JF - Glycoconjugate Journal
IS - 5
ER -