TY - JOUR
T1 - Polyvalent GalNAcα1→Ser/Thr (Tn) and Galβ1→ 3GalNAcα1→Ser/Thr (T α) as the most potent recognition factors involved in Maclura pomifera agglutinin-glycan interactions
AU - Wu, Albert M.
PY - 2005/1
Y1 - 2005/1
N2 - The agglutinin isolated from the seeds of Maclura pomifera (MPA) recognizes a mucin-type disaccharide sequence, Galβ1→3GalNAc (T) on a human erythrocyte membrane. We have utilized the enzyme-linked lectinosorbent assay (ELLSA) and inhibition assay to more systematically analyze the carbohydrate specificity of MPA with glyco-recognition factors and mammalian Gal/GalNAc structural units in lectin-glycoform interactions. From the results, it is concluded that the high densities of polyvalent GalNAcα1→Ser/Thr (Tn) and Galβ1→3GalNAcα1→Ser/Thr (Tα) glycotopes in macromolecules are the most critical factors for MPA binding, being on a nanogram basis 2.0 × 105, 4.6 × 104 and 3.9 × 104 more active than monovalent Gal, monomeric T and Tn glycotope, respectively. Other carbohydrate structural units in mammalian glycoconjugates, such as human blood group Sd (a+) related disaccharide (GalNAcβ1→4Gal) and Pk/P1 active disaccharide (Galα1→4Gal) were inactive. These results demonstrate that the configurations of carbon-4 and carbon-2 are essential for MPA binding and establish the importance of affinity enhancement by high-density polyvalencies of Tn/T glycotopes in MPA-glycan interactions. The overall binding profile of MPA can be defined in decreasing order as high density of polyvalent Tn/Tα (M.W. > 4.0 × 104) >> Tn-containing glycopeptides (M.W. < 3.0 × 103) > monomeric T/Tn and P (GalNAcβ1→3Gal) > GalNAc > Gal >> Man, L Ara, DFuc and Glc (inactive). Our findings should aid in the selection of this lectin for elucidating functions of carbohydrate chains in life processes and for applications in the biomedical sciences.
AB - The agglutinin isolated from the seeds of Maclura pomifera (MPA) recognizes a mucin-type disaccharide sequence, Galβ1→3GalNAc (T) on a human erythrocyte membrane. We have utilized the enzyme-linked lectinosorbent assay (ELLSA) and inhibition assay to more systematically analyze the carbohydrate specificity of MPA with glyco-recognition factors and mammalian Gal/GalNAc structural units in lectin-glycoform interactions. From the results, it is concluded that the high densities of polyvalent GalNAcα1→Ser/Thr (Tn) and Galβ1→3GalNAcα1→Ser/Thr (Tα) glycotopes in macromolecules are the most critical factors for MPA binding, being on a nanogram basis 2.0 × 105, 4.6 × 104 and 3.9 × 104 more active than monovalent Gal, monomeric T and Tn glycotope, respectively. Other carbohydrate structural units in mammalian glycoconjugates, such as human blood group Sd (a+) related disaccharide (GalNAcβ1→4Gal) and Pk/P1 active disaccharide (Galα1→4Gal) were inactive. These results demonstrate that the configurations of carbon-4 and carbon-2 are essential for MPA binding and establish the importance of affinity enhancement by high-density polyvalencies of Tn/T glycotopes in MPA-glycan interactions. The overall binding profile of MPA can be defined in decreasing order as high density of polyvalent Tn/Tα (M.W. > 4.0 × 104) >> Tn-containing glycopeptides (M.W. < 3.0 × 103) > monomeric T/Tn and P (GalNAcβ1→3Gal) > GalNAc > Gal >> Man, L Ara, DFuc and Glc (inactive). Our findings should aid in the selection of this lectin for elucidating functions of carbohydrate chains in life processes and for applications in the biomedical sciences.
KW - Carbohydrate specificities
KW - Glycoprotein binding
KW - Lectins
KW - Maclura pomifera
KW - Multivalent effect
KW - Polyvalency
UR - http://www.scopus.com/inward/record.url?scp=17744387316&partnerID=8YFLogxK
U2 - 10.1007/s11373-004-8178-4
DO - 10.1007/s11373-004-8178-4
M3 - 文章
C2 - 15864746
AN - SCOPUS:17744387316
SN - 1021-7770
VL - 12
SP - 135
EP - 152
JO - Journal of Biomedical Science
JF - Journal of Biomedical Science
IS - 1
ER -
