Premium
The fine sugar specificity of the Lathyrus ochrus seed lectin and isolectins
Author(s) -
Debray Henri,
Rougé Pierre
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80924-2
Subject(s) - lectin , glycopeptide , glycan , biochemistry , fucose , cd69 , residue (chemistry) , glycoprotein , chemistry , mannose , ficolin , biology , mannan binding lectin , in vitro , cytotoxic t cell , il 2 receptor , antibiotics
Glycoproteins and their derived glycopeptides have been used to define the specificity of the Lathyrus ochrus lectin and isolectins, by determining their ability to inhibit the agglutination of human erythrocytes induced by the lectin or isolectins. This α‐D‐mannose/α‐D‐glucose‐specific lectin possessess the ability to recognize a well‐defined saccharide sequence on a bi‐antennary N ‐acetyllactosamine‐type glycan. For other Vicieae lectins, the best inhibitor is a glycopeptide from human lactotransferrin with an α‐L‐fucose residue at the C‐6 position on the N ‐acetylglucosamine residue involved in the N ‐glycosylamine bond. This fucose seems to be a major determinant of the binding since its removal with an α‐L‐fucosidase gives glycopeptides 8‐fold less inhibitory. Our results confirm that the Vicieae lectins are evolutionarily related proteins even at the level of their binding sites.