Specificity of syn. lectin for -glycopeptides

Amaranthus leucocarpus lectin recognizes a moesin‐like O‐glycoprotein and costimulates murine CD3‐activated CD4+ T cells

“…This protein sequence was also analyzed by NetOGlyc 4.0 software 27 showing nine potential sites for O-glycosylation, of which four of them exhibited a very high probability of being recognized by ALL . Previous studies have shown that the binding site of ALL interacts with inner core of the Thomsen–Friedenreich antigen, and that ALL binds GalNAc residues, which are separated by four amino acids, whereas GalNAc residue clusters prevent recognition by ALL 33. Another analysis on protein sequence was performed using Phyre 2 26 that showed 90% identity with the FERM domain of moesin.…”

The Amaranthus leucocarpus Lectin Enhances the Anti-CD3 Antibody-Mediated Activation of Human Peripheral Blood CD4+ T Cells

“…Many studies have shown that lectins can recognize subtle glycosylation modifications and these observations may explain how lectins bind to distinct molecules, thereby eliciting different functions (Nakamura-Tsuruta et al 2008). In this regard, Hernandez et al (2004) reported that the affinity of ALL for glycans was determined by the spatial conformation of saccharides present in the protein backbone, suggesting that ALL expressed allosteric restrictions that may have allowed it to recognize different ligand domains.…”

“…Moreover, some lectins can activate T cells by cross-linking T cell surface r e c e p t o r s i n a c a r b o h y d r a t e -d e p e n d e n t m a n n e r (Shanmugham et al 2006;Kesherwani and Sodhi 2007). Our laboratory isolated a lectin from Amaranthus leucocarpus seeds (ALL) that is specific for structures containing the galactose-N-acetylgalactosamine and N-acetylgalactosamine saccharides found in glycoproteins (Zenteno et al 1992;Hernandez et al 2004). ALL recognizes human and murine peripheral CD4 + T cells and ALL recognition increased three-fold on activated CD4 + T cells harvested from mouse lymph nodes (Lascurain et al 1994;Ortiz et al 2002).…”

Expression of antigen tf and galectin-3 in fibroadenoma

“…This ability could be explained by the variability in the size of the carbohydrate-recognition domain (CDR) and the variability in quaternary association [25]. Interestingly, the CDR of A. leucocarpus lectin recognizes GalNAc residues when they are spaced out in glycan structures, whereas GalNAc residues arranged in clusters prevent interaction with the lectin [26]. These glycans have been related with cervical cancer development [27] and are present in fibroadenomas [28], whereas Artocarpus integrifolia lectin can recognize clusters of TF antigen.…”