Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold

Phytohemagglutinin from Phaseolus vulgaris (PHA-E), a legume lectin, has an unusual specificity toward biantennary galactosylated N-glycan with bisecting N-acetylglucosamine (GlcNAc). To investigate the interaction in detail, we have solved the crystal structures of PHA-E without ligand and in compl...

Full description

Saved in:
Bibliographic Details
Published in:Glycobiology (Oxford) 2014-04, Vol.24 (4), p.368-378
Main Authors: Nagae, Masamichi, Soga, Keisuke, Morita-Matsumoto, Kana, Hanashima, Shinya, Ikeda, Akemi, Yamamoto, Kazuo, Yamaguchi, Yoshiki
Format: Article
Language:English
Subjects:
Models, Molecular
Molecular Conformation
Phaseolus - chemistry
Phytohemagglutinins - chemistry
Phytohemagglutinins - genetics
Phytohemagglutinins - metabolism
Polysaccharides - chemistry
Polysaccharides - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Phytohemagglutinin from Phaseolus vulgaris (PHA-E), a legume lectin, has an unusual specificity toward biantennary galactosylated N-glycan with bisecting N-acetylglucosamine (GlcNAc). To investigate the interaction in detail, we have solved the crystal structures of PHA-E without ligand and in complex with biantennary N-glycan derivatives. PHA-E interacts with the trisaccharide unit (Galβ1-4GlcNAcβ1-2Man) in a manner completely different from that of mannose/glucose-specific legume lectins. The inner mannose residue binds to a novel site on the protein, and its rotation is opposite to that occurring in the monosaccharide-binding site of other lectins around the sugar O3 axis. Saturation-transfer difference NMR using biantennary di-galactosylated and bisected glycans reveals that PHA-E interacts with both antennas almost equally. The unique carbohydrate interaction explains the glycan-binding specificity and high affinity.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/cwu004