Title: A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer
Authors: Liu, Jiwei ×
Xu, Xiaochao
Liu, Jinzhi
Balzarini, Jan
Luo, Yongtin
Kong, Yang
Li, Jian
Chen, Fang
Van Damme, Els
Bao, Jinku #
Issue Date: 4-Mar-2007
Publisher: Panstwowe Wydawnictwo Naukowe
Series Title: Acta Biochimica Polonica vol:54 issue:1 pages:159-166
Abstract: The mannose-binding agglutinin from bulbs of Lycoris aurea (LAA) agglutinates rabbit but not human erythrocytes. The molecular mass of the monomer in SDS/PAGE is 12 kDa while the apparent molecular mass in gel filtration is 48 kDa, indicating that LAA is a homotetramer. The full-length cDNA of LAA contains 683 bp with an open reading frame encoding a protomer of 162 amino-acid residues. Hydrophobic Cluster Analysis and molecular modeling of the 109-residue mature polypeptide suggested a similar secondary and tertiary structure to those of Narcissus pseudonarcissus agglutinin (NPA). Molecular docking revealed that, besides the three mannose-binding sites common among Amaryllidaceae lectins, LAA also contains a fourth unique mannose-binding site formed by a tryptophan cluster. The existence of four mannose-binding sites in each monomer of LAA is very unusual and has only been reported for NPA earlier.
ISSN: 0001-527X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Virology and Chemotherapy (Rega Institute)
Faculty of Bioscience Engineering
× corresponding author
# (joint) last author

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