A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer.
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.
Liu
Jiwei
J
College of Life Sciences, Sichuan University, Chengdu, PR China.
Xu
Xiaochao
X
Liu
Jinzhi
J
Balzarini
Jan
J
Luo
Yongtin
Y
Kong
Yang
Y
Li
Jian
J
Chen
Fang
F
Van Damme
Els
E
Bao
Jinku
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D002241:Carbohydrates / Q000032:analysis; D017124:Conserved Sequence; D017931:DNA Primers; D018744:DNA, Plant / Q000235:genetics; D031426:Lycoris / Q000737:chemistry* / Q000235:genetics*; D008358:Mannose; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry; D037121:Plant Lectins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D016415:Sequence Alignment
D002241:Carbohydrates; D017931:DNA Primers; D018744:DNA, Plant; D046912:Multiprotein Complexes; D037121:Plant Lectins; D008358:Mannose