Interaction of Diocleinae lectins with glycoproteins based in surface plasmon resonance.
Interaction of glucose/mannose-binding lectins in solution with immobilized glycoproteins was followed in real time using surface plasmon resonance technology. The lectins which share many biochemical and structural features could be clearly differentiated in terms of their specificity for complex glycoconjugates. The most prominent interaction of the lectins with PHA-E comparing with soybean agglutinin, both glycoproteins exhibiting high mannose oligosaccharides, suggests that the whole structure of the glycoproteins themselves, may interfere in affinity. These findings also support the hypothesis that minor amino acid replacements in the primary sequence of the lectins might be responsible for their divergence in fine specificity and biological activities. This is the first report using surface plasmon resonance technology that evidences differences of Diocleinae lectins in respect their fine glycan-specificity.
Ramos
Marcio V
MV
Departamento de Biologia, Universidade Federal do Ceará, Fortaleza, CE, 60451-970, Brasil.
Cavada
Benildo S
BS
Mazard
Anne-Marie
AM
Rougé
Pierre
P
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D004347:Drug Interactions; D007887:Fabaceae; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D020349:Surface Plasmon Resonance
D006023:Glycoproteins; D037121:Plant Lectins