Mucin-lectin interactions assessed by flow cytometry

作者：Jeffers Faye; Fuell Christine; Tailford Louise E; MacKenzie Donald A; Bongaerts Roy J^*; Juge Nathalie

来源：Carbohydrate Research, 2010, 345(10): 1486-1491.

DOI：10.1016/j.carres.2010.05.012

• Flow cytometry
• Mucin
• Lectin
• Protein-carbohydrate interaction

The O-glycosylated domains of mucins and mucin-type glycoproteins contain 50-80% of carbohydrate and possess expanded conformations. Herein, we describe a flow cytometry (FCM) method for determining the carbohydrate-binding specificities of lectins to mucin. Biotinylated mucin was immobilized on streptavidin-coated beads, and the binding specificities of the major mucin sugar chains, as determined by GC-MS and MALDI-ToF, were monitored using fluorescein-labeled lectins. The specificities of lectins toward specific biotinylated glycans were determined as controls. The advantage of flexibility, multiparametric data acquisition, speed, sensitivity, and high-throughput capability makes flow cytometry a valuable tool to study diverse interactions between glycans and proteins.

• 出版日期2010-7-2