Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts.
Concanavalin A, the lectin from Canavalia ensiformis, develops arginase activity depending on Mn(2+). The cation cannot be substituted by Ca(2+) which, in addition, inhibits Mn(2+)-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from Evernia prunastri and Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease.
Fontaniella
Blanca
B
Department of Plant Physiology, Faculty of Biology, José Antonio Novais st. s/n, Complutense University, 28040 Madrid, Spain.
Millanes
Ana-María
AM
Vicente
Carlos
C
Legaz
María-Estrella
ME
D002473:Cell Wall / Q000378:metabolism*; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008011:Lichens / Q000378:metabolism*; D008024:Ligands; D008358:Mannose / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding
D008024:Ligands; D010940:Plant Proteins; D003208:Concanavalin A; D008358:Mannose