FEMS Microbiology Letters · 1992 · 11 citations · 11 references
Life SciencesBiochemistryMicrobiologyGlycobiologyPlant BiochemistryPlant-microbe InteractionsCarbohydrate RecognitionGlycan RecognitionGlycan StructureGlycan-protein InteractionsPathogen RecognitionPlant Cell Wall PolysaccharidesLectin Binding SpecificityLectin InteractionsLectin RecognitionLectin-carbohydrate InteractionsLectin-carbohydrate RecognitionLectinsPlant LectinsSeed Lectins
Interaction of 24 different seed lectins/ isolectins from the Leguminosae with muramic acid (MurAc), N-acetylmuramic acid (MurNAc) and muramyl-dipeptides (MDP), was studied by hapten-inhibition of haemagglutination. Although many lectins were shown to interact, irrespective of their monosaccharide-specificity or systematic position, glucose/mannose-specific lectins from the tribe Vicieae exhibited the best affinity for these components of the bacterial cell wall. The discrepancies observed in the binding of the muramyl-dipeptide diastereo-isomers to lectins suggest that the binding is somewhat conformation-dependent. These interactions could be possibly involved in the recognition of bacteria by plants.
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