Legume lectins interact with muramic acid and N-acetylmuramic acid.
The inhibitory potency of both muramic acid (MurAc) and N-acetylmuramic acid (MurNAc) on various legume lectins, including Glc/Man- and Gal/GalNAc-specific lectins, was investigated by a haemagglutination inhibition technique. Data indicated that many lectins, especially those specific for Glc/Man, specifically interact with MurAc and MurNAc often to a greater extent than with other monosaccharides and their derivatives, such as N-acetylglucosamine (GlcNAc) and sialic acid. Glc/Man-specific lectins were also shown to interact with the muramyl-dipeptide MurNAc-D-Ala-D-isoGln. These interactions could explain why various lectins readily agglutinate some bacterial strains of which cell walls contain peptidoglycans with high amounts of MurNAc.
Ayouba
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A
Laboratoire de Biologie Cellulaire, Faculté des Sciences Pharmaceutiques, Université Paul Sabatier, Toulouse, France.
Chatelain
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C
Rougé
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P
D002240:Carbohydrate Sequence; D007887:Fabaceae / Q000378:metabolism*; D006385:Hemagglutination Inhibition Tests; D037102:Lectins / Q000037:antagonists & inhibitors*; D008969:Molecular Sequence Data; D009112:Muramic Acids / Q000378:metabolism*; D037121:Plant Lectins; D010946:Plants, Medicinal; D013379:Substrate Specificity
D037102:Lectins; D009112:Muramic Acids; D037121:Plant Lectins; C031651:N-acetylmuramic acid