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Legume lectins interact with muramic acid and N ‐acetylmuramic acid
Author(s) -
Ayouba Ahidjo,
Chatelain Christian,
Rougé Pierre
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80918-s
Subject(s) - muramic acid , biochemistry , sialic acid , monosaccharide , glycan , lectin , chemistry , muramyl dipeptide , biology , peptidoglycan , glycoprotein , microbiology and biotechnology , cell wall , in vitro
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 or which cell walls contain peptidoglycans with high amounts of MurNAc.