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L2/HNK‐1 carbohydrate and protein‐protein interactions mediate the homophilic binding of the neural adhesion molecule P0
Author(s) -
Griffith L. S.,
Schmitz B.,
Schachner M.
Publication year - 1992
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490330417
Subject(s) - epitope , glycoprotein , neural cell adhesion molecule , polyclonal antibodies , chemistry , immunoglobulin superfamily , myelin associated glycoprotein , microbiology and biotechnology , antibody , biochemistry , lectin , protein–protein interaction , plasma protein binding , receptor , cell adhesion , biology , myelin , central nervous system , neuroscience , cell , immunology
The neural adhesion molecule P0, the most abundant glycoprotein in peripheral myelin of mammals, is a member of the immunoglobulin superfamily and expresses the L2/HNK‐1 and L3 oligosaccharides at a single N‐glycosylation site. It acts in both homophilic and heterophilic binding mechanisms. To investigate the molecular requirements for homophilic interaction, we have used P0 from human sciatic nerve and the extracellular domain of P0 expressed in bacteria to determine binding of P0 to P0 in solid phase and bead aggregation assays. The binding of P0 to P0 could be partially inhibited in both assays by antibodies to the L2/HNK‐1 epitope and by the L2/HNK‐1 carbohydrate, but not by L3 antibodies or other carbohydrates. Inhibition of binding was also seen with polyclonal antibodies reacting with the protein backbone of P0. These observations indicate that both carbohydrate and protein structures are involved in the binding of P0 to P0 and that P0 acts as a presenter of and a receptor for a functionally important carbohydrate. © 1992 Wiley‐Liss, Inc.