Glycerol phosphate
(GroP)-based teichoic acids (TAs) are antigenic
cell-wall components found in both enterococcus and staphylococcus
species. Their immunogenicity has been explored using both native
and synthetic structures, but no details have yet been reported on
the structural basis of their interaction with antibodies. This work
represents the first case study in which a monoclonal antibody, generated
against a synthetic TA, was developed and employed for molecular-level
binding analysis using TA microarrays, ELISA, SPR-analyses, and STD-NMR
spectroscopy. Our findings show that the number and the chirality
of the GroP residues are crucial for interaction and that the sugar
appendage contributes to the presentation of the backbone to the binding
site of the antibody.
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