Open AccessEpitope Recognition of a Monoclonal Antibody Raised against a Synthetic Glycerol Phosphate Based Teichoic Acid
Author(s) -
Francesca Berni,
Ermioni Kalfopoulou,
Ana M Gimeno Cardells,
Filippo Carboni,
Daan van der Es,
Felipe Romero-Saavedra,
Diana Laverde,
Karmela Miklić,
Suzana Malić,
Tihana Lenac Roviš,
Stipan Jonjić,
Sara Ali,
Herman S. Overkleeft,
Cornelis H. Hokke,
Angela van Diepen,
Roberto Adamo,
Jesús JiménezBarbero,
Gijsbert A. van der Marel,
Johannes Hüebner,
Jeroen D. C. Codée
Publication year - 2021
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/acschembio.1c00422
Subject(s) - teichoic acid , epitope , monoclonal antibody , immunogenicity , biochemistry , chemistry , chirality (physics) , antibody , biology , cell wall , peptidoglycan , genetics , nambu–jona lasinio model , chiral symmetry breaking , physics , quantum mechanics , quark
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.