Open AccessKinetic Analysis of Synthetic Analogues of Linear‐Epitope Peptides of Glycoprotein D of Herpes Simplex Virus Type 1 by Surface Plasmon Resonance
Author(s) -
Lasonder Edwin,
Schellekens Gerard A.,
Koedijk Danny G. A. M.,
Damhof Ria A.,
WellingWester Sytske,
Feijlbrief Matty,
Scheffer Albert J.,
Welling Gjalt W.
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.0209h.x
Subject(s) - epitope , peptide , surface plasmon resonance , chemistry , mimotope , epitope mapping , residue (chemistry) , monoclonal antibody , amino acid , receptor–ligand kinetics , linear epitope , glycoprotein , peptide sequence , stereochemistry , phage display , biochemistry , antibody , biology , materials science , nanoparticle , receptor , gene , immunology , nanotechnology
The interaction between mAb A16 and glycoprotein D (gD) of herpes simplex virus type 1 was analyzed by studying the kinetics of binding with a surface‐plasmon‐resonance biosensor. mAb A16 belongs to group VII antibodies, which recognize residues 11–19 of gD. In a previous study, three critical residues, Asp13, Arg16 and Phe17, of this epitope were identified by screening a phage display library that contained a random 15‐amino‐acid insert with the antibody. The contribution to binding of these residues in the motif DXXRF was further analyzed by an amino‐acid‐replacement study of the epitope gD‐(9–19)‐peptide and of a gD‐(9–19)‐peptide mimotope, previously obtained by screening the phage display library. Amino acid residues of the motif were replaced by a neutral amino acid residue, an amino acid residue with opposite charge and a corresponding D‐amino acid residue. Kinetic parameters of peptide analogues were determined with a surface plasmon‐resonance biosensor. The kinetic parameters of the peptide analogues were compared with the kinetic parameters of the interaction between mAb A16 and the epitope gD‐(9–19)‐peptide. The minimal size of the gD epitope for mAb A16 was also determined in this study. The kinetic constants of the resulting gD‐(11–17)‐peptide were found to be similar to those of entire gD. The kinetic analysis precisely defined the epitope on gD for mAb A16 to residues 11–17, identified Argl6 as an essential residue and suggested that Asp 13 and Phe17 are mainly involved in stabilization of the secondary structure of the peptide.