Abstract
Multiple peptide synthesis gives access to a set of reagents that permit thorough answers to such questions as: Where are all the linear epitopes in this protein? How long is the critical part of each epitope? Which epitopes are commonly recognized and which are rarely recognized? What are the affinities for each epitope? Which amino acids in the epitope are in contact with the antibody/TCR/MHC molecule? What variants of the epitope are still recognized by the antibody/TCR/MHC molecule? Which peptides are antagonistic peptides for this epitope?
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Geysen, H. M., Meloen, R. H., and Barteling, S. J. (1984) Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc. Natl. Acad. Sci. USA 81, 3998–4002.
Smith, J. A., Hurrell, J. G. R., and Leach, S. J. (1977) A novel method for delineating antigenic determinants: peptide synthesis and radioimmunoassay using the same solid support. Immunochemistry 14, 565–568.
Geysen, H. M., Rodda, S. J., Mason, T. J., Tribbick, G., and Schoofs, P. G (1987) Strategies for epitope analysis using peptide synthesis. J. Immunol. Methods 102, 259–274.
Maeji, N. J., Bray, A. M., and Geysen, H. M. (1990) Multi-pin peptide synthesis strategy for T cell determinant analysis. J. Immunol. Methods 134, 23–33.
Maeji, N. J., Valerio, R. M., Bray, A. M., Campbell, R. A., and Geysen, H. M. (1994) Grafted supports used with the multipin method of peptide synthesis. Reactive Polymers 22, 203–212.
Valerio, R. M., Bray, A. M., Campbell, R. A., Dipasquale, A., Margellis, C., Rodda, S. J., Geysen, H. M., and Maeji, N. J. (1993) Multipin peptide synthesis at the micromole scale using 2-hydroxyethyl methacrylate grafted polyethylene supports. Int. J. Pept. Protein Res. 42, 1–9.
Bray, A. M., Maeji, N. J., Jhingran, A. G., and Valerio, R. M. (1991) Gas phase cleavage of peptides from a solid support with ammonia vapour. Application in simultaneous multiple peptide synthesis. Tetrahedron Lett. 32, 6163–6166.
Maeji, N. J., Bray, A. M., Valerio, R. M., and Wang, W. (1995) Larger scale multipin peptide synthesis. Pept. Res. 8, 33–38.
Rodda, S. J., Geysen, H. M., Mason, T. J., and Schoofs, P. G. (1986) The antibody response to myoglobin-I. Systematic synthesis of myoglobin peptides reveals location and substructure of species dependent continuous antigenic determinants. Mol. Immunol. 23, 603–610.
Getzoff, E. D., Geysen, H. M., Rodda, S. J., Alexander, H., Tainer, J. A., and Lerner, R. A. (1987) Mechanisms of antibody binding to a protein. Science 235, 1191–1196.
Mutch, D. A., Rodda, S. J., Benstead, M., Valerio, R. M., and Geysen, H. M. (1991) Effects of end groups on the stimulatory capacity of minimal length T cell determinant peptides. Pept. Res. 4, 132–137.
Burrows, S. R., Gardner, J., Khanna, R., Steward, T., Moss, D. J., Rodda, S., and Suhrbier, A. (1994) Five new cytotoxic T cell epitopes identified within Epstein-Barr virus nuclear antigen 3. J. Gen. Virol. 75, 2489–2493.
Trifilieff, E., Dubs, M. C., and van Regenmortel, M. H. V. (1991) Antigenic cross-reactivity potential of synthetic peptides immobilized on polyethylene rods. Mol. Immunol. 28, 889–896.
Weiner, A. J., Geysen, H. M., Christopherson, C., Hall, J. E., Mason, T. J., Saracco, G., Bonino, F., Crawford, K., Marion, C. D., Crawford, K. A., Brunetto, M., Barr, P. J., Miyamura, T., McHutchinson, J., and Houghton, M. (1992) Evidence for immune selection of hepatitis C virus (HCV) putative envelope glycoprotein variants: potential role in chronic HCV infections. Proc. Natl. Acad. Sci. USA 89, 3468–3472.
Hunt, D. F., Henderson, R. A., Shabanowitz, J., Sakaguchi, K., Michel, H., Sevilir, N., Cox, A. L., Appella, E., and Engelhard, V. H. (1992) Characterization of peptides bound to the class I MHC molecule by mass spectrometry. Science 255, 1261–1266.
Rudensky, A. Y., Preston-Hurlburt, P., Al-Ramadi, B. K., Rothbard, J., and Janeway, C. A. (1992) Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs. Nature 359, 429–431.
Widmann, C., Maryanski, J. L., Romero, P., and Corradin, G. (1991) Differential stability of antigenic MHC class I-restricted synthetic peptides. J. Immunol. 147, 3745–3751.
Tribbick, G., Triantafyllou, B., Lauricella, R., Rodda, S. J., Mason, T. J., and Geysen, H. M. (1991) Systematic fractionation of serum antibodies using multiple antigen homologous peptides as affinity ligands. J. Immunol. Methods 139, 155–166.
van’t Hof, W., van Milligen, F. J., Driedijk, P. C., van den Berg, M., and Aalberse, R. C. (1993) How to demonstrate specificity of antibody binding to synthetic peptides? J. Immunol. Methods 161, 273–275.
Geysen, H. M., Mason, T. J., and Rodda S. J. (1988) Cognitive features of continuous antigenic determinants. J. Mol. Recognition 1, 32–41.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Humana Press Inc.
About this protocol
Cite this protocol
Rodda, S.J., Maeji, N.J., Tribbick, G. (1996). Epitope Mapping Using Multipin Peptide Synthesis. In: Morris, G.E. (eds) Epitope Mapping Protocols. Methods in Molecular Biology™, vol 66. Humana Press. https://doi.org/10.1385/0-89603-375-9:137
Download citation
DOI: https://doi.org/10.1385/0-89603-375-9:137
Publisher Name: Humana Press
Print ISBN: 978-0-89603-375-7
Online ISBN: 978-1-59259-552-5
eBook Packages: Springer Protocols