Stabilization of peptide guinea pig myelin basic protein 72-85 by N-terminal acetylation - implications for immunological studies

Dehaan, E., Wauben, M., Wagenaarhilbers, J., Grosfeldstulemeyer, M., Rijkers, D., Moret, E. and Liskamp, R.M.J. (2004) Stabilization of peptide guinea pig myelin basic protein 72-85 by N-terminal acetylation - implications for immunological studies. Molecular Immunology, 40(13), pp. 943-948. (doi:10.1016/j.molimm.2003.10.015)

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Publisher's URL: http://dx.doi.org/10.1016/j.molimm.2003.10.015

Abstract

Peptide gpMBP72–85, containing amino acids 72–85 of guinea pig myelin basic protein is commonly used to induce experimental autoimmune encephalomyelitis in Lewis rats. The N-terminal glutamine in this peptide can cyclize to pyroglutamic acid, leading to loss of the first MHC anchor for binding to MHC class II. Acetylation of the peptide N-terminus prevents pyroglutamic acid formation and ensures a constant quality. An increased MHC binding affinity after N-terminal acetylation was observed. This modification also enhanced T cell proliferation of a gpMBP reactive T cell clone. The encephalitogenicity of peptide gpMBP72–85 was unaffected by acetylation. It is concluded that acetylation improves the chemical stability of gpMBP72–85, and is not detrimental but rather favorable for its biochemical and immunological, in vitro, and in vivo behavior.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Dehaan, E., Wauben, M., Wagenaarhilbers, J., Grosfeldstulemeyer, M., Rijkers, D., Moret, E., and Liskamp, R.M.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Molecular Immunology
ISSN:0161-5890
ISSN (Online):1872-9142

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