| Autor: |
de Haan EC; Department of Medicinal Chemistry, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, P.O. Box 80082, 3508 TB, Utrecht, The Netherlands., Wauben MH, Wagenaar-Hilbers JP, Grosfeld-Stulemeyer MC, Rijkers DT, Moret EE, Liskamp RM |
| Jazyk: |
angličtina |
| Zdroj: |
Molecular immunology [Mol Immunol] 2004 Feb; Vol. 40 (13), pp. 943-8. |
| DOI: |
10.1016/j.molimm.2003.10.015 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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