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

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.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

de Haan EC,Wauben MH,Wagenaar-Hilbers JP,Grosfeld-Stulemeyer MC,Rijkers DT,Moret EE,Liskamp RM

doi

10.1016/j.molimm.2003.10.015

subject

Has Abstract

pub_date

2004-02-01 00:00:00

pages

943-8

issue

13

eissn

0161-5890

issn

1872-9142

pii

S0161589003003274

journal_volume

40

pub_type

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