- Abstract:
-
This study extends our previous observation that glycopeptides bind to class I major histocompatibility complex (MHC) molecules and elicit carbohydrate-specific CTL responses. The Sendai virus nucleoprotein wild-type (WT) peptide (FAPGNYPAL) binds H-2Db using the P5-Asn as an anchor. The peptide K2 carrying a P5 serine substitution did not bind Db. Surprisingly, glycosylation of the serine (K2-O-GlcNAc) with N-acetylglucosamine (GlcNAc), a novel cytosolic O-linked glycosylation, partially res...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/eji.1830251211
-
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- Journal:
- European journal of immunology
- Volume:
- 25
- Issue:
- 12
- Pages:
- 3270-3276
- Publication date:
- 1995-12-05
- DOI:
- EISSN:
-
1521-4141
- ISSN:
-
0014-2980
- URN:
-
uuid:38efd787-b61b-41ad-958d-f202615d3fb6
- Source identifiers:
-
35896
- Local pid:
- pubs:35896
- Copyright date:
- 1995
Journal article
Peptide anchor residue glycosylation: effect on class I major histocompatibility complex binding and cytotoxic T lymphocyte recognition.
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