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Major histocompatibility complex class I binding glycopeptides for the estimation of 'empty' class I molecules

Abdel-Motal, Ussama M. ; Berg, Louise ; Bengtsson, Marita ; Dahmén, Jan ; Kihlberg, Jan ; Magnusson, Göran LU ; Nilsson, Ulf LU and Jondal, Mikael (1995) In Journal of Immunological Methods 188(1). p.21-31
Abstract

Different forms of major histocompatibility complex (MHC) class I heavy chains are known to be expressed on the cell surface, including molecules which are functionally 'empty'. Direct peptide binding to cells is obvious during sensitization of target cells in vitro for cytotoxic T lymphocyte killing and 'empty' MHC-I molecules are comparatively abundant on TAP- 1 2 peptide transporter mutant cells. In the present work we have estimated the fraction of 'empty' MHC class I molecules using glycosylated peptides and cellular staining with carbohydrate specific monoclonal antibodies. Synthetic Db and Kb binding peptides were coupled at different positions with different di- or trisaccharides, using different spacing... (More)

Different forms of major histocompatibility complex (MHC) class I heavy chains are known to be expressed on the cell surface, including molecules which are functionally 'empty'. Direct peptide binding to cells is obvious during sensitization of target cells in vitro for cytotoxic T lymphocyte killing and 'empty' MHC-I molecules are comparatively abundant on TAP- 1 2 peptide transporter mutant cells. In the present work we have estimated the fraction of 'empty' MHC class I molecules using glycosylated peptides and cellular staining with carbohydrate specific monoclonal antibodies. Synthetic Db and Kb binding peptides were coupled at different positions with different di- or trisaccharides, using different spacing between the carbohydrate and the peptide backbone. Binding of sugar specific mAbs was compared in ELISA and cellular assays. An optimal Db binding glycopeptide was used for comparative staining with anti-Db and anti-carbohydrate monoclonal antibodies to estimate fractions of 'empty' molecules on different T lymphoid cells. On activated normal T cells, a large fraction of Db molecules were found to be 'empty'. The functional cole of such 'empty' MHC class I molecules on T cells is presently unclear. However, on antigen presenting cells they might participate in the antigen presentation process.

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author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Binding, Glycopeptide, Major histocompatibility complex class I
in
Journal of Immunological Methods
volume
188
issue
1
pages
11 pages
publisher
Elsevier
external identifiers
  • scopus:0029622437
  • pmid:8551035
ISSN
0022-1759
DOI
10.1016/0022-1759(96)82888-2
language
English
LU publication?
yes
id
40b9b2ce-7165-4526-99f0-e497c1c5089c
date added to LUP
2023-02-07 09:45:13
date last changed
2025-01-11 21:19:25
@article{40b9b2ce-7165-4526-99f0-e497c1c5089c,
  abstract     = {{<p>Different forms of major histocompatibility complex (MHC) class I heavy chains are known to be expressed on the cell surface, including molecules which are functionally 'empty'. Direct peptide binding to cells is obvious during sensitization of target cells in vitro for cytotoxic T lymphocyte killing and 'empty' MHC-I molecules are comparatively abundant on TAP- 1 2 peptide transporter mutant cells. In the present work we have estimated the fraction of 'empty' MHC class I molecules using glycosylated peptides and cellular staining with carbohydrate specific monoclonal antibodies. Synthetic D<sup>b</sup> and K<sup>b</sup> binding peptides were coupled at different positions with different di- or trisaccharides, using different spacing between the carbohydrate and the peptide backbone. Binding of sugar specific mAbs was compared in ELISA and cellular assays. An optimal D<sup>b</sup> binding glycopeptide was used for comparative staining with anti-D<sup>b</sup> and anti-carbohydrate monoclonal antibodies to estimate fractions of 'empty' molecules on different T lymphoid cells. On activated normal T cells, a large fraction of D<sup>b</sup> molecules were found to be 'empty'. The functional cole of such 'empty' MHC class I molecules on T cells is presently unclear. However, on antigen presenting cells they might participate in the antigen presentation process.</p>}},
  author       = {{Abdel-Motal, Ussama M. and Berg, Louise and Bengtsson, Marita and Dahmén, Jan and Kihlberg, Jan and Magnusson, Göran and Nilsson, Ulf and Jondal, Mikael}},
  issn         = {{0022-1759}},
  keywords     = {{Binding; Glycopeptide; Major histocompatibility complex class I}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{1}},
  pages        = {{21--31}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Immunological Methods}},
  title        = {{Major histocompatibility complex class I binding glycopeptides for the estimation of 'empty' class I molecules}},
  url          = {{http://dx.doi.org/10.1016/0022-1759(96)82888-2}},
  doi          = {{10.1016/0022-1759(96)82888-2}},
  volume       = {{188}},
  year         = {{1995}},
}