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

Ussama M. Abdel-Motal, Louise Berg, Marita Bengtsson, Jan Dahmén, Jan Kihlberg, Göran Magnusson, Ulf Nilsson, Mikael Jondal

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)21-31
Number of pages11
JournalJournal of Immunological Methods
Volume188
Issue number1
DOIs
Publication statusPublished - 15 Dec 1995
Externally publishedYes

Fingerprint

Glycopeptides
Major Histocompatibility Complex
Peptides
Carbohydrates
Monoclonal Antibodies
Staining and Labeling
T-Lymphocytes
Trisaccharides
Disaccharides
Antigen Presentation
Cytotoxic T-Lymphocytes
Antigen-Presenting Cells
Enzyme-Linked Immunosorbent Assay
Lymphocytes

Keywords

  • Binding
  • Glycopeptide
  • Major histocompatibility complex class I

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

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; Nilsson, Ulf; Jondal, Mikael.

In: Journal of Immunological Methods, Vol. 188, No. 1, 15.12.1995, p. 21-31.

Research output: Contribution to journalArticle

Abdel-Motal, Ussama M. ; Berg, Louise ; Bengtsson, Marita ; Dahmén, Jan ; Kihlberg, Jan ; Magnusson, Göran ; Nilsson, Ulf ; Jondal, Mikael. / Major histocompatibility complex class I binding glycopeptides for the estimation of 'empty' class I molecules. In: Journal of Immunological Methods. 1995 ; Vol. 188, No. 1. pp. 21-31.
@article{2690ceef57214034b1f22ecf28b5652a,
title = "Major histocompatibility complex class I binding glycopeptides for the estimation of 'empty' class I molecules",
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 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.",
keywords = "Binding, Glycopeptide, Major histocompatibility complex class I",
author = "Abdel-Motal, {Ussama M.} and Louise Berg and Marita Bengtsson and Jan Dahm{\'e}n and Jan Kihlberg and G{\"o}ran Magnusson and Ulf Nilsson and Mikael Jondal",
year = "1995",
month = "12",
day = "15",
doi = "10.1016/0022-1759(96)82888-2",
language = "English",
volume = "188",
pages = "21--31",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Major histocompatibility complex class I binding glycopeptides for the estimation of 'empty' class I molecules

AU - Abdel-Motal, Ussama M.

AU - Berg, Louise

AU - Bengtsson, Marita

AU - Dahmén, Jan

AU - Kihlberg, Jan

AU - Magnusson, Göran

AU - Nilsson, Ulf

AU - Jondal, Mikael

PY - 1995/12/15

Y1 - 1995/12/15

N2 - 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.

AB - 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.

KW - Binding

KW - Glycopeptide

KW - Major histocompatibility complex class I

UR - http://www.scopus.com/inward/record.url?scp=0029622437&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029622437&partnerID=8YFLogxK

U2 - 10.1016/0022-1759(96)82888-2

DO - 10.1016/0022-1759(96)82888-2

M3 - Article

C2 - 8551035

AN - SCOPUS:0029622437

VL - 188

SP - 21

EP - 31

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

SN - 0022-1759

IS - 1

ER -