Establishment of a quantitative ELISA capable of determining peptide - MHC class I interaction.
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Establishment of a quantitative ELISA capable of determining peptide - MHC class I interaction. / Sylvester-Hvid, C; Kristensen, N; Blicher, T; Ferré, H; Lauemøller, S L; Wolf, X A; Lamberth, K; Nissen, Mogens Holst; Pedersen, L Ø; Buus, S.
I: HLA, Bind 59, Nr. 4, 2002, s. 251-8.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Establishment of a quantitative ELISA capable of determining peptide - MHC class I interaction.
AU - Sylvester-Hvid, C
AU - Kristensen, N
AU - Blicher, T
AU - Ferré, H
AU - Lauemøller, S L
AU - Wolf, X A
AU - Lamberth, K
AU - Nissen, Mogens Holst
AU - Pedersen, L Ø
AU - Buus, S
N1 - Keywords: Buffers; Enzyme-Linked Immunosorbent Assay; Histocompatibility Antigens Class I; Humans; Peptides; Protein Binding; Protein Renaturation; Sensitivity and Specificity; beta 2-Microglobulin
PY - 2002
Y1 - 2002
N2 - Many different assays for measuring peptide-MHC interactions have been suggested over the years. Yet, there is no generally accepted standard method available. We have recently generated preoxidized recombinant MHC class I molecules (MHC-I) which can be purified to homogeneity under denaturing conditions (i.e., in the absence of any contaminating peptides). Such denatured MHC-I molecules are functional equivalents of "empty molecules". When diluted into aqueous buffer containing beta-2 microglobulin (beta2m) and the appropriate peptide, they fold rapidly and efficiently in an entirely peptide dependent manner. Here, we exploit the availability of these molecules to generate a quantitative ELISA-based assay capable of measuring the affinity of the interaction between peptide and MHC-I. This assay is simple and sensitive, and one can easily envisage that the necessary reagents, standards and protocols could be made generally available to the scientific community.
AB - Many different assays for measuring peptide-MHC interactions have been suggested over the years. Yet, there is no generally accepted standard method available. We have recently generated preoxidized recombinant MHC class I molecules (MHC-I) which can be purified to homogeneity under denaturing conditions (i.e., in the absence of any contaminating peptides). Such denatured MHC-I molecules are functional equivalents of "empty molecules". When diluted into aqueous buffer containing beta-2 microglobulin (beta2m) and the appropriate peptide, they fold rapidly and efficiently in an entirely peptide dependent manner. Here, we exploit the availability of these molecules to generate a quantitative ELISA-based assay capable of measuring the affinity of the interaction between peptide and MHC-I. This assay is simple and sensitive, and one can easily envisage that the necessary reagents, standards and protocols could be made generally available to the scientific community.
M3 - Journal article
C2 - 12135423
VL - 59
SP - 251
EP - 258
JO - HLA
JF - HLA
SN - 2059-2302
IS - 4
ER -
ID: 8746165