A quantitative assay to measure the interaction between immunogenic peptides and purified class I major histocompatibility complex molecules

A C Olsen; L O Pedersen; A S Hansen; S Buus; Mogens Holst Nissen; M Olsen; P R Hansen; A Holm

doi:10.1002/eji.1830240218

A quantitative assay to measure the interaction between immunogenic peptides and purified class I major histocompatibility complex molecules

A C Olsen, L O Pedersen, A S Hansen, S Buus, Mogens Holst Nissen, M Olsen, P R Hansen, A Holm

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

57 Citationer (Scopus)

Abstract

Udgivelsesdato: 1994-Feb

Originalsprog	Engelsk
Tidsskrift	European Journal of Immunology
Vol/bind	24
Udgave nummer	2
Sider (fra-til)	385-92
Antal sider	7
ISSN	0014-2980
DOI	https://doi.org/10.1002/eji.1830240218
Status	Udgivet - 1994

Adgang til dokumentet

10.1002/eji.1830240218

Citationsformater

A quantitative assay to measure the interaction between immunogenic peptides and purified class I major histocompatibility complex molecules. / Olsen, A C; Pedersen, L O; Hansen, A S; Buus, S ; Nissen, Mogens Holst; Olsen, M; Hansen, P R; Holm, A.

I: European Journal of Immunology, Bind 24, Nr. 2, 1994, s. 385-92.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

@article{efca3d90ba3311ddae57000ea68e967b,

title = "A quantitative assay to measure the interaction between immunogenic peptides and purified class I major histocompatibility complex molecules",

abstract = "A direct and sensitive biochemical assay to measure the interaction in solution between peptides and affinity-purified major histocompatibility complex (MHC) class I molecules has been generated. Specific binding reflecting the known class I restriction of cytotoxic T cell responses was obtained. Adding an excess of beta 2-microglobulin (beta 2m) significantly increased the rate of peptide association, but it did not affect the rate of dissociation. Binding was complicated by a rapid and apparently irreversible loss of functional MHC class I at 37 degrees C which might limit the life span of empty MHC class I thereby preventing the inadvertent exchange of peptides at the target cell surface. All class I molecules tested bound peptides of the canonical octa- to nona-meric length. However, one class I molecule, Kk, also bound peptides, which were much longer suggesting that the preference of class I molecules for short epitopes is not absolute and may be caused by factors other than the peptide-MHC class I binding event itself.",

author = "Olsen, {A C} and Pedersen, {L O} and Hansen, {A S} and S Buus and Nissen, {Mogens Holst} and M Olsen and Hansen, {P R} and A Holm",

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pages = "385--92",

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T1 - A quantitative assay to measure the interaction between immunogenic peptides and purified class I major histocompatibility complex molecules

AU - Olsen, A C

AU - Pedersen, L O

AU - Hansen, A S

AU - Buus, S

AU - Nissen, Mogens Holst

AU - Olsen, M

AU - Hansen, P R

AU - Holm, A

PY - 1994

Y1 - 1994

N2 - A direct and sensitive biochemical assay to measure the interaction in solution between peptides and affinity-purified major histocompatibility complex (MHC) class I molecules has been generated. Specific binding reflecting the known class I restriction of cytotoxic T cell responses was obtained. Adding an excess of beta 2-microglobulin (beta 2m) significantly increased the rate of peptide association, but it did not affect the rate of dissociation. Binding was complicated by a rapid and apparently irreversible loss of functional MHC class I at 37 degrees C which might limit the life span of empty MHC class I thereby preventing the inadvertent exchange of peptides at the target cell surface. All class I molecules tested bound peptides of the canonical octa- to nona-meric length. However, one class I molecule, Kk, also bound peptides, which were much longer suggesting that the preference of class I molecules for short epitopes is not absolute and may be caused by factors other than the peptide-MHC class I binding event itself.

AB - A direct and sensitive biochemical assay to measure the interaction in solution between peptides and affinity-purified major histocompatibility complex (MHC) class I molecules has been generated. Specific binding reflecting the known class I restriction of cytotoxic T cell responses was obtained. Adding an excess of beta 2-microglobulin (beta 2m) significantly increased the rate of peptide association, but it did not affect the rate of dissociation. Binding was complicated by a rapid and apparently irreversible loss of functional MHC class I at 37 degrees C which might limit the life span of empty MHC class I thereby preventing the inadvertent exchange of peptides at the target cell surface. All class I molecules tested bound peptides of the canonical octa- to nona-meric length. However, one class I molecule, Kk, also bound peptides, which were much longer suggesting that the preference of class I molecules for short epitopes is not absolute and may be caused by factors other than the peptide-MHC class I binding event itself.

U2 - 10.1002/eji.1830240218

DO - 10.1002/eji.1830240218

M3 - Journal article

C2 - 8299688

VL - 24

SP - 385

EP - 392

JO - European Journal of Immunology

JF - European Journal of Immunology

SN - 0014-2980

IS - 2

ER -