Irreversible association of peptides with class II MHC molecules in living cells

Antonio  Lanzavecchia; Pamela A.  Reid; Colin Watts

doi:10.1038/357249a0

Irreversible association of peptides with class II MHC molecules in living cells

Antonio Lanzavecchia
, Pamela A. Reid
, Colin Watts

University of Dundee

Research output: Contribution to journal › Article › peer-review

166 Citations (Scopus)

Abstract

FUNCTIONAL, morphological and biochemical evidence indicates that class II major istocompatibility complex (MHC) molecules associate with processed peptides during biosynthesis^1-9. Peptide/MHC complexes in living cells have been reported to be less stable than similar complexes generated in vitro, which has led to the suggestion that there may be a peptide exchange mechanism operating in vivo ^l0-12. Although this could increase the capacity for binding incoming antigens, it would reduce the efficacy of processed antigenic peptides by exchanging these for self peptides. Here we measure the half-life of peptide/class II complexes in human antigen-presenting cells and find that it is very similar to the half-life of class II molecules themselves, indicating that peptides are bound irreversibly under physiological conditions. Thus class II MHC retains long-term 'memory' of past encounters with antigen to maximize the opportunity for T cell/antigen-presenting cell interaction.

Original language	English
Pages (from-to)	249-252
Number of pages	4
Journal	Nature
Volume	357
Issue number	6375
DOIs	https://doi.org/10.1038/357249a0
Publication status	Published - 21 May 1992

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title = "Irreversible association of peptides with class II MHC molecules in living cells",

abstract = "FUNCTIONAL, morphological and biochemical evidence indicates that class II major istocompatibility complex (MHC) molecules associate with processed peptides during biosynthesis1-9. Peptide/MHC complexes in living cells have been reported to be less stable than similar complexes generated in vitro, which has led to the suggestion that there may be a peptide exchange mechanism operating in vivo l0-12. Although this could increase the capacity for binding incoming antigens, it would reduce the efficacy of processed antigenic peptides by exchanging these for self peptides. Here we measure the half-life of peptide/class II complexes in human antigen-presenting cells and find that it is very similar to the half-life of class II molecules themselves, indicating that peptides are bound irreversibly under physiological conditions. Thus class II MHC retains long-term 'memory' of past encounters with antigen to maximize the opportunity for T cell/antigen-presenting cell interaction.",

author = "Antonio Lanzavecchia and Reid, \{Pamela A.\} and Colin Watts",

year = "1992",

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T1 - Irreversible association of peptides with class II MHC molecules in living cells

AU - Lanzavecchia, Antonio

AU - Reid, Pamela A.

AU - Watts, Colin

PY - 1992/5/21

Y1 - 1992/5/21

N2 - FUNCTIONAL, morphological and biochemical evidence indicates that class II major istocompatibility complex (MHC) molecules associate with processed peptides during biosynthesis1-9. Peptide/MHC complexes in living cells have been reported to be less stable than similar complexes generated in vitro, which has led to the suggestion that there may be a peptide exchange mechanism operating in vivo l0-12. Although this could increase the capacity for binding incoming antigens, it would reduce the efficacy of processed antigenic peptides by exchanging these for self peptides. Here we measure the half-life of peptide/class II complexes in human antigen-presenting cells and find that it is very similar to the half-life of class II molecules themselves, indicating that peptides are bound irreversibly under physiological conditions. Thus class II MHC retains long-term 'memory' of past encounters with antigen to maximize the opportunity for T cell/antigen-presenting cell interaction.

AB - FUNCTIONAL, morphological and biochemical evidence indicates that class II major istocompatibility complex (MHC) molecules associate with processed peptides during biosynthesis1-9. Peptide/MHC complexes in living cells have been reported to be less stable than similar complexes generated in vitro, which has led to the suggestion that there may be a peptide exchange mechanism operating in vivo l0-12. Although this could increase the capacity for binding incoming antigens, it would reduce the efficacy of processed antigenic peptides by exchanging these for self peptides. Here we measure the half-life of peptide/class II complexes in human antigen-presenting cells and find that it is very similar to the half-life of class II molecules themselves, indicating that peptides are bound irreversibly under physiological conditions. Thus class II MHC retains long-term 'memory' of past encounters with antigen to maximize the opportunity for T cell/antigen-presenting cell interaction.

U2 - 10.1038/357249a0

DO - 10.1038/357249a0

M3 - Article

SN - 0028-0836

VL - 357

SP - 249

EP - 252

JO - Nature

JF - Nature

IS - 6375

ER -

Irreversible association of peptides with class II MHC molecules in living cells

Abstract

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