Structural requirements for the interaction between class II MHC molecules and peptide antigens

A Sette; S Buus; E Appella; L Adorini; H M Grey

Structural requirements for the interaction between class II MHC molecules and peptide antigens

A Sette, S Buus, E Appella, L Adorini, H M Grey

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

13 Citationer (Scopus)

Abstract

Udgivelsesdato: 1990-null

Originalsprog	Engelsk
Tidsskrift	Immunologic Research
Vol/bind	9
Udgave nummer	1
Sider (fra-til)	2-7
Antal sider	5
ISSN	0257-277X
Status	Udgivet - 1990

Bibliografisk note

Keywords: Amino Acid Sequence; Animals; Antigens; Histocompatibility Antigens Class II; Molecular Sequence Data; Peptides; Protein Binding

Citationsformater

@article{f6e070b0ebcd11ddbf70000ea68e967b,

title = "Structural requirements for the interaction between class II MHC molecules and peptide antigens",

abstract = "Previous work from our and other laboratories indicates that T cells recognize a complex between the MHC restriction element and peptide antigen fragments. This paper reviews the structural characteristics of the formation of such a complex. By analyzing in detail the interactions between purified IA(d) and IE(d) molecules and their peptide ligands, we found that some structural characteristics apply to both antigen-MHC interactions. In particular, we found: 1) each MHC molecule is capable of binding many unrelated peptides through the same peptide-binding site; 2) despite this permissiveness of binding, it is possible to define certain structural features of peptides that are associated with the capacity to bind to a particular MHC specificity (IA(d) or IE(d)); 3) IA(d) and IE(d) molecules recognize different and independent structures on the antigen molecule; 4) only about 10% of the single amino acid substitutions tested on two IA(d)- and IE(d)-binding peptides had significant effect on their MHC-binding capacities, while over 80% of these substitutions significantly impaired T cell recognition of the Ia-peptide complex; 5) based on the segregation between residues that are crucial for T cell activation and Ia binding, the easiest model for the antigen-Ia-T-cell-receptor complex pictures the antigen molecule sandwiched in a planar conformation between the MHC and the T cell.",

author = "A Sette and S Buus and E Appella and L Adorini and Grey, {H M}",

note = "Keywords: Amino Acid Sequence; Animals; Antigens; Histocompatibility Antigens Class II; Molecular Sequence Data; Peptides; Protein Binding",

year = "1990",

language = "English",

volume = "9",

pages = "2--7",

journal = "Immunologic Research",

issn = "0257-277X",

publisher = "Humana Press",

number = "1",

}

TY - JOUR

T1 - Structural requirements for the interaction between class II MHC molecules and peptide antigens

AU - Sette, A

AU - Buus, S

AU - Appella, E

AU - Adorini, L

AU - Grey, H M

N1 - Keywords: Amino Acid Sequence; Animals; Antigens; Histocompatibility Antigens Class II; Molecular Sequence Data; Peptides; Protein Binding

PY - 1990

Y1 - 1990

N2 - Previous work from our and other laboratories indicates that T cells recognize a complex between the MHC restriction element and peptide antigen fragments. This paper reviews the structural characteristics of the formation of such a complex. By analyzing in detail the interactions between purified IA(d) and IE(d) molecules and their peptide ligands, we found that some structural characteristics apply to both antigen-MHC interactions. In particular, we found: 1) each MHC molecule is capable of binding many unrelated peptides through the same peptide-binding site; 2) despite this permissiveness of binding, it is possible to define certain structural features of peptides that are associated with the capacity to bind to a particular MHC specificity (IA(d) or IE(d)); 3) IA(d) and IE(d) molecules recognize different and independent structures on the antigen molecule; 4) only about 10% of the single amino acid substitutions tested on two IA(d)- and IE(d)-binding peptides had significant effect on their MHC-binding capacities, while over 80% of these substitutions significantly impaired T cell recognition of the Ia-peptide complex; 5) based on the segregation between residues that are crucial for T cell activation and Ia binding, the easiest model for the antigen-Ia-T-cell-receptor complex pictures the antigen molecule sandwiched in a planar conformation between the MHC and the T cell.

AB - Previous work from our and other laboratories indicates that T cells recognize a complex between the MHC restriction element and peptide antigen fragments. This paper reviews the structural characteristics of the formation of such a complex. By analyzing in detail the interactions between purified IA(d) and IE(d) molecules and their peptide ligands, we found that some structural characteristics apply to both antigen-MHC interactions. In particular, we found: 1) each MHC molecule is capable of binding many unrelated peptides through the same peptide-binding site; 2) despite this permissiveness of binding, it is possible to define certain structural features of peptides that are associated with the capacity to bind to a particular MHC specificity (IA(d) or IE(d)); 3) IA(d) and IE(d) molecules recognize different and independent structures on the antigen molecule; 4) only about 10% of the single amino acid substitutions tested on two IA(d)- and IE(d)-binding peptides had significant effect on their MHC-binding capacities, while over 80% of these substitutions significantly impaired T cell recognition of the Ia-peptide complex; 5) based on the segregation between residues that are crucial for T cell activation and Ia binding, the easiest model for the antigen-Ia-T-cell-receptor complex pictures the antigen molecule sandwiched in a planar conformation between the MHC and the T cell.

M3 - Journal article

C2 - 2406349

VL - 9

SP - 2

EP - 7

JO - Immunologic Research

JF - Immunologic Research

SN - 0257-277X

IS - 1

ER -