Shared fine specificity between T-cell receptors and an antibody recognizing a peptide/major histocompatibility class I complex

A Stryhn; P S Andersen; L O Pedersen; A Svejgaard; A Holm; C J Thorpe; L Fugger; S Buus; J Engberg

Shared fine specificity between T-cell receptors and an antibody recognizing a peptide/major histocompatibility class I complex

A Stryhn, P S Andersen, L O Pedersen, A Svejgaard, A Holm, C J Thorpe, L Fugger, S Buus, J Engberg

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

43 Citationer (Scopus)

Abstract

Udgivelsesdato: 1996-Sep-17

Originalsprog	Engelsk
Tidsskrift	Proceedings of the National Academy of Science of the United States of America
Vol/bind	93
Udgave nummer	19
Sider (fra-til)	10338-42
Antal sider	4
ISSN	0027-8424
Status	Udgivet - 1996

Bibliografisk note

Keywords: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibody Specificity; Binding Sites; Epitopes; Histocompatibility Antigens Class I; Lymphoma, T-Cell; Major Histocompatibility Complex; Mice; Mice, Inbred AKR; Models, Molecular; Peptide Fragments; Protein Structure, Secondary; Receptors, Antigen, T-Cell; Recombinant Proteins; T-Lymphocytes, Cytotoxic; Tumor Cells, Cultured; Vesicular stomatitis Indiana virus

Citationsformater

Shared fine specificity between T-cell receptors and an antibody recognizing a peptide/major histocompatibility class I complex. / Stryhn, A; Andersen, P S; Pedersen, L O; Svejgaard, A; Holm, A; Thorpe, C J; Fugger, L; Buus, S; Engberg, J.

I: Proceedings of the National Academy of Science of the United States of America, Bind 93, Nr. 19, 1996, s. 10338-42.

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

@article{a2839110ebcc11ddbf70000ea68e967b,

title = "Shared fine specificity between T-cell receptors and an antibody recognizing a peptide/major histocompatibility class I complex",

abstract = "Cytotoxic T cells recognize mosaic structures consisting of target peptides embedded within self-major histocompatibility complex (MHC) class I molecules. This structure has been described in great detail for several peptide-MHC complexes. In contrast, how T-cell receptors recognize peptide-MHC complexes have been less well characterized. We have used a complete set of singly substituted analogs of a mouse MHC class I, Kk-restricted peptide, influenza hemagglutinin (Ha)255-262, to address the binding specificity of this MHC molecule. Using the same peptide-MHC complexes we determined the fine specificity of two Ha255-262-specific, Kk-restricted T cells, and of a unique antibody, pSAN, specific for the same peptide-MHC complex. Independently, a model of the Ha255-262-Kk complex was generated through homology modeling and molecular mechanics refinement. The functional data and the model corroborated each other showing that peptide residues 1, 3, 4, 6, and 7 were exposed on the MHC surface and recognized by the T cells. Thus, the majority, and perhaps all, of the side chains of the non-primary anchor residues may be available for T-cell recognition, and contribute to the stringent specificity of T cells. A striking similarity between the specificity of the T cells and that of the pSAN antibody was found and most of the peptide residues, which could be recognized by the T cells, could also be recognized by the antibody.",

author = "A Stryhn and Andersen, {P S} and Pedersen, {L O} and A Svejgaard and A Holm and Thorpe, {C J} and L Fugger and S Buus and J Engberg",

note = "Keywords: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibody Specificity; Binding Sites; Epitopes; Histocompatibility Antigens Class I; Lymphoma, T-Cell; Major Histocompatibility Complex; Mice; Mice, Inbred AKR; Models, Molecular; Peptide Fragments; Protein Structure, Secondary; Receptors, Antigen, T-Cell; Recombinant Proteins; T-Lymphocytes, Cytotoxic; Tumor Cells, Cultured; Vesicular stomatitis Indiana virus",

year = "1996",

language = "English",

volume = "93",

pages = "10338--42",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "The National Academy of Sciences of the United States of America",

number = "19",

}

TY - JOUR

T1 - Shared fine specificity between T-cell receptors and an antibody recognizing a peptide/major histocompatibility class I complex

AU - Stryhn, A

AU - Andersen, P S

AU - Pedersen, L O

AU - Svejgaard, A

AU - Holm, A

AU - Thorpe, C J

AU - Fugger, L

AU - Buus, S

AU - Engberg, J

N1 - Keywords: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibody Specificity; Binding Sites; Epitopes; Histocompatibility Antigens Class I; Lymphoma, T-Cell; Major Histocompatibility Complex; Mice; Mice, Inbred AKR; Models, Molecular; Peptide Fragments; Protein Structure, Secondary; Receptors, Antigen, T-Cell; Recombinant Proteins; T-Lymphocytes, Cytotoxic; Tumor Cells, Cultured; Vesicular stomatitis Indiana virus

PY - 1996

Y1 - 1996

N2 - Cytotoxic T cells recognize mosaic structures consisting of target peptides embedded within self-major histocompatibility complex (MHC) class I molecules. This structure has been described in great detail for several peptide-MHC complexes. In contrast, how T-cell receptors recognize peptide-MHC complexes have been less well characterized. We have used a complete set of singly substituted analogs of a mouse MHC class I, Kk-restricted peptide, influenza hemagglutinin (Ha)255-262, to address the binding specificity of this MHC molecule. Using the same peptide-MHC complexes we determined the fine specificity of two Ha255-262-specific, Kk-restricted T cells, and of a unique antibody, pSAN, specific for the same peptide-MHC complex. Independently, a model of the Ha255-262-Kk complex was generated through homology modeling and molecular mechanics refinement. The functional data and the model corroborated each other showing that peptide residues 1, 3, 4, 6, and 7 were exposed on the MHC surface and recognized by the T cells. Thus, the majority, and perhaps all, of the side chains of the non-primary anchor residues may be available for T-cell recognition, and contribute to the stringent specificity of T cells. A striking similarity between the specificity of the T cells and that of the pSAN antibody was found and most of the peptide residues, which could be recognized by the T cells, could also be recognized by the antibody.

AB - Cytotoxic T cells recognize mosaic structures consisting of target peptides embedded within self-major histocompatibility complex (MHC) class I molecules. This structure has been described in great detail for several peptide-MHC complexes. In contrast, how T-cell receptors recognize peptide-MHC complexes have been less well characterized. We have used a complete set of singly substituted analogs of a mouse MHC class I, Kk-restricted peptide, influenza hemagglutinin (Ha)255-262, to address the binding specificity of this MHC molecule. Using the same peptide-MHC complexes we determined the fine specificity of two Ha255-262-specific, Kk-restricted T cells, and of a unique antibody, pSAN, specific for the same peptide-MHC complex. Independently, a model of the Ha255-262-Kk complex was generated through homology modeling and molecular mechanics refinement. The functional data and the model corroborated each other showing that peptide residues 1, 3, 4, 6, and 7 were exposed on the MHC surface and recognized by the T cells. Thus, the majority, and perhaps all, of the side chains of the non-primary anchor residues may be available for T-cell recognition, and contribute to the stringent specificity of T cells. A striking similarity between the specificity of the T cells and that of the pSAN antibody was found and most of the peptide residues, which could be recognized by the T cells, could also be recognized by the antibody.

M3 - Journal article

C2 - 8816801

VL - 93

SP - 10338

EP - 10342

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 19

ER -