pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction

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Standard

pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction. / Mouritsen, S; Buus, Anette Stryhn; Petersen, B L; Buus, S.

I: Journal of Immunology, Bind 148, Nr. 5, 1992, s. 1438-44.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Mouritsen, S, Buus, AS, Petersen, BL & Buus, S 1992, 'pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction', Journal of Immunology, bind 148, nr. 5, s. 1438-44.

APA

Mouritsen, S., Buus, A. S., Petersen, B. L., & Buus, S. (1992). pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction. Journal of Immunology, 148(5), 1438-44.

Vancouver

Mouritsen S, Buus AS, Petersen BL, Buus S. pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction. Journal of Immunology. 1992;148(5):1438-44.

Author

Mouritsen, S ; Buus, Anette Stryhn ; Petersen, B L ; Buus, S. / pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction. I: Journal of Immunology. 1992 ; Bind 148, Nr. 5. s. 1438-44.

Bibtex

@article{cd10b470ebcd11ddbf70000ea68e967b,
title = "pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction",
abstract = "The pH dependence of the interaction between immunogenic peptide and MHC class II was studied both in a direct biochemical binding assay and in a functional Ag presentation assay. The two approaches yielded similar results. All of the peptides tested bound optimally to their relevant MHC class II restriction element at around pH 4.5. Indeed, several of the peptides did not bind at neutral pH. These results demonstrate that Ag under physiologic conditions meet MHC class II in a quite acidic environment. The very acidic pH optimal for peptide-MHC class II interaction is only found intracellularly and most notably in the endosome-lysosome compartment in which Ag processing is thought to occur. Thus, Ag processing and interaction with MHC class II molecules can potentially happen in the very same compartment. This yet undefined acidic compartment would have to contain proteolytic enzymes and MHC class II molecules.",
author = "S Mouritsen and Buus, {Anette Stryhn} and Petersen, {B L} and S Buus",
note = "Keywords: Amino Acid Sequence; Histocompatibility Antigens Class II; Humans; Hydrogen-Ion Concentration; Molecular Sequence Data; Peptide Fragments; T-Lymphocytes",
year = "1992",
language = "English",
volume = "148",
pages = "1438--44",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "5",

}

RIS

TY - JOUR

T1 - pH dependence of the interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction

AU - Mouritsen, S

AU - Buus, Anette Stryhn

AU - Petersen, B L

AU - Buus, S

N1 - Keywords: Amino Acid Sequence; Histocompatibility Antigens Class II; Humans; Hydrogen-Ion Concentration; Molecular Sequence Data; Peptide Fragments; T-Lymphocytes

PY - 1992

Y1 - 1992

N2 - The pH dependence of the interaction between immunogenic peptide and MHC class II was studied both in a direct biochemical binding assay and in a functional Ag presentation assay. The two approaches yielded similar results. All of the peptides tested bound optimally to their relevant MHC class II restriction element at around pH 4.5. Indeed, several of the peptides did not bind at neutral pH. These results demonstrate that Ag under physiologic conditions meet MHC class II in a quite acidic environment. The very acidic pH optimal for peptide-MHC class II interaction is only found intracellularly and most notably in the endosome-lysosome compartment in which Ag processing is thought to occur. Thus, Ag processing and interaction with MHC class II molecules can potentially happen in the very same compartment. This yet undefined acidic compartment would have to contain proteolytic enzymes and MHC class II molecules.

AB - The pH dependence of the interaction between immunogenic peptide and MHC class II was studied both in a direct biochemical binding assay and in a functional Ag presentation assay. The two approaches yielded similar results. All of the peptides tested bound optimally to their relevant MHC class II restriction element at around pH 4.5. Indeed, several of the peptides did not bind at neutral pH. These results demonstrate that Ag under physiologic conditions meet MHC class II in a quite acidic environment. The very acidic pH optimal for peptide-MHC class II interaction is only found intracellularly and most notably in the endosome-lysosome compartment in which Ag processing is thought to occur. Thus, Ag processing and interaction with MHC class II molecules can potentially happen in the very same compartment. This yet undefined acidic compartment would have to contain proteolytic enzymes and MHC class II molecules.

M3 - Journal article

C2 - 1538129

VL - 148

SP - 1438

EP - 1444

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 5

ER -

ID: 9946329