Assessment of major histocompatibility complex class I interaction with Epstein-Barr virus and human immunodeficiency virus peptides by elevation of membrane H-2 and HLA in peptide loading-deficient cells

URN to cite this document:

urn:nbn:de:bvb:355-epub-204132 Copy

DOI to cite this document:

10.5283/epub.20413 Copy

Stuber, G. ; Modrow, Susanne ; Höglund, P. ; Franksson, L. ; Elvin, J. ; Wolf, Hans J. ; Kärre, K. ; Klein, G.

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Date of publication of this fulltext: 12 Apr 2011 07:23

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Details

Item type:	Article
Journal or Publication Title:	European journal of immunology
Publisher:	Wiley-VCH
Volume:	22
Number of Issue or Book Chapter:	10
Page Range:	pp. 2697-2703
Date:	1992
Institutions:	Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene
Identification Number:	Value Type 1327802 PubMed ID 10.1002/eji.1830221033 DOI
Classification:	Notation Type Amino Acid Sequence MESH Animals MESH Antigens, Viral/immunology MESH DNA-Binding Proteins/immunology MESH Epstein-Barr Virus Nuclear Antigens MESH Gene Products, gag/immunology MESH H-2 Antigens/analysis MESH HIV-1/immunology MESH HLA-A2 Antigen/analysis MESH Herpesvirus 4, Human/immunology MESH Humans MESH Mice MESH Mice, Inbred C57BL MESH Molecular Sequence Data MESH Viral Proteins/immunology MESH
Dewey Decimal Classification:	600 Technology > 610 Medical sciences Medicine
Status:	Published
Refereed:	Unknown
Created at the University of Regensburg:	Unknown
Item ID:	20413

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Abstract

Earlier findings indicate that peptides can affect the expression of major histocompatibility complex (MHC) class I molecules on the surface of cells with defective peptide loading mechanism. We have used peptide induced increase of class I antigen expression to assess peptide interaction with MHC class I molecules. A panel of 41 overlapping synthetic peptides derived from the human ...

Abstract

Earlier findings indicate that peptides can affect the expression of major histocompatibility complex (MHC) class I molecules on the surface of cells with defective peptide loading mechanism. We have used peptide induced increase of class I antigen expression to assess peptide interaction with MHC class I molecules. A panel of 41 overlapping synthetic peptides derived from the human immunodeficiency virus-1 (HIV-1) gag protein and 33 nonoverlapping peptides from Epstein-Barr virus (EBV) proteins EBNA-1, 2, 3, 4, 5, 6, LMP, BZLF2, BILF2, BSLF2, BALF4 and BcLF1 was assessed for the ability to enhance the expression of HLA-A2.1, H-2Db, Kb and Dd on the murine RMA-S and human 721.174/T2 (.174/T2) lines by indirect immunofluorescence. Considering doubling of the fluorescence intensity in the peptide-treated samples as positivity, 6 of 39 HIV and 1 of 32 EBV peptides were found to bind to A2.1, 6 of 39 HIV gag and 7 of 16 EBV peptides to Db, 8 of 39 HIV gag and 5 of 16 EBV peptides to Kb and 2 of 39 HIV gag and 1 of 17 EBV peptides to Dd. The sensitivity of the method is comparable to the in vitro class I assembly assay with conformation-dependent monoclonal antibody and is more discriminating than the solid-phase assay. Due to its simplicity this method can also serve for testing large peptide panels for binding capacity to various class I molecules. Moreover, the method provides information about the relevance of in vitro tests for class I assembly in living cells.

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