Association of class I major histocompatibility heavy and light chains induced by viral peptides

Townsend, Alain; Öhlén, Claes; Bastin, Judy; Ljunggren, Hans‐Gustaf; Foster, L.; Kärre, Klas

doi:10.1038/340443a0

Cited by 951 publications

(521 citation statements)

References 47 publications

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“…The egress of functional MHC class I complexes from the ER to the plasma membrane is dependent on the acquisition of peptide by a chain-b 2 M heterodimers [27][28][29]. Augmented chaperone activity may therefore influence the formation of stable MHC-peptide complexes by increasing the concentration of peptides available for binding MHC class I molecules within the ER.…”

Section: Discussionmentioning

confidence: 99%

Restoration of MHC Class I Surface Expression and Endogenous Antigen Presentation by a Molecular Chaperone

Wells

Rai²,

Salvato³

et al. 1997

Scand J Immunol

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Wells AD, Rai SK, Salvato MS, Band H, Malkovsky M. Restoration of MHC Class I Surface Expression and Endogenous Antigen Presentation by a Molecular Chaperone. Scand J Immunol 1997;45:605-612 Presentation of cytosolic peptides in the context of major histocompatibility complex (MHC) class I antigen is crucial for immune recognition of virus-infected and malignant cells. This process, which is often defective in cancer cells, involves a series of cellular events which may be facilitated by heat shock proteins (molecular chaperones). To address the influence of chaperone function on the presentation of cytosolic peptides, we have utilized B16 melanoma cells (H-2 b ). These tumour cells are resistant to lysis by MHC class I-restricted cytotoxic T lymphocytes (CTL), due to a very low level of surface MHC expression. The authors found that stably transfected clones of B16 expressing a heterologous heat shock protein (Hsp65) exhibit significantly increased levels of MHC class I antigens on their surface, and are effectively lysed by alloreactive CTL. These MHC class I molecules can form functional MHC-peptide complexes which are recognized by virus-specific CTL. Moreover, mice immunized with Hsp65-expressing tumour cells, but not with control-transfected tumour cells, display a significantly increased resistance to a subsequent challenge with live, wild-type B16. Together, these results indicate that the suitable expression of a molecular chaperone can overcome a defect in MHC class I expression and antigen presentation, and suggest a novel approach to cancer immunotherapy.

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Section: Discussionmentioning

confidence: 99%

Restoration of MHC Class I Surface Expression and Endogenous Antigen Presentation by a Molecular Chaperone

Wells

Rai²,

Salvato³

et al. 1997

Scand J Immunol

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“…Two of these peptides, LNSVFDQL and TRVLNLGPI, were tested for their ability to bind to MHC class I molecules using an assay based on the peptide-induced stabilization and thereby increase of MHC molecules on the surface of RMA-S cells (H2 b haplotype) 30,31 . As expected, LNSVFDQL showed binding to H2-K b and TRVLNLGPI did assemble with H2-D b molecules (Supplementary Methods and Supplementary Fig.…”

Section: Isolation and Analysis Of Urinary Peptides By Mass Spectromementioning

confidence: 99%

Mouse urinary peptides provide a molecular basis for genotype discrimination by nasal sensory neurons

et al. 2013

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Selected groups of peptides, including those that are presented by major histocompatibility complex (MHC) proteins, have been proposed to transmit information to the olfactory system of vertebrates via their ability to stimulate chemosensory neurons. However, the lack of knowledge about such peptides in natural sources accessible for nasal recognition has been a major barrier for this hypothesis. Here we analyse urinary peptides from selected mouse strains with respect to genotype-related individual differences. We discover many abundant peptides with single amino-acid variations corresponding to genomic differences. The polymorphism of major urinary proteins is reflected by variations in prominent urinary peptides. We also demonstrate an MHC-dependent peptide (SIINFEKL) occurring at very low concentrations in mouse urine. Chemoreceptive neurons in the vomeronasal organ detect and discriminate single amino-acid variation peptides as well as SIINFEKL. Hence, urinary peptides represent a real-time sampling of the expressed genome available for chemosensory assessment by other individuals.

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“…The H chains associate with P 2 m shortly after synthesis in the endoplasmic reticulum (ER) [3]. Assembly of the H chain with p^m and peptide is required for conformational stability and presentation at the cell surface of peptides [4][5][6][7]. Proteins present in the cytosol appear to be cleaved into fragments of 8-11 amino acids [8,9].…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies have identified mouse and human cell lines, designated RMA-S [4], 721.174 [14] and 174CEM.T2 (T2) [15], which produce abundant cytoplasmic H chains and p^m, but present low amounts of surface MHC molecules. These so-called processing-defective cell lines are unable to present endogenously synthesized peptides to CTL [4,16].…”

Section: Introductionmentioning

confidence: 99%

“…These so-called processing-defective cell lines are unable to present endogenously synthesized peptides to CTL [4,16]. The processing defect in the T2 cell line is due to a homozygous deletion of the MHC class II region located on chromosome 6 including theTAPl and TAP2 (transporters associated with antigen processing) genes which encode the transporter proteins [17].The HLA-A2.…”

Section: Introductionmentioning

confidence: 99%

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Identification of peptide sequences that potentially trigger HLA‐A2.1‐restricted cytotoxic T lymphocytes

Nijman¹,

Houbiers²,

Vierboom³

et al. 1993

Eur J Immunol

180

142

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We used the human processing defective cell line 174CEM.T2 (T2) to identify potential cytotoxic T lymphocyte (CTL) epitopes of human proteins. Exogenously added peptides can increase the number of properly folded HLA‐A2.1 molecules on the cell surface of T2 cells, as shown by immunofluorescence measurements using the mouse monoclonal antibody BB7.2 (anti‐HLA‐A2.1) and fluorescein isothiocyanate‐labeled goat anti‐mouse F(ab')2 antibody. The peptides were selected on the basis of a computer score derived from the recently described HLA‐A2.1 specific motif. Analysis of the influenza matrix protein showed that 15 out of 35 high‐scoring peptides up‐regulate the expression of HLA‐A2.1 molecules on theT2 cell surface. The combination of the computer scoring program and an immunofluorescence‐based peptide binding assay allows rapid detection of potential CTL target peptides.

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Association of class I major histocompatibility heavy and light chains induced by viral peptides

Cited by 951 publications

References 47 publications

Restoration of MHC Class I Surface Expression and Endogenous Antigen Presentation by a Molecular Chaperone

Restoration of MHC Class I Surface Expression and Endogenous Antigen Presentation by a Molecular Chaperone

Mouse urinary peptides provide a molecular basis for genotype discrimination by nasal sensory neurons

Identification of peptide sequences that potentially trigger HLA‐A2.1‐restricted cytotoxic T lymphocytes

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