HLA-A2.1-Associated Peptides from a Mutant Cell Line: A Second Pathway of Antigen Presentation

Henderson, Robert A.; Michel, Hanspeter; Sakaguchi, Kazuyasu; Shabanowitz, Jeffrey; Appella, Ettore; Hunt, Donald F.; Engelhard, Víctor H.

doi:10.1126/science.1546329

Cited by 489 publications

(337 citation statements)

References 32 publications

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“…The presence of peptides longer than nine residues was previously reported examining natural bound peptides [33][34][35][36][37][38][39][40], although few laboratories evaluated their features and mode of presentation. Some long peptides contained protein signal sequences and were thought to derive from the endoplasmic reticulum [35,41].…”

Section: Features Of Naturally Processed Peptides Selected By Kdmentioning

confidence: 99%

“…Some long peptides contained protein signal sequences and were thought to derive from the endoplasmic reticulum [35,41]. Presentation of long peptides bound to HLA-B27 was reported to depend on TAP transporters [36], while a different analysis suggested that some long peptides bound to HLA-A21 were TAP-independent [42].…”

Section: Features Of Naturally Processed Peptides Selected By Kdmentioning

confidence: 99%

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Identification of naturally processed peptides bound to the class I MHC molecule H‐2K^d of normal and TAP‐deficient cells

et al. 2006

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This report details the biochemical features of natural peptides selected by the H-2K d class I MHC molecule. In normal cell lines, the length of the naturally processed peptides ranged from 8 to 18 amino acids, although the majority were 9-mers (16% were longer than nine residues). The binding motif for the 9-mer peptides was dominated by the presence of a tyrosine at P2 and an isoleucine/leucine at the P9 position. The P2 residue contributed most towards binding; and the short peptides bound better and formed longer-lived cell surface complexes than the long peptides, which bound poorly and dissociated rapidly. The longer peptides did not exhibit this strictly defined motif. Trimming the long peptides to their shorter forms did not enhance binding and conversely, extending the 9-mer peptides did not decrease binding. The long peptides were present on the cell-surface bound to H-2K d (Kd) and were not intermediate products of the class I MHC processing pathway. Finally, in two different TAP-deficient cells the long peptides were the dominant species, which suggested that TAPindependent pathways selected for long peptides by class I MHC molecules.

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Section: Features Of Naturally Processed Peptides Selected By Kdmentioning

confidence: 99%

Section: Features Of Naturally Processed Peptides Selected By Kdmentioning

confidence: 99%

Identification of naturally processed peptides bound to the class I MHC molecule H‐2K^d of normal and TAP‐deficient cells

et al. 2006

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“…On the other hand Henderson et al and Wei et al [47, 481 found recently that HLA-A2.1 bound peptides which are longer than nanomers can be eluted from the T2 cells. Such peptides bind to the A2.1 with affinities similar to those of nanomers [47].…”

Section: The 174/t2 Cellsmentioning

confidence: 99%

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

et al. 1992

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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 BcLFl was assessed for the ability to enhance the expression of HLA-A2.1, H-2Db, Kh 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 HIVand 1 of 32 EBVpeptides were found to bind to A2.1,6 of 39 HIVgag and 7 of 16 EBVpeptides to Dh, 8 of 39 HIVgag 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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“…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. 1 [18][19][20].…”

Section: Introductionmentioning

confidence: 99%

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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HLA-A2.1-Associated Peptides from a Mutant Cell Line: A Second Pathway of Antigen Presentation

Cited by 489 publications

References 32 publications

Identification of naturally processed peptides bound to the class I MHC molecule H‐2K^d of normal and TAP‐deficient cells

Identification of naturally processed peptides bound to the class I MHC molecule H‐2K^d of normal and TAP‐deficient cells

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

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

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HLA-A2.1-Associated Peptides from a Mutant Cell Line: A Second Pathway of Antigen Presentation

Cited by 489 publications

References 32 publications

Identification of naturally processed peptides bound to the class I MHC molecule H‐2Kd of normal and TAP‐deficient cells

Identification of naturally processed peptides bound to the class I MHC molecule H‐2Kd of normal and TAP‐deficient cells

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

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

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Identification of naturally processed peptides bound to the class I MHC molecule H‐2K^d of normal and TAP‐deficient cells

Identification of naturally processed peptides bound to the class I MHC molecule H‐2K^d of normal and TAP‐deficient cells