Major histocompatibility complex conformational epitopes are peptide specific.

Catipovic, Branimir; Porto, Joseph Dal; Mage, Michael G.; Johansen, Teit E.; Schneck, Jonathan P.

doi:10.1084/jem.176.6.1611

Cited by 103 publications

(62 citation statements)

References 40 publications

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“…The DAP/OVA/K b cell line was generated by transfection using Lipofectamine Plus (Invitrogen Life Technologies), according to the manufacturer's recommendations. Approximately 4 g of the K b plasmid pKbT.8 (24,25) was linearized with PvuI (Fermentas Life Sciences), ethanol precipitated, resuspended in 100 l of DMEM (Biofluids), mixed with 16 l of Plus reagent, and incubated for 15 min at room temperature. One hundred microliters of DMEM containing 10 l of lipofectamine was then added, and the mixture was incubated for an additional 15 min.…”

Section: Micementioning

confidence: 99%

Dendritic Cells Cross-Dressed with Peptide MHC Class I Complexes Prime CD8+ T Cells

Dolan

Gibbs

Ostrand‐Rosenberg

2006

The Journal of Immunology

132

114

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The activation of naive CD8+ T cells has been attributed to two mechanisms: cross-priming and direct priming. Cross-priming and direct priming differ in the source of Ag and in the cell that presents the Ag to the responding CD8+ T cells. In cross-priming, exogenous Ag is acquired by professional APCs, such as dendritic cells (DC), which process the Ag into peptides that are subsequently presented. In direct priming, the APCs, which may or may not be DC, synthesize and process the Ag and present it themselves to CD8+ T cells. In this study, we demonstrate that naive CD8+ T cells are activated by a third mechanism, called cross-dressing. In cross-dressing, DC directly acquire MHC class I-peptide complexes from dead, but not live, donor cells by a cell contact-mediated mechanism, and present the intact complexes to naive CD8+ T cells. Such DC are cross-dressed because they are wearing peptide-MHC complexes generated by other cells. CD8+ T cells activated by cross-dressing are restricted to the MHC class I genotype of the donor cells and are specific for peptides generated by the donor cells. In vivo studies demonstrate that optimal priming of CD8+ T cells requires both cross-priming and cross-dressing. Thus, cross-dressing may be an important mechanism by which DC prime naive CD8+ T cells and may explain how CD8+ T cells are primed to Ags that are inefficiently cross-presented.

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Section: Micementioning

confidence: 99%

Dendritic Cells Cross-Dressed with Peptide MHC Class I Complexes Prime CD8+ T Cells

Dolan

Gibbs

Ostrand‐Rosenberg

2006

The Journal of Immunology

132

114

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“…The following peptides were used: the E␣-derived peptide Ep [52][53][54][55][56][57][58][59][60][61][62][63][64][65][66][67][68] …”

Section: Peptidesmentioning

confidence: 99%

The Alloreactive and Self-Restricted CD4+ T Cell Response Directed Against a Single MHC Class II/Peptide Combination

Kovalik

Singh

Mendiratta

et al. 2000

The Journal of Immunology

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The cellular basis for allograft rejection derives from the strong T cell response to cells bearing foreign MHC. While it was originally assumed that alloreactive T cells focus their recognition on the polymorphic residues that differ between syngeneic and allogeneic MHC molecules, studies with MHC class I-restricted CTL have shown that MHC-bound peptides play a critical role in allorecognition. It has been suggested that alloreactive T cells depend more strongly on interactions with the MHC molecule than with the associated peptide, but there is little evidence to support this idea. Here we have studied the alloreactive and self-restricted response directed against the class II H2-Ab molecule bound with a single peptide, Ep, derived from the H2-Eα chain. This MHC class II-peptide combination was a poor target and stimulator of alloreactive CD4+ T cell responses, indicating that MHC-bound peptides are as important for alloreactive CD4+ T cells as they are for alloreactive CTL. We also generated alloreactive T cells with exquisite specificity for the Ab/Ep complex, and compared their reactivity with self-restricted T cells specific for the same Ab/Ep complex. Our results showed that peptide-specific alloreactive T cells, as compared with self-restricted T cells, were more sensitive to peptide stimulation, but equally sensitive to amino acid substitutions in the peptide. These findings indicate that alloreactive and self-restricted T cells interact similarly with their MHC/peptide ligand.

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“…These molecules can be exogenously loaded with a single type of synthetic peptide thereby creating a situation in which all class I-peptide complexes on the cell surface are identical. In a set of recent reports, we (10) and others (11) (17) using either 1 mg of antibody or 1 ml of ascites fluid coupled to protein A-Sepharose beads for immunoabsorption. The mAbs used in these studies included SF1.2, Y3, and 100-30.…”

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confidence: 99%

Alloantibodies can discriminate class I major histocompatibility complex molecules associated with various endogenous peptides.

Sherman

Chattopadhyay²,

Biggs³

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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Molecules encoded by a single major histo- (7)(8)(9). These molecules can be exogenously loaded with a single type of synthetic peptide thereby creating a situation in which all class I-peptide complexes on the cell surface are identical. In a set of recent reports, we (10) and others (11) observed that loading unoccupied Kb molecules with different synthetic peptide antigens altered their recognition by alloantibodies. For instance, the Kb-specific monoclonal antibody (mAb) SF1.2 bound Kbovalbumin peptide complexes significantly better than empty Kb or Kb-Sendai (SV9) peptide complexes (10). In contrast, the Kb-specific mAb 100-30 reacted strongly to empty Kb or Kb-SV9 complexes but not to Kb-ovalbumin peptide complexes. These results suggested that the nature of the peptide bound to the class I molecule influenced alloantibody recognition. However, such results were obtained using synthetic antigens, some of which were much longer than endogenous peptides that are generally eight or nine residues long. Based on these results, as well as the observation by several laboratories that antibodies can be specific for certain MHC-

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Major histocompatibility complex conformational epitopes are peptide specific.

Cited by 103 publications

References 40 publications

Dendritic Cells Cross-Dressed with Peptide MHC Class I Complexes Prime CD8+ T Cells

Dendritic Cells Cross-Dressed with Peptide MHC Class I Complexes Prime CD8+ T Cells

The Alloreactive and Self-Restricted CD4+ T Cell Response Directed Against a Single MHC Class II/Peptide Combination

Alloantibodies can discriminate class I major histocompatibility complex molecules associated with various endogenous peptides.

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