T-cell recognition of a chimaeric class II/class I MHC molecule and the role of L3T4

Nature ◽  
1985 ◽  
Vol 317 (6036) ◽  
pp. 425-427 ◽  
Author(s):  
Hana Golding ◽  
James McCluskey ◽  
Terry I. Munitz ◽  
Ronald N. Germain ◽  
David H. Margulies ◽  
...  
Keyword(s):  
T Cell ◽  
Class Ii ◽  
Class I ◽  
Cell Recognition ◽  
Class I Mhc ◽  
T Cell Recognition

scholarly journals Clustering Class I MHC Modulates Sensitivity of T Cell Recognition

2006 ◽  
Vol 176 (11) ◽  
pp. 6673-6680 ◽  
Author(s):  
David R. Fooksman ◽  
Gigi Kwik Grönvall ◽  
Qing Tang ◽  
Michael Edidin
Keyword(s):  
T Cell ◽  
Class I ◽  
Cell Recognition ◽  
Class I Mhc ◽  
T Cell Recognition

The role of Class I and II antigens in T cell recognition

1987 ◽  
Vol 43 (1) ◽  
pp. 228-240 ◽  
Author(s):  
Michael J Owen ◽  
Michael J Crumpton
Keyword(s):  
T Cell ◽  
Class I ◽  
Cell Recognition ◽  
T Cell Recognition

scholarly journals Class I major histocompatibility complex-restricted T lymphocyte recognition of the influenza hemagglutinin. Overlap between class I cytotoxic T lymphocytes and antibody sites.

1989 ◽  
Vol 170 (4) ◽  
pp. 1357-1368 ◽  
Author(s):  
M T Sweetser ◽  
V L Braciale ◽  
T J Braciale
Keyword(s):  
T Cell ◽  
T Lymphocytes ◽  
Influenza Virus Infection ◽  
Neutralizing Antibody ◽  
Class I ◽  
Cell Recognition ◽  
Class I Mhc ◽  
T Cell Recognition ◽  
Influenza Hemagglutinin ◽  
A Site

The influenza hemagglutinin is a critical regulator of disease expression during influenza virus infection and serves as a major target for the host immune response to this pathogen. In this report, we have analyzed an immunodominant site on the hemagglutinin (residues 202-221) recognized by murine class I MHC-restricted T lymphocytes. This analysis has revealed evidence for the duplication of a T cell recognition site within the region 202-221. We have also identified critical amino acids necessary for class I-restricted T cell recognition within these two epitopes. In addition, we provide evidence that a site on the influenza hemagglutinin recognized by neutralizing antibody directly overlaps with an epitope recognized by class I MHC-restricted CTL.

Class I MHC/Peptide/ β 2-Microglobulin Interactions:The Basis of Cytotoxic T-Cell Recognition

1993 ◽  
pp. 58-64
Author(s):  
David H. Margulies ◽  
Lisa F. Boyd ◽  
Maripat Corr ◽  
Rosemarie D. Hunziker ◽  
Sergei Khilko ◽  
...  
Keyword(s):  
T Cell ◽  
Class I ◽  
Cytotoxic T Cell ◽  
Cell Recognition ◽  
Class I Mhc ◽  
T Cell Recognition

scholarly journals The Missing Link in Epstein-Barr Virus Immune Evasion: the BDLF3 Gene Induces Ubiquitination and Downregulation of Major Histocompatibility Complex Class I (MHC-I) and MHC-II

2015 ◽  
Vol 90 (1) ◽  
pp. 356-367 ◽  
Author(s):  
Laura L. Quinn ◽  
Luke R. Williams ◽  
Claire White ◽  
Calum Forrest ◽  
Jianmin Zuo ◽  
...  
Keyword(s):  
T Cell ◽  
Mhc Class I ◽  
Immune Evasion ◽  
Class Ii ◽  
Lytic Cycle ◽  
Class I ◽  
Target Cells ◽  
Cell Recognition ◽  
T Cell Recognition ◽  
Mhc Molecules

ABSTRACTThe ability of Epstein-Barr virus (EBV) to spread and persist in human populations relies on a balance between host immune responses and EBV immune evasion. CD8+cells specific for EBV late lytic cycle antigens show poor recognition of target cells compared to immediate early and early antigen-specific CD8+cells. This phenomenon is due in part to the early EBV protein BILF1, whose immunosuppressive activity increases with lytic cycle progression. However, published data suggest the existence of a hitherto unidentified immune evasion protein further enhancing protection against late EBV antigen-specific CD8+cells. We have now identified the late lytic BDLF3 gene as the missing link accounting for efficient evasion during the late lytic cycle. Interestingly, BDLF3 also contributes to evasion of CD4+cell responses to EBV. We report that BDLF3 downregulates expression of surface major histocompatibility complex (MHC) class I and class II molecules in the absence of any effect upon other surface molecules screened, including CD54 (ICAM-1) and CD71 (transferrin receptor). BDLF3 both enhanced internalization of surface MHC molecules and reduced the rate of their appearance at the cell surface. The reduced expression of surface MHC molecules correlated with functional protection against CD8+and CD4+T cell recognition. The molecular mechanism was identified as BDLF3-induced ubiquitination of MHC molecules and their subsequent downregulation in a proteasome-dependent manner.IMPORTANCEImmune evasion is a necessary feature of viruses that establish lifelong persistent infections in the face of strong immune responses. EBV is an important human pathogen whose immune evasion mechanisms are only partly understood. Of the EBV immune evasion mechanisms identified to date, none could explain why CD8+T cell responses to late lytic cycle genes are so infrequent and, when present, recognize lytically infected target cells so poorly relative to CD8+T cells specific for early lytic cycle antigens. The present work identifies an additional immune evasion protein, BDLF3, that is expressed late in the lytic cycle and impairs CD8+T cell recognition by targeting cell surface MHC class I molecules for ubiquitination and proteasome-dependent downregulation. Interestingly, BDLF3 also targets MHC class II molecules to impair CD4+T cell recognition. BDLF3 is therefore a rare example of a viral protein that impairs both the MHC class I and class II antigen-presenting pathways.

scholarly journals Structurally silent peptide anchor modifications allosterically modulate T cell recognition in a receptor-dependent manner

2021 ◽  
Vol 118 (4) ◽  
pp. e2018125118
Author(s):  
Angela R. Smith ◽  
Jesus A. Alonso ◽  
Cory M. Ayres ◽  
Nishant K. Singh ◽  
Lance M. Hellman ◽  
...  
Keyword(s):  
T Cell ◽  
Immune Responses ◽  
Class I ◽  
Immune Recognition ◽  
Dependent Manner ◽  
Cell Recognition ◽  
Class I Mhc ◽  
T Cell Recognition ◽  
Modified Peptides ◽  
The Impact

Presentation of peptides by class I MHC proteins underlies T cell immune responses to pathogens and cancer. The association between peptide binding affinity and immunogenicity has led to the engineering of modified peptides with improved MHC binding, with the hope that these peptides would be useful for eliciting cross-reactive immune responses directed toward their weak binding, unmodified counterparts. Increasing evidence, however, indicates that T cell receptors (TCRs) can perceive such anchor-modified peptides differently than wild-type (WT) peptides, although the scope of discrimination is unclear. We show here that even modifications at primary anchors that have no discernible structural impact can lead to substantially stronger or weaker T cell recognition depending on the TCR. Surprisingly, the effect of peptide anchor modification can be sensed by a TCR at regions distant from the site of modification, indicating a through-protein mechanism in which the anchor residue serves as an allosteric modulator for TCR binding. Our findings emphasize caution in the use and interpretation of results from anchor-modified peptides and have implications for how anchor modifications are accounted for in other circumstances, such as predicting the immunogenicity of tumor neoantigens. Our data also highlight an important need to better understand the highly tunable dynamic nature of class I MHC proteins and the impact this has on various forms of immune recognition.

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