Specificity of peptide presentation by a set of hybrid mouse class I MHC molecules

Nature ◽  
1987 ◽  
Vol 330 (6149) ◽  
pp. 660-662 ◽  
Author(s):  
Janet L. Maryanski ◽  
Jean-Pierre Abastado ◽  
Philippe Kourilsky
Keyword(s):  
Class I ◽  
Class I Mhc ◽  
Hybrid Mouse ◽  
Mhc Molecules ◽  
Peptide Presentation ◽  
Mouse Class

scholarly journals Self–class I MHC molecules support survival of naive CD8 T cells, but depress their functional sensitivity through regulation of CD8 expression levels

2009 ◽  
Vol 206 (10) ◽  
pp. 2253-2269 ◽  
Author(s):  
Kensuke Takada ◽  
Stephen C. Jameson
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Survival ◽  
Cd8 T Cells ◽  
Cd8 T Cell ◽  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules ◽  
T Cell Survival ◽  
And Function

Previous studies have suggested that naive CD8 T cells require self-peptide–major histocompatability complex (MHC) complexes for maintenance. However, interpretation of such studies is complicated because of the involvement of lymphopenic animals, as lymphopenia drastically alters naive T cell homeostasis and function. In this study, we explored naive CD8 T cell survival and function in nonlymphopenic conditions by using bone marrow chimeric donors and hosts in which class I MHC expression is absent or limited to radiosensitive versus radioresistant cells. We found that long-term survival of naive CD8 T cells (but not CD4 T cells) was impaired in the absence of class I MHC. However, distinct from this effect, class I MHC deprivation also enhanced naive CD8 T cell responsiveness to low-affinity (but not high-affinity) peptide–MHC ligands. We found that this improved sensitivity was a consequence of up-regulated CD8 levels, which was mediated through a transcriptional mechanism. Hence, our data suggest that, in a nonlymphopenic setting, self-class I MHC molecules support CD8 T cell survival, but that these interactions also attenuate naive T cell sensitivity by dynamic tuning of CD8 levels.

scholarly journals Characterization of a Murine Cytomegalovirus Class I Major Histocompatibility Complex (MHC) Homolog: Comparison to MHC Molecules and to the Human Cytomegalovirus MHC Homolog

1998 ◽  
Vol 72 (1) ◽  
pp. 460-466 ◽  
Author(s):  
Tara L. Chapman ◽  
Pamela J. Bjorkman
Keyword(s):  
Major Histocompatibility Complex ◽  
Heavy Chain ◽  
Class I ◽  
Major Histocompatibility ◽  
Class I Mhc ◽  
Endogenous Peptides ◽  
Β2 Microglobulin ◽  
Mhc Molecules ◽  
Histocompatibility Complex ◽  
Infected Cells

ABSTRACT Both human and murine cytomegaloviruses (HCMV and MCMV) down-regulate expression of conventional class I major histocompatibility complex (MHC) molecules at the surfaces of infected cells. This allows the infected cells to evade recognition by cytotoxic T cells but leaves them susceptible to natural killer cells, which lyse cells that lack class I molecules. Both HCMV and MCMV encode class I MHC heavy-chain homologs that may function in immune response evasion. We previously showed that a soluble form of the HCMV class I homolog (UL18) expressed in Chinese hamster ovary cells binds the class I MHC light-chain β2-microglobulin and a mixture of endogenous peptides (M. L. Fahnestock, J. L. Johnson, R. M. R. Feldman, J. M. Neveu, W. S. Lane, and P. J. Bjorkman, Immunity 3:583–590, 1995). Consistent with this observation, sequence comparisons suggest that UL18 contains the well-characterized groove that serves as the binding site in MHC molecules for peptides derived from endogenous and foreign proteins. By contrast, the MCMV homolog (m144) contains a substantial deletion within the counterpart of its α2 domain and might not be expected to contain a groove capable of binding peptides. We have now expressed a soluble version of m144 and verified that it forms a heavy chain–β2-microglobulin complex. By contrast to UL18 and classical class I MHC molecules, m144 does not associate with endogenous peptides yet is thermally stable. These results suggest that UL18 and m144 differ structurally and might therefore serve different functions for their respective viruses.

scholarly journals An endogenous antigenic peptide bypasses the class I antigen presentation defect in RMA-S.

1992 ◽  
Vol 175 (3) ◽  
pp. 719-729 ◽  
Author(s):  
N A Hosken ◽  
M J Bevan
Keyword(s):  
Cell Line ◽  
High Performance ◽  
Genetic Defect ◽  
Class I ◽  
Chromosome 17 ◽  
Antigenic Peptides ◽  
Class I Mhc ◽  
Nucleoprotein Gene ◽  
Mhc Molecules ◽  
Murine Cell Line

The RMA-S cell line was derived from the Raucher virus-induced murine cell line RBL-5 by ethylmethane sulfonate mutagenesis and anti-H-2 antibody plus complement selection (Ljunggren, H.-G., and K. Karre. 1985. J. Exp. Med. 162:1745). RMA-S is defective in the ability to present endogenously synthesized antigens to class I major histocompatibility complex (MHC)-restricted cytotoxic T lymphocytes (CTL) (Townsend, A., C. Ohlen, J. Bastin, H.-G. Ljunggren, L. Foster, and K. Karre. 1989. Nature [Lond.]. 340:443; Ohlen, C., J. Bastin, H.-G. Ljunggren, L. Foster, E. Wolpert, G. Klein, A. R. M. Townsend, and K. Karre. 1990. J. Immunol. 145:52). This defect has been attributed to the inability of RMA-S to deliver antigenic peptides derived from antigens in the cytosol into the endoplasmic reticulum (ER), where they can associate with class I MHC molecules (Townsend, A., C. Ohlen, J. Bastin, H.-G. Ljunggren, L. Foster, and K. Karre. 1989. Nature [Lond.]. 340:443). We show that RMA-S can present at least one endogenous antigen, vesicular stomatitis virus nucleoprotein (VSV-N), to class I MHC-restricted CTL. RMA-S presents VSV-N to CTL both when infected with VSV or transfected with the VSV nucleoprotein gene. The natural antigenic VSV nucleoprotein peptides purified from either RMA or RMA-S are indistinguishable when analyzed by high performance liquid chromatography. We also show that the genetic defect responsible for the RMA-S phenotype maps to the murine chromosome 17. This chromosome encodes the murine class I MHC genes as well as two genes, HAM-1 and -2, with homology to the adenosine triphosphate-dependent transporter superfamily (Monaco, J. J., S. Cho, and M. Attaya. 1990. Science [Wash. DC]. 250:1723). These results suggest that the system that delivers antigenic peptides from the cytosol to the ER in RMA-S may still be present and retain partial function.

scholarly journals Cross-Reactivity of Herpesvirus-Specific CD8 T Cell Lines Toward Allogeneic Class I MHC Molecules

PLoS ONE ◽  
2010 ◽  
Vol 5 (8) ◽  
pp. e12120 ◽  
Author(s):  
Alexis Morice ◽  
Béatrice Charreau ◽  
Bérangère Neveu ◽  
Sophie Brouard ◽  
Jean-Paul Soulillou ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Lines ◽  
Cd8 T Cell ◽  
Cross Reactivity ◽  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules ◽  
T Cell Lines

scholarly journals Use of 8-methoxypsoralen and ultraviolet-A pretreated platelet concentrates to prevent alloimmunization against class I major histocompatibility antigens

Blood ◽  
1991 ◽  
Vol 77 (11) ◽  
pp. 2530-2537 ◽  
Author(s):  
NH Grana ◽  
KJ Kao
Keyword(s):  
Class I ◽  
Major Histocompatibility ◽  
Ultraviolet A ◽  
Platelet Concentrates ◽  
Spleen Cells ◽  
Control Groups ◽  
Class I Mhc ◽  
Mhc Molecules ◽  
Major Histocompatibility Antigens ◽  
The Mean

Abstract The use of 8-methoxypsoralen (8-MOP) and UV-A irradiation to inactivate contaminating donor leukocytes in platelet concentrates and to prevent primary alloimmunization against donor class I major histocompatibility (MHC) antigens in mice was investigated. CBA/CaH-T6J mice with the H2k haplotype and BALB/cByJ mice with the H2d haplotype were used as donors and recipients, respectively. The mixed leukocyte reaction between these two strains of mice showed that treatment of spleen cells with 500 ng/mL 8-MOP and 5J/cm2 UV-A inhibited 99% of responder and 92% of stimulator function. There was no measurable loss of platelet aggregating activity after the treatment. After two weekly transfusions of platelets without any treatment, 93% of control mice (n = 15) developed anti-H2k antibody. In contrast, only 33% of mice (n = 15) receiving platelets treated with 8-MOP and UV-A became alloimmunized. After six weekly platelet transfusions, all mice became alloimmunized. Nevertheless, the mean titers of anti-H2k antibody in sera of the treated groups were significantly lower than the control groups. One hour posttransfusion recoveries of 51Cr-labeled donor platelets were also higher in mice transfused with the treated platelets. Thus, the pretreatment of platelet concentrates with 8-MOP and UV-A irradiation effectively reduced the alloantigenicity of class I MHC molecules. The implication of this finding in relation to the mechanism by which donor leukocytes allosensitize recipients is discussed.

scholarly journals Role of  3 domain of class I MHC molecules in the activation of high- and low-avidity CD8+ CTLs

2007 ◽  
Vol 19 (12) ◽  
pp. 1413-1420 ◽  
Author(s):  
I. M. Belyakov ◽  
S. Kozlowski ◽  
M. Mage ◽  
J. D. Ahlers ◽  
L. F. Boyd ◽  
...  
Keyword(s):  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules

Biotinylation of class I MHC molecules abrogates recognition by W6/32 antibody

1999 ◽  
Vol 53 (6) ◽  
pp. 576-579 ◽  
Author(s):  
P. Malik ◽  
E. Baba ◽  
J.L. Strominger
Keyword(s):  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules

Residue 3 of β 2 -microglobulin affects binding of class I MHC molecules by the W6/32 antibody

1999 ◽  
Vol 49 (4) ◽  
pp. 312-320 ◽  
Author(s):  
John J. Ladasky ◽  
Benny P. Shum ◽  
Flávio Canavez ◽  
Héctor N. Seuánez ◽  
P. Parham
Keyword(s):  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules

A method to quantify binding of unlabeled peptides to class I MHC molecules and detect their allele specificity

1993 ◽  
Vol 158 (2) ◽  
pp. 161-171 ◽  
Author(s):  
John Elvin ◽  
Colin Potter ◽  
Tim Elliott ◽  
Vincenzo Cerundolo ◽  
Alain Townsend
Keyword(s):  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules ◽  
Allele Specificity
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