Structural principles that govern the peptide-binding motifs of class I MHC molecules 1 1Edited by I. Wilson

1998 ◽  
Vol 281 (5) ◽  
pp. 929-947 ◽  
Author(s):  
Chao Zhang ◽  
Abraham Anderson ◽  
Charles DeLisi
Keyword(s):  
Peptide Binding ◽  
Class I ◽  
Class I Mhc ◽  
Binding Motifs ◽  
Mhc Molecules ◽  
Structural Principles

scholarly journals Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses

2017 ◽  
Vol 69 (5) ◽  
pp. 351-358
Author(s):  
Tobias Bergmann ◽  
Mikaela Lindvall ◽  
Erin Moore ◽  
Eugene Moore ◽  
John Sidney ◽  
...  
Keyword(s):  
Peptide Binding ◽  
Class I ◽  
Class I Mhc ◽  
Binding Motifs ◽  
Mhc Molecules ◽  
Thoroughbred Horses

Detailed characterization of the peptide binding specificity of five common Patr class I MHC molecules

2006 ◽  
Vol 58 (7) ◽  
pp. 559-570 ◽  
Author(s):  
John Sidney ◽  
Shinichi Asabe ◽  
Bjoern Peters ◽  
Kelly-Anne Purton ◽  
Josan Chung ◽  
...  
Keyword(s):  
Peptide Binding ◽  
Binding Specificity ◽  
Class I ◽  
Detailed Characterization ◽  
Class I Mhc ◽  
Peptide Binding Specificity ◽  
Mhc Molecules

scholarly journals Dynamic Characteristics of a Peptide-Binding Groove of Human HLA-A2 Class I MHC Molecules: Normal Mode Analysis of the Antigen Peptide–Class I MHC Complex

2002 ◽  
Vol 50 (9) ◽  
pp. 1209-1209 ◽  
Author(s):  
Hiroyuki Nojima ◽  
Mayuko Takeda-Shitaka ◽  
Youji Kurihara ◽  
Masaaki Adachi ◽  
Shigetaka Yoneda ◽  
...  
Keyword(s):  
Dynamic Characteristics ◽  
Normal Mode Analysis ◽  
Peptide Binding ◽  
Class I ◽  
Mode Analysis ◽  
Class I Mhc ◽  
Mhc Molecules ◽  
Antigen Peptide ◽  
Peptide Binding Groove ◽  
Binding Groove

An improved assembly assay for peptide binding to HLA-B*2705 and H-2Kk class I MHC molecules

1997 ◽  
Vol 209 (1) ◽  
pp. 25-36 ◽  
Author(s):  
Linda Tan ◽  
Mads Hald Andersen ◽  
Tim Elliott ◽  
John S Haurum
Keyword(s):  
Peptide Binding ◽  
Class I ◽  
Class I Mhc ◽  
Mhc Molecules

Importance of a single amino acid substitution of the α helices of class I MHC molecules for the induction of a primary allogeneic response

1996 ◽  
Vol 47 (1-2) ◽  
pp. 162
Author(s):  
Reboul Murielle ◽  
Noun Ghada ◽  
Abastado Jean-Pierre ◽  
Kourilsky Philippe ◽  
Pla Marika
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Class I ◽  
Single Amino Acid ◽  
Class I Mhc ◽  
Mhc Molecules ◽  
Allogeneic Response

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.

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 Peptide-binding motifs associated with MHC molecules common in Chinese rhesus macaques are analogous to those of human HLA supertypes and include HLA-B27-like alleles

2013 ◽  
Vol 65 (5) ◽  
pp. 371-386 ◽  
Author(s):  
Bianca R. Mothé ◽  
Scott Southwood ◽  
John Sidney ◽  
A. Michelle English ◽  
Amanda Wriston ◽  
...  
Keyword(s):  
Rhesus Macaques ◽  
Peptide Binding ◽  
Hla B27 ◽  
Binding Motifs ◽  
Mhc Molecules ◽  
Chinese Rhesus Macaques

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.

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