scholarly journals TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide

1998 ◽  
Vol 8 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Veronique M. Braud ◽  
David S.J. Allan ◽  
Douglas Wilson ◽  
Andrew J. McMichael
Keyword(s):  
Mhc Class I ◽  
Surface Expression ◽  
Class I ◽  
Leader Peptide

scholarly journals A Distinctive Cytoplasmic Tail Contributes to Low Surface Expression and Intracellular Retention of the Patr-AL MHC Class I Molecule

2015 ◽  
Vol 195 (8) ◽  
pp. 3725-3736 ◽  
Author(s):  
Ana Goyos ◽  
Lisbeth A. Guethlein ◽  
Amir Horowitz ◽  
Hugo G. Hilton ◽  
Michael Gleimer ◽  
...  
Keyword(s):  
Mhc Class I ◽  
Cytoplasmic Tail ◽  
Surface Expression ◽  
Class I ◽  
Mhc Class I Molecule

scholarly journals Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein.

1995 ◽  
Vol 182 (5) ◽  
pp. 1615-1619 ◽  
Author(s):  
J Hombach ◽  
H Pircher ◽  
S Tonegawa ◽  
R M Zinkernagel
Keyword(s):  
Antigen Presentation ◽  
Mhc Class I ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Signal Sequence ◽  
Class I ◽  
Signal Peptidase ◽  
Leader Peptide ◽  
Virus Protein ◽  
Mhc Class I Molecules

Peptides presented by major histocompatibility complex (MHC) class I molecules are derived from intracellularly synthesized proteins. Cytosolic proteins are fragmented into peptides, which are subsequently transported via the transporter of antigen presentation (TAP) into the endoplasmic reticulum (ER), where they bind to MHC class I molecules. We have investigated the requirements for MHC class I presentation of the immunodominant gp33 cytotoxic T lymphocyte epitope of the lymphocytic choriomeningitis virus. This epitope is located within the leader peptide of the virus glycoprotein. Such an epitope is expected to be presented in a TAP-independent manner, since it is released into the ER by signal peptidase. Taking advantage of TAP1-/- mice, however, we show both in vitro and in vivo that, after virus infection, the presentation of the gp33 epitope is strictly dependent on a functional TAP heterodimer. The results are discussed with respect to peptide trimming processes in the ER.

scholarly journals Modulation of Transporter Associated with Antigen Processing (TAP)-Mediated Peptide Import into the Endoplasmic Reticulum by Flavivirus Infection

2001 ◽  
Vol 75 (12) ◽  
pp. 5663-5671 ◽  
Author(s):  
Frank Momburg ◽  
Arno Müllbacher ◽  
Mario Lobigs
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Surface ◽  
Mhc Class I ◽  
Antigen Processing ◽  
Surface Expression ◽  
Class I ◽  
Peptide Transport ◽  
Cell Surface Expression ◽  
Flavivirus Infection ◽  
Mhc Class I Molecules

ABSTRACT In contrast to many other viruses that escape the cellular immune response by downregulating major histocompatibility complex (MHC) class I molecules, flavivirus infection can upregulate their cell surface expression. Previously we have presented evidence that during flavivirus infection, peptide supply to the endoplasmic reticulum is increased (A. Müllbacher and M. Lobigs, Immunity 3:207–214, 1995). Here we show that during the early phase of infection with different flaviviruses, the transport activity of the peptide transporter associated with antigen processing (TAP) is augmented by up to 50%. TAP expression is unaltered during infection, and viral but not host macromolecular synthesis is required for enhanced peptide transport. This study is the first demonstration of transient enhancement of TAP-dependent peptide import into the lumen of the endoplasmic reticulum as a consequence of a viral infection. We suggest that the increased supply of peptides for assembly with MHC class I molecules in flavivirus-infected cells accounts for the upregulation of MHC class I cell surface expression with the biological consequence of viral evasion of natural killer cell recognition.

scholarly journals Cell Surface Expression of Major Histocompatibility Complex Class I Molecules Is Reduced in Hepatitis C Virus Subgenomic Replicon-Expressing Cells

2003 ◽  
Vol 77 (21) ◽  
pp. 11644-11650 ◽  
Author(s):  
Keith D. Tardif ◽  
Aleem Siddiqui
Keyword(s):  
Major Histocompatibility Complex ◽  
Hepatitis C ◽  
Cell Surface ◽  
Mhc Class I ◽  
Surface Expression ◽  
Protein Glycosylation ◽  
Class I ◽  
Cell Surface Expression ◽  
Histocompatibility Complex ◽  
Mhc Class I Molecules

ABSTRACT The hepatitis C virus (HCV) causes chronic hepatitis in most infected individuals by evading host immune defenses. In this investigation, we show that HCV-infected cells may go undetected in the immune system by suppressing major histocompatibility complex (MHC) class I antigen presentation to cytotoxic T lymphocytes. Cells expressing HCV subgenomic replicons have lower MHC class I cell surface expression. This is due to reduced levels of properly folded MHC class I molecules. HCV replicons induce endoplasmic reticulum (ER) stress (K. Tardif, K. Mori, and A. Siddiqui, J. Virol. 76:7453-7459, 2002), which results from a decline in protein glycosylation. Decreasing protein glycosylation can disrupt protein folding, preventing the assembly of MHC class I molecules. This results in the accumulation of unfolded MHC class I. Therefore, the persistence and pathogenesis of HCV may depend upon the ER stress-mediated interference of MHC class I assembly and cell surface expression.

scholarly journals Orf virus interferes with MHC class I surface expression by targeting vesicular transport and Golgi

2012 ◽  
Vol 8 (1) ◽  
pp. 114 ◽  
Author(s):  
Jörg Rohde ◽  
Frederic Emschermann ◽  
Michael R Knittler ◽  
Hanns-Joachim Rziha
Keyword(s):  
Mhc Class I ◽  
Vesicular Transport ◽  
Surface Expression ◽  
Orf Virus ◽  
Class I

MHC class I surface expression in embryo-derived cell lines inducible with peptide or interferon

Nature ◽  
1991 ◽  
Vol 354 (6350) ◽  
pp. 235-238 ◽  
Author(s):  
Elizabeth K. Bikoff ◽  
Leah Jaffe ◽  
Randall K. Ribaudo ◽  
Gillis R. Otten ◽  
Ronald N. Germain ◽  
...  
Keyword(s):  
Mhc Class I ◽  
Cell Lines ◽  
Surface Expression ◽  
Class I

scholarly journals The cationic region from HIV tat enhances the cell-surface expression of epitope/MHC class I complexes

Gene Therapy ◽  
2003 ◽  
Vol 10 (25) ◽  
pp. 2067-2073 ◽  
Author(s):  
J A Leifert ◽  
P D Holler ◽  
S Harkins ◽  
D M Kranz ◽  
J L Whitton
Keyword(s):  
Cell Surface ◽  
Mhc Class I ◽  
Surface Expression ◽  
Class I ◽  
Cell Surface Expression ◽  
Hiv Tat
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