Faculty Opinions recommendation of Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer.

2007 ◽  
Author(s):  
Peter Van Endert
Keyword(s):  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
High Affinity ◽  
Histocompatibility Complex

scholarly journals Physical Association of the K3 Protein of Gamma-2 Herpesvirus 68 with Major Histocompatibility Complex Class I Molecules with Impaired Peptide and β2-Microglobulin Assembly

2002 ◽  
Vol 76 (6) ◽  
pp. 2796-2803 ◽  
Author(s):  
Y. Y. Lawrence Yu ◽  
Michael R. Harris ◽  
Lonnie Lybarger ◽  
Lisa A. Kimpler ◽  
Nancy B. Myers ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Molecular Chaperones ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
High Affinity ◽  
Histocompatibility Complex ◽  
Peptide Loading ◽  
Mouse Class

ABSTRACT To persist in the presence of an active immune system, viruses encode proteins that decrease expression of major histocompatibility complex class I molecules by using a variety of mechanisms. For example, murine gamma-2 herpesvirus 68 expresses the K3 protein, which causes the rapid turnover of nascent class I molecules. In this report we show that certain mouse class I alleles are more susceptible than others to K3-mediated down regulation. Prior to their rapid degradation, class I molecules in K3-expressing cells exhibit impaired assembly with β2-microglobulin. Furthermore, K3 is detected predominantly in association with class I molecules lacking assembly with high-affinity peptides, including class I molecules associated with the peptide loading complex TAP/tapasin/calreticulin. The detection of K3 with class I assembly intermediates raises the possibility that molecular chaperones involved in class I assembly are involved in K3-mediated class I regulation.

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