Insight into the mechanism of human herpesvirus 7 U21-mediated diversion of class I MHC molecules to lysosomes. J Biol Chem 2010 Nov 19;285(47):37016-29
Date
09/14/2010Pubmed ID
20833720Pubmed Central ID
PMC2978630DOI
10.1074/jbc.M110.125849Scopus ID
2-s2.0-78449233108 (requires institutional sign-in at Scopus site) 14 CitationsAbstract
The U21 open reading frame from human herpesvirus-7 encodes a membrane protein that associates with and redirects class I MHC molecules to the lysosomal compartment. The mechanism by which U21 accomplishes this trafficking excursion is unknown. Here we have examined the contribution of localization, glycosylation, domain structure, and the absence of substrate class I MHC molecules on the ability of U21 to traffic to lysosomes. Our results suggest the existence of a cellular protein necessary for U21-mediated rerouting of class I MHC molecules.
Author List
Glosson NL, Gonyo P, May NA, Schneider CL, Ristow LC, Wang Q, Hudson AWAuthor
Amy W. Hudson PhD Emeritus Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Blotting, WesternCarrier Proteins
Cell Differentiation
Cytoplasm
Endoplasmic Reticulum
Flow Cytometry
Fluorescent Antibody Technique
Glioblastoma
Glycosylation
HLA-A2 Antigen
Herpesvirus 7, Human
Humans
Immunoprecipitation
Lysosomes
Peptide Fragments
Protein Transport
RNA Interference
RNA, Messenger
RNA, Small Interfering
Reverse Transcriptase Polymerase Chain Reaction
Tumor Cells, Cultured
Viral Proteins
beta 2-Microglobulin
