The ER-lumenal domain of the HHV-7 immunoevasin U21 directs class I MHC molecules to lysosomes. Traffic 2003 Dec;4(12):824-37
Date
11/18/2003Pubmed ID
14617346DOI
10.1046/j.1398-9219.2003.0137.xScopus ID
2-s2.0-0348013275 (requires institutional sign-in at Scopus site) 31 CitationsAbstract
Like all members of the herpesvirus family, human herpesvirus-7 has evolved mechanisms to evade immune detection. The human herpesvirus-7 gene product U21 encodes an immunoevasin that binds to class I major histocompatibility complex molecules and diverts them to a lysosomal compartment. Here we show that the cytoplasmic tail of U21, although sufficient to sequester a heterologous membrane protein (CD4 chimera), has no effect on U21's ability to redirect class I major histocompatibility complex molecules to lysosomes. Instead, the ER-lumenal domain of U21 is sufficient to redirect class I major histocompatibility complex molecules to the lysosomal compartment. These observations demonstrate a novel viral immunoevasive mechanism for U21, and implicate the ER-lumenal domain of a type I transmembrane protein in lysosomal sorting.
Author List
Hudson AW, Blom D, Howley PM, Ploegh HLAuthor
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
Amino Acid MotifsAmino Acid Sequence
Antibodies, Monoclonal
CD4 Antigens
Carrier Proteins
Cell Line, Tumor
Cytoplasm
Endoplasmic Reticulum
Flow Cytometry
Herpesvirus 7, Human
Histocompatibility Antigens Class I
Humans
Leucine
Lysosomes
Mannose
Microscopy, Fluorescence
Molecular Sequence Data
Mutation
Phosphorylation
Plasmids
Protein Binding
Protein Folding
Protein Structure, Tertiary
RNA Interference
RNA, Small Interfering
Retroviridae
Viral Proteins
