A human herpesvirus 7 glycoprotein, U21, diverts major histocompatibility complex class I molecules to lysosomes. J Virol 2001 Dec;75(24):12347-58
Date
11/17/2001Pubmed ID
11711625Pubmed Central ID
PMC116131DOI
10.1128/JVI.75.24.12347-12358.2001Scopus ID
2-s2.0-0035201673 (requires institutional sign-in at Scopus site) 56 CitationsAbstract
All members of the herpesvirus family persist in their host throughout life. In doing so, herpesviruses exploit a surprising number of different strategies to evade the immune system. Human herpesvirus 7 (HHV-7) is a relatively recently discovered member of the herpesvirus family, and little is known about how it escapes immune detection. Here we show that HHV-7 infection results in premature degradation of major histocompatibility complex class I molecules. We identify and characterize a protein from HHV-7, U21, that binds to and diverts properly folded class I molecules to a lysosomal compartment. Thus, U21 is likely to function in the normal course of HHV-7 infection to downregulate surface class I molecules and prevent recognition of infected cells by cytotoxic T lymphocytes.
Author List
Hudson AW, 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 SequenceCell Line
Concanavalin A
Genes, MHC Class I
Glycoproteins
Herpesvirus 7, Human
Histocompatibility Antigens Class I
Humans
Lysosomes
Molecular Sequence Data
Molecular Weight
Protein Folding
Viral Proteins
