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Journal of Virology, December 2001, p. 12347-12358, Vol. 75, No. 24
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.24.12347-12358.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

A Human Herpesvirus 7 Glycoprotein, U21, Diverts Major Histocompatibility Complex Class I Molecules to Lysosomes

Amy W. Hudson,* Peter M. Howley, and Hidde L. Ploegh

Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115

Received 24 July 2001/Accepted 12 September 2001

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.

* Corresponding author. Mailing address: Department of Pathology, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-2892. Fax: (617) 432-0727. E-mail: ahudson{at}hms.harvard.edu.

Journal of Virology, December 2001, p. 12347-12358, Vol. 75, No. 24
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.24.12347-12358.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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