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The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling

The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling ▿ Brian M. Sullivan and Laurent Coscoy * Department of Molecular and Cell Biology, Division of Immunology and Pathogenesis, University of California, Berkeley, 142 Life Sciences Addition, Berkeley, California 94720 ABSTRACT Modulation of T-cell receptor expression and signaling is essential to the survival of many viruses. The U24 protein expressed by human herpesvirus 6A, a ubiquitous human pathogen, has been previously shown to downregulate the T-cell receptor. Here, we show that U24 also mediates cell surface downregulation of a canonical early endosomal recycling receptor, the transferrin receptor, indicating that this viral protein acts by blocking early endosomal recycling. We present evidence that U24 is a C-tail-anchored protein that is dependent for its function on TRC40/Asna-1, a component of a posttranslational membrane insertion pathway. Finally, we find that U24 proteins from other roseoloviruses have a similar genetic organization and a conserved function that is dependent on a proline-rich motif. Inhibition of a basic cellular process by U24 has interesting implications not only for the pathogenicity of roseoloviruses but also for our understanding of the biology of endosomal transport. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Virology American Society For Microbiology

The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling

Journal of Virology , Volume 84 (3): 1265 – Feb 1, 2010

The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling

Journal of Virology , Volume 84 (3): 1265 – Feb 1, 2010

Abstract

The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling ▿ Brian M. Sullivan and Laurent Coscoy * Department of Molecular and Cell Biology, Division of Immunology and Pathogenesis, University of California, Berkeley, 142 Life Sciences Addition, Berkeley, California 94720 ABSTRACT Modulation of T-cell receptor expression and signaling is essential to the survival of many viruses. The U24 protein expressed by human herpesvirus 6A, a ubiquitous human pathogen, has been previously shown to downregulate the T-cell receptor. Here, we show that U24 also mediates cell surface downregulation of a canonical early endosomal recycling receptor, the transferrin receptor, indicating that this viral protein acts by blocking early endosomal recycling. We present evidence that U24 is a C-tail-anchored protein that is dependent for its function on TRC40/Asna-1, a component of a posttranslational membrane insertion pathway. Finally, we find that U24 proteins from other roseoloviruses have a similar genetic organization and a conserved function that is dependent on a proline-rich motif. Inhibition of a basic cellular process by U24 has interesting implications not only for the pathogenicity of roseoloviruses but also for our understanding of the biology of endosomal transport.

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References (67)

Publisher
American Society For Microbiology
Copyright
Copyright © 2010 by the American society for Microbiology.
ISSN
0022-538X
eISSN
1098-5514
DOI
10.1128/JVI.01775-09
pmid
19923186
Publisher site
See Article on Publisher Site

Abstract

The U24 Protein from Human Herpesvirus 6 and 7 Affects Endocytic Recycling ▿ Brian M. Sullivan and Laurent Coscoy * Department of Molecular and Cell Biology, Division of Immunology and Pathogenesis, University of California, Berkeley, 142 Life Sciences Addition, Berkeley, California 94720 ABSTRACT Modulation of T-cell receptor expression and signaling is essential to the survival of many viruses. The U24 protein expressed by human herpesvirus 6A, a ubiquitous human pathogen, has been previously shown to downregulate the T-cell receptor. Here, we show that U24 also mediates cell surface downregulation of a canonical early endosomal recycling receptor, the transferrin receptor, indicating that this viral protein acts by blocking early endosomal recycling. We present evidence that U24 is a C-tail-anchored protein that is dependent for its function on TRC40/Asna-1, a component of a posttranslational membrane insertion pathway. Finally, we find that U24 proteins from other roseoloviruses have a similar genetic organization and a conserved function that is dependent on a proline-rich motif. Inhibition of a basic cellular process by U24 has interesting implications not only for the pathogenicity of roseoloviruses but also for our understanding of the biology of endosomal transport.

Journal

Journal of VirologyAmerican Society For Microbiology

Published: Feb 1, 2010

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