Herpes simplex virus UL56 interacts with and regulates the Nedd4-family ubiquitin ligase ItchReportar como inadecuado




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Virology Journal

, 7:179

First Online: 03 August 2010Received: 16 March 2010Accepted: 03 August 2010

Abstract

BackgroundHerpes simplex virus type 2 HSV-2 is one of many viruses that exploits and modifies the cellular ubiquitin system. HSV-2 expresses the tegument protein UL56 that has been implicated in cytoplasmic transport and-or release of virions, and is a putative regulatory protein of Nedd4 ubiquitin ligase. In order to elucidate the biological function of UL56, this study examined the interaction of UL56 with the Nedd4-family ubiquitin ligase Itch and its role in the regulation of Itch. Additionally, we assessed the similarity between UL56 and regulatory proteins of Itch and Nedd4, Nedd4-family-interactins proteins Ndfip.

ResultsUL56 interacted with Itch, independent of additional viral proteins, and mediated more striking degradation of Itch, compared to Nedd4. Moreover, it was suggested that the lysosome pathway as well as the proteasome pathway was involved in the degradation of Itch. Other HSV-2 proteins with PY motifs, such as VP5 and VP16, did not mediate the degradation of endogenous Itch. Ndfip1 and Ndfip2 were similar in subcellular distribution patterns to UL56 and colocalized with UL56 in co-transfected cells.

ConclusionsWe believe that this is the first report demonstrating the interaction of a HSV-specific protein and Itch. Thus, UL56 could function as a regulatory protein of Itch. The mechanism, function and significance of regulating Itch in HSV-2 infection remain unclear and warrant further investigation.

Electronic supplementary materialThe online version of this article doi:10.1186-1743-422X-7-179 contains supplementary material, which is available to authorized users.

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Autor: Yoko Ushijima - Chenhong Luo - Maki Kamakura - Fumi Goshima - Hiroshi Kimura - Yukihiro Nishiyama

Fuente: https://link.springer.com/







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