IndraLab

Statements

VIRF-2 activates USP7. 5 / 5
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"The specific identification of TRAF3 and TRAF6 regulation via vIRF-2 targeting of USP7 represents a novel mechanism of viral protein activity via USP7 interaction."
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"The presented data are the first to identify vIRF-2 targeting of USP7 and its role in HHV-8 biology, expanding our understanding of the repertoire and importance of virus-host interactions."
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"To determine the influence of vIRF-2 targeting of USP7 on TRAF3 and TRAF6 polyubiquitination in the context of infection, we compared the ubiquitination status of these TRAFs, expressed in tagged form from lentiviral vectors, in lytically reactivated iSLK cells infected with wild-type or vIRF-2."
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"The present finding of USP7 targeting by vIRF-2, in addition to interactions of HHV-8 vIRFs 1, 3, and 4 with the deubiquitinase, is intriguing, especially as the biological consequences of these interactions appear to be somewhat contradictory and counterintuitive."
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"Here, we report that vIRF-2 also interacts with USP7, via a means distinguishable from USP7 interactions with other vIRFs and other proteins, that this interaction modulates antiviral signaling via disruption of USP7 interactions with innate immune signaling proteins TRAF3 and TRAF6, and that vIRF-2 targeting of USP7 regulates HHV-8 productive replication."
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