English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Understanding how viruses modulate host cell function is central to prospects for potential therapies. A recently described mechanism mediates selective protein interactions between acidic domain readers and unacetylated, lysine-rich regions, opposite of bromodomain function. Here we show that the latency-associated nuclear antigen (LANA) encoded by Kaposi´s sarcoma-associated herpesvirus (KSHV) contains a SET oncoprotein homologous acidic domain reader that interacts with p53 in an acetylation-dependent manner. Significantly, the LANA acidic domain reader is critical for viral latency and persistent infection. The finding that KSHV has evolved a mechanism for acetylation-dependent protein interaction underscores the physiological importance of this cellular regulatory posttranslational modification. Furthermore, opportunity may exist to develop inhibitors that disrupt LANA acidic domain reader function for therapy of KSHV-associated tumors.

KSHV LANA acetylation-selective acidic domain reader sequence mediates virus persistence