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

Franceline Juillard1, Marta Pires de Miranda2, Shijun Li1

  • 1Departments of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115.

Proceedings of the National Academy of Sciences of the United States of America
|August 22, 2020
PubMed
Summary

Kaposi's sarcoma-associated herpesvirus (KSHV) latency relies on its LANA protein interacting with unacetylated p53. This acidic domain reader mechanism is crucial for viral persistence and infection establishment.

Keywords:
Kaposi´s sarcoma herpesvirusacetylation-regulated interactionacidic domain readerlatency-associated nuclear antigenvirus persistence

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Area of Science:

  • Virology
  • Molecular Biology
  • Epigenetics

Background:

  • Viruses manipulate host cell pathways for infection.
  • Kaposi's sarcoma-associated herpesvirus (KSHV) causes significant diseases.
  • KSHV latency involves the latency-associated nuclear antigen (LANA) for episome persistence.

Purpose of the Study:

  • To investigate the role of LANA's acidic domain reader in KSHV latency.
  • To determine the interaction mechanism between LANA and p53.
  • To assess the necessity of the acidic domain reader for viral persistence.

Main Methods:

  • Analysis of LANA protein structure and homology to acidic domain readers.
  • Biochemical assays to study LANA-p53 interaction, including effects of p53 acetylation.
  • In vivo studies using KSHV LANA mutants and a murine gammaherpesvirus 68 chimera.

Main Results:

  • LANA possesses acidic domain reader sequences that interact with unacetylated p53.
  • p53 acetylation by CBP or mimicking mutations disrupts LANA binding.
  • Acetylation-deficient p53 mutants show enhanced binding to LANA.
  • KSHV LANA mutants lacking the acidic domain reader are severely impaired in establishing latency and persistent infection.
  • This impairment was confirmed in a murine model.

Conclusions:

  • The acidic domain reader in LANA is essential for KSHV latency and viral persistence.
  • An acetylation-dependent mechanism governs KSHV persistence.
  • This study expands the known functions of acidic domain readers in viral biology.