Viral proteins piggybacking chromatin, what else?

15 April 2022 by Delphine LAPAILLERIE
Check out our latest review published in mBio

Accessing the nuclear milieu is an obligate step for many viruses. Many of them rely on mitosis to cross the nuclear envelope, facing the problem of nuclear retention after cell division. To overcome this issue, various viral families elaborated a shared chromatin-tethering strategy. In this review we discussed the structural basis of such viral protein binding to host nucleosomes and how this interaction may contribute to the alteration of higher order chromatin folding.


Bullet point summary:

  • Some DNA virus and retroviral proteins can directly bind nucleosome
  • These viral proteins bind the conserved H2A-H2B acidic patch
  • All acidic patch binders use an invariant Arginine anchor
  • The acidic patch is a hot spot for many cellular chromatin factors interaction
  • Higher order chromatin folding requires free acidic patch to bring closer nucleosomes
  • Acidic patch occupancy by viral proteins alters chromatin folding in vitro.


More details in the open access manuscript:

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