UL25 Capsid Binding Facilitates Mechanical Maturation of the Herpesvirus Capsid and Allows Retention of Pressurized DNA.

ABSTRACT: The maturation process that occurs in most viruses is evolutionarily driven, as it resolves several conflicting virion assembly requirements. During herpesvirus assembly in a host cell nucleus, micron-long double-stranded herpes DNA is packaged into a nanometer-sized procapsid. This leads to strong confinement of the viral genome, resulting in tens of atmospheres of intracapsid DNA pressure. Yet, the procapsid is unstable due to weak reversible interactions between its protein subunits, which ensures free energy minimization and reduces assembly errors. In this work, we show that herpesviruses resolve these contradictory capsid requirements through a mechanical capsid maturation process facilitated by multifunctional auxiliary protein UL25. Through mechanical interrogation of herpes simple

SUBMITTER: Freeman KG 

PROVIDER: S-EPMC8475538 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature