Key result
Host importin 5 (IPO5) facilitates PCV2 replication by directly binding to the nuclear localization signal of the viral capsid protein to block its proteasome degradation.
Why the study?
The molecular mechanism maintaining the stability of the PCV2 capsid protein during nuclear trafficking was unknown.
IPO5-PCV2 interaction merits antiviral target exploration; leaves open efficacy and safety in porcine models.
Circovirus is the smallest virus to cause immune suppression in pigs. The capsid protein (Cap) is the only viral structural protein that is closely related to viral infection. The nuclear entry and stability of Cap are necessary for PCV2 replication. However, the molecular mechanism maintaining the stability of Cap during nuclear trafficking of PCV2 is unknown. Here, we report that IPO5 aggregates within the nuclear periphery and combines with incoming PCV2 capsids to promote their nuclear entry. Concurrently, IPO5 inhibits the degradation of newly synthesized Cap protein, which facilitates the synthesis of virus proteins and virus replication. These findings highlight a mechanism whereby IPO5 plays a dual role in PCV2 infection, which not only enriches our understanding of the virus replication cycle but also lays the foundation for the subsequent development of antiviral drugs.
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Lin et al. (2022) studied Porcine Circovirus Type 2 (PCV2) infection. IPO5 knockdown or overexpression vs. Control (shCON or empty vector) was evaluated on PCV2 replication and Cap protein stability. Host importin 5 (IPO5) facilitates PCV2 replication by directly binding to the nuclear localization signal of the viral capsid protein to block its proteasome degradation.
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