Autophagy induced by human adenovirus B7 structural protein VI inhibits viral replication

Human adenovirus B7 (HAdV-B7) causes severe acute lower respiratory tract infections in children. However, neither the child-specific antivirals or vaccines are available, nor the pathogenesis is clear. Autophagy, as part of innate immunity, plays an important role in resistance to viral infection by degrading the virus and promoting the development of innate and adaptive immunity. This study provided evidence that HAdV-B7 infection induced complete autophagic flux, and the pharmacological induction of autophagy decreased HAdV-B7 replication. In this process, the host protein Bcl2-associated athanogene 3 (BAG3) mediated autophagy to inhibit the replication of HAdV-B7 by binding to the PPSY structural domain of viral protein pVI through its WW structural domain. These findings further our understanding of the host immune response during viral infection and will help to develop broad anti-HAdV therapies.

Automated summary

HAdV-B7 infection induces complete autophagic flux, and pharmacological induction of autophagy inhibits HAdV-B7 replication. Host protein BAG3 mediates autophagy to inhibit HAdV-B7 replication by binding to the PPSY structural domain of viral protein pVI.