BmATAD3A negatively regulates BmIGF2BP1 to promote BmNPV proliferation

Baculoviruses, large double-stranded DNA viruses, are widely used in biological control and biotechnology; however, their success depends on complex interactions with host factors. Members of the AAA ATPase family are emerging as key regulators in these processes. Previous studies identified Bombyx mori ATAD3A (BmATAD3A) as a host factor hijacked by the viral protein LEF-11 to facilitate Bombyx mori nucleopolyhedrovirus (BmNPV) replication. However, the underlying mechanisms remain poorly understood. We generated transgenic silkworms overexpressing BmATAD3A and demonstrated that its overexpression enhances viral proliferation in vivo. Co-immunoprecipitation (Co-IP) combined with mass spectrometry analysis identified BmIGF2BP1 as an interacting protein of BmATAD3A. Further analysis showed that BmATAD3A negatively regulated the expression of BmIGF2BP1. Additionally, our results showed that BmIGF2BP1 suppresses BmNPV replication, while BmATAD3A-mediated downregulation of BmIGF2BP1 further promotes viral proliferation. This study solidifies the critical role of ATAD3A in BmNPV replication, identifies its interacting proteins, and elucidates the functional interplay between BmIGF2BP1 and BmATAD3A in viral propagation. These findings advance our understanding of the mechanisms by which AAA ATPase family members regulate viral replication, thereby enriching the baculovirus-host interaction network.