Novel interactions of cardamom mosaic virus VPg with cardamom histones H3 and H4.

The host genome targeting potyviral proteins is sparsely reported. Viral genome-linked protein (VPg) is a multifaceted protein known for its interactions with a suite of host proteins, guides essential viral life cycle processes such as genome replication, translation, genome packing, and antiviral defence. Besides, VPg also plays a crucial role in assisting the transport of nuclear inclusion a protease (NIa protease) into the host nucleus. Apart from that, the role of VPg in the nucleus of the cognate host is not clear. Although NIa protease has been reported for DNase activity, the molecular mechanisms underlying host genome accessibility are not yet understood completely. Here, we employed yeast two hybrid assays to test the cardamom histones H3 and H4 interaction with the VPg and NIa protease of macluravirus (CdMV). Although CdMV NIa protease has the putative histone-binding ER motif of MYST histone acetyltransferase, it did not interact with host histones H3 and H4. Surprisingly, CdMV VPg displayed strong interaction with histone proteins H3 and H4. Leucine prototrophy and β-galactosidase assays were performed which validated VPg interaction with histones. To the best of our knowledge, this study is the first report for the multipartnered potyvirid protein VPg interaction with host histones H3 and H4.