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Expression of a Viral Histone H4 Suppresses Expressions of lysine-specific Demethylase and Serine Proteinase Inhibitor to Inhibit Host Growth and Development
Cotesia plutellae, an endoparasitoids braconid wasp, possesses a polydnaviruses (PDVs) called Cotesia plutellae bracovirus (CpBV) that encodes viral histone H4 (= CpBV-H4). This viral histone H4 shares high sequence homology (82.5%) with host`s H4 of P.xylostella, except an extended N-terminal tail consisting of 38 amino acid residues with nine lysines. Its extended N-terminal tail has been postulated to play a crucial role in suppressing host immunity, growth and development-associated genes, presumably through an epigenetic control mechanism. A suppression subtractive hybridization (SSH) analysis was analyzed in transcriptome by short-read sequencing technology and provided several target and non-target genes of a viral histone H4. In this study, we analyzed the effect CpBV-H4 on the expression of two target genes: Lysine-specific demethylase (KDM) and Serine proteinase inhibitor (Serpins). Transient expression of CpBV-H4 into non parasitized P. xylostella was performed by microinjection of a recombinant expression vector, and showed the expression up to 70 h. Under this transient expression condition, we analyzed the effect of CpBV-H4 on the expression of target genes by RT-PCR at different time points. Interestingly, the CpBV-H4 significantly inhibited the expression of these target genes, while the truncated CpBV-H4 deleting the N-terminal tail did not show this inhibitory effect. This study also showed that the viral histone H4 suppresses expressions of lysine-specific demethylase and serine proteinase inhibitor (Serpin2) to inhibit host growth and development.
