We have previously shown that non-structural protein p35, encoded by Scylla serrata reovirus (SsRV) S10, may act as a viroporin. To characterize the role of p35 protein in the modulation of cellular function, a yeast two-hybrid system was used to screen a cDNA library derived from S. serrata to find its interacting partner. Protein interactions were confirmed in vitro by GST pull-down. Full cDNAs of p35 interactors were cloned by the rapid amplification of cDNA ends. After two-hybrid library screening, we isolated partial cDNAs encoding hemocyanin, cryptocyanin, and TAX1BP1. Interaction of p35 with each of hemocyanin, cryptocyanin, and TAX1BP1 was confirmed by GST pull-down. The full-length cDNA fragments of hemocyanin, cryptocyanin, and TAX1BP1 were 2287, 2422, and 3437 bp, respectively, and they encoded three putative proteins with molecular masses of ~76.9, ~79.2, and ~107.2 kDa, respectively. This study casts new light on the function and physiological significance of p35 during the SsRV replication cycle.
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