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Macrobrachium rosenbergii  is a highly valued farmed freshwater species and its production has been affected globally by white tail disease caused by  M. rosenbergii  nodavirus (MrNV). MrNV is a single stranded positive sense RNA virus encoding RNA-dependent RNA polymerase (RdRp) for genome replication. Due to its essentiality for pathogenesis, it is an important drug target. The domain prediction of the complete sequence revealed the presence of two enzymatic regions namely methyl transferase and RdRp separated by transmembrane region. The predicted three-dimensional (3D) structure of MnRdRp using AlphaFold 2 shows that the structure is composed of three major sub-domains common for other polymerases namely fingers, palm and thumb. Structural similarity search revealed its similarity with other  flaviviridea  members especially with BVDV RdRp (BvdvRdRp). The structure of fingers and palm sub-domains is more conserved than the thumb sub-domain. A small α-helix named ‘priming helix’ having conserve Tyr was identified at position 829–833 with a potential role in  de novo  initiation. Analysis of electrostatic potential revealed that nucleotide and template channels are electropositive. Metal binding residues were identified as Asp599, Asp704 and Asp705. The α and β phosphates of incoming nucleotide interact with two Mn 2+ , Arg455 and Arg537. For recognition of 2′–OH of incoming rNTP, Asp604, Ser661 and Asn670 were identified which can form H-bond network with 2′–OH group. Docking study revealed that Dasabuvir can potentially inhibit MnRdRp. The study concluded that the overall structure and function of MnRdRp are similar to  Flaviviridae  polymerases and their inhibitors can work against this enzyme. Communicated by Ramaswamy H. Sarma

Structural and functional characterization of RNA dependent RNA polymerase of Macrobrachium rosenbergii nodavirus (MnRdRp)