The extreme 5′-end of the enterovirus RNA genome contains a conserved cloverleaf-like domain that recruits 3CD and PCBP proteins required for initiating genome replication. Here, we report the crystal structure at 1.9 Å resolution of this domain from the CVB3 genome in complex with an antibody chaperone. The RNA folds into an antiparallel H-type four-way junction comprising four subdomains with co-axially stacked sA-sD and sB-sC helices. Long-range interactions between a conserved A40 in the sC-loop and Py-Py helix within the sD subdomain organize near-parallel orientations of the sA-sB and sC-sD helices. Our NMR studies confirm that these long-range interactions occur in solution and without the chaperone. The phylogenetic analyses indicate that our crystal structure represents a conserved architecture of enteroviral cloverleaf-like domains, including the A40 and Py-Py interactions. The protein binding studies further suggest that the H-shape architecture provides a ready-made platform to recruit 3CD and PCBP2 for viral replication.

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With increasing climate variability, a sustainable crop production approach remains an indispensable concern across the globe. In this study, P retention/availability of MgCl2.6H2O/KOH modified Douglas fir biochar was assessed. The MgCl2·6H2O/KOH treated Douglas fir biochar was prepared by sequentially treating Douglas fir biochar with magnesium chloride and potassium hydroxide solutions. The biochar’s surface area, pore volume, morphology, and elemental compositions were determined using BET, SEM, SEM/EDS, and powder X-ray analyzes. Both surface area and pore volume were reduced by more than 97% following modification. Similarly, the morphology and elemental compositions changed after modification. The maximum P adsorbed corresponding to Langmuir–Freundlich model was 41.18 mg g−1. P sorption on biochar soil mixture was pH dependent. More studies are required to establish the field applicability of P-laden MgCl2 ·6H2O/KOH-modified Douglas fir biochar as a soil additive.

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