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Reduced graphene quantum dots (r-GQD), graphene oxide quantum dots (GOQD), and carboxylated graphene quantum dots (C-GQD) are screened to promote tobacco growth and combat tobacco mosaic virus (TMV). First, a 21-day foliar exposure is employed to explore GQDs' impacts on N. benthamiana. Surface-defective GOQD and C-GQD are screened out to facilitate N. benthamiana uptake through leaf stomata, and to promote seedlings of differently leaf ages to various degrees at different concentrations after different durations of foliar exposure. Specially, compared to the ddH 2 O treatment, GOQD/C-GQD at 400 mg L -1 increase biomass by 44%/68%, increase chlorophyll content by 43%/54% and up-regulate the expression of growth-related genes NtLRX1, CycB, and NtPIP1 by more than two-fold. Second, different from the transient inhibition shown by r-GQD and the TMV enhancement shown by GOQD, C-GQD can directly inactivate TMV infection by inducing TMV aggregation and attachment outside TMV, significantly decreasing TMV replication and hindering TMV spread over 21-day. Specially, C-GQD decreases the transcript abundance of TMV RdRp and TMV CP to 0.11-fold and 0.29-fold, and down-regulates the host defensive response pathways. This work provides a comparative analysis of GQDs with different surface-functionalizations, highlighting C-GQD as a promising nanotechnology tool for promoting plant growth and inactivating phytovirus., (© 2024 Wiley‐VCH GmbH.)

Tobacco mosaic virus coat protein (TMV-CP), as a potential target for the development of antiviral agents, can assist in the long-distance movement of viruses and plays an extremely important role in virus replication and propagation. This work focuses on the synthesis and the action mechanism of novel 4 H -pyrazolo[3,4- d ] pyrimidin-4-one hydrazine derivatives. The synthesized compounds exhibited promising antiviral activity on TMV. Specifically, compound G2 exhibited high inactivating activity (93%) toward TMV, slightly better than commercial reagent NNM (90%). The action of mechanism was further explored by employed molecular docking, molecular dynamics simulation, microscale thermophoresis, qRT-PCR, and transmission electron microscopy. Results indicated that G2 had the capability to interact with amino acid residues such as Trp352 , Tyr139 , and Asn73 in the active pocket of TMV-CP, creating strong hydrophobic interactions and thus obstructing the virus's self-assembly.