The Bacillus velezensis GJ-7 strain isolated from the rhizosphere soil of Panax notoginseng showed high nematicidal activity and therefore has been considered a biological control agent that could act against the root-knot nematode Meloidogyne hapla. However, little was known about whether the GJ-7 strain could produce volatile organic compounds (VOCs) that were effective in biocontrol against M. hapla. In this study, we evaluated the nematicidal activity of VOCs produced by the fermentation of GJ-7 in three-compartment Petri dishes. The results revealed that the mortality rates of M. hapla J2s were 85% at 24 h and 97.1% at 48 h after treatment with the VOCs produced during GJ-7 fermentation. Subsequently, the VOCs produced by the GJ-7 strain were identified through solid-phase micro-extraction gas chromatography mass spectrometry (SPME-GC/MS). Six characteristic VOCs from the GJ-7 strain fermentation broth were identified, including 3-methyl-1-butanol, 3-methyl-2-pentanone, 5-methyl-2-hexanone, 2-heptanone, 2,5-dimethylpyrazine, and 6-methyl-2-heptanone. The in vitro experimental results from 24-well culture plates showed that the six volatiles had direct-contact nematicidal activity against M. hapla J2s and inhibition activity against egg hatching. In addition, 3-methyl-1-butanol and 2-heptanone showed significant fumigation effects on M. hapla J2s and eggs. Furthermore, all six of the VOCs repelled M. hapla J2 juveniles in 2% water agar Petri plates. The above data suggested that the VOCs of B. velezensis GJ-7 acted against M. hapla through multiple prevention and control modes (including direct-contact nematicidal activity, fumigant activity, and repellent activity), and therefore could be considered as potential biocontrol agents against root-knot nematodes.

Panax notoginseng round spot disease (PRSD), caused by Mycocentrospora acerina, is the main leaf disease occurring in cultured P. notoginseng. Aiming to find a safe and efficient control method for PRSD, we studied the disease characteristics of PRSD and the optimal growth conditions of M. acerina and evaluated the efficacy of rain-shelter cultivation in PRSD control. Moreover, we described M. acerina based on morphological characterization and molecular analyses (ITS, ACT, LSU, and TEF-1α). The optimum temperature for M. acerina conidial germination was found to be 14 to 22°C. Furthermore, leaf surface wetness for at least 4 h is required for conidial germination, and conidia can successfully infect P. notoginseng when the leaf wetness lasts for more than 8 h. Additionally, rainwater splashing determines the conidial transfection distance, which is less than 2 m. Finally, our study revealed that rain-shelter cultivation is an effective and simple physical prevention strategy to control PRSD, with an average efficacy of up to 100%.

RGA5 is a component of the Pia resistance-protein pair (RGA4/RGA5) fromOryza sativaL.japonica. It acts as an immune receptor that directly recognizes the effector AVR1-CO39 fromMagnaporthe oryzae viaa C-terminal non-LRR domain (RGA5A_S). The interaction between RGA5A_S and AVR1-CO39 relieves the repression of RGA4, leading to effector-independent cell death. To determine the structure of the complex of RGA5A_S and AVR1-CO39 and to understand the details of this interaction, the complex was prepared by fusing the proteins together, by mixing themin vitroor by co-expressing them in one host cell. Samples purifiedviathe first two strategies were crystallized under two different conditions. A mixture of AVR1-CO39 and RGA5A_S (complex I) crystallized in 1.1 Mammonium tartrate dibasic, 0.1 Msodium acetate–HCl pH 4.6, while crystals of the fusion complex RGA5A_S-TEV-AVR1-CO39 (complex II) were grown in 2 MNaCl. The crystal of complex I belonged to space groupP3₁21, with unit-cell parametersa = b= 66.2,c= 108.8 Å, α = β = 90, γ = 120°. The crystals diffracted to a Bragg spacing of 2.4 Å, and one molecule each of RGA5A_S and AVR1-CO39 were present in the asymmetric unit of the initial model. The crystal of complex II belonged to space groupI4, with unit-cell parametersa=b= 137.4,c= 66.2 Å, α = β = γ = 90°. The crystals diffracted to a Bragg spacing of 2.72 Å, and there were two molecules of RGA5A_S and two molecules of AVR1-CO39 in the asymmetric unit of the initial model. Further structural characterization of the interaction between RGA5A_S and AVR1-CO39 will lead to a better understanding of the mechanism underlying effector recognition by R proteins.