A facile and cost-efficient hydrothermal and lyophilization two-step strategy has been developed to prepare three-dimensional (3D) SnO2/rGO composites as NO2 gas sensor. In the present study, two different metal salt precursors (Sn(2+) and Sn(4+)) were used to prepare the 3D porous composites. It was found that the products prepared from different tin salts exhibited different sensing performance for NO2 detection. The scanning electron microscopy and transmission electron microscopy characterizations clearly show the macroporous 3D hybrids, nanoporous structure of reduce graphene oxide (rGO), and the supported SnO2 nanocrystals with an average size of 2-7 nm. The specific surface area and porosity properties of the 3D mesoporous composites were analyzed by Braunauer-Emmett-Teller method. The results showed that the SnO2/rGO composite synthesized from Sn(4+) precursor (SnO2/rGO-4) has large surface area (441.9 m(2)/g), which is beneficial for its application as a gas sensing material. The gas sensing platform fabricated from the SnO2/rGO-4 composite exhibited a good linearity for NO2 detection, and the limit of detection was calculated to be as low as about 2 ppm at low temperature. The present work demonstrates that the 3D mesoporous SnO2/rGO composites with extremely large surface area and stable nanostructure are excellent candidate materials for gas sensing.

Verticillium wilt diseases caused by the soil-borne fungus Verticillium dahliae result in devastating yield losses in many economically important crops annually. Here, we identified a novel ethyleneinducing xylanase (EIX)-like protein, VdEIX3, from V. dahliae, which exhibits immunity-inducing activity in Nicotiana benthamiana. In vitro-purified VdEIX3 can induce strong oxidative burst, activate the expression of defense-related genes, and increase resistance against oomycete and fungal pathogens in N. benthamiana. VdEIX3 orthologs of other Verticillium pathogens also induce cell death in N. benthamiana, which form a new type of EIX protein family that is distinct from the known EIX proteins. A leucine-rich repeat receptor-like protein, NbEIX2, regulates the perception of VdEIX3 in N. benthamiana. Our results demonstrate that VdEIX3 is a novel EIX-like protein that can be recognized by N. benthamiana NbEIX2, and also suggest that NbEIX2 is a promising receptor-like protein that is potentially applicable to transgenic breeding for improving resistance to Verticillium wilt diseases.