Author Correction: Mobile Real-Time Grasshopper Detection and Data Aggregation Framework.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Mobile Real-Time Grasshopper Detection and Data Aggregation Framework.

Insects of the family Orthoptera: Acrididae including grasshoppers and locust devastate crops and eco-systems around the globe. The effective control of these insects requires large numbers of trained extension agents who try to spot concentrations of the insects on the ground so that they can be destroyed before they take flight. This is a challenging and difficult task. No automatic detection system is yet available to increase scouting productivity, data scale and fidelity. Here we demonstrate MAESTRO, a novel grasshopper detection framework that deploys deep learning within RBG images to detect insects. MAESTRO uses a state-of-the-art two-stage training deep learning approach. The framework can be deployed not only on desktop computers but also on edge devices without internet connection such as smartphones. MAESTRO can gather data using cloud storge for further research and in-depth analysis. In addition, we provide a challenging new open dataset (GHCID) of highly variable grasshopper populations imaged in Inner Mongolia. The detection performance of the stationary method and the mobile App are 78 and 49 percent respectively; the stationary method requires around 1000 ms to analyze a single image, whereas the mobile app uses only around 400 ms per image. The algorithms are purely data-driven and can be used for other detection tasks in agriculture (e.g. plant disease detection) and beyond. This system can play a crucial role in the collection and analysis of data to enable more effective control of this critical global pest.

Modular assembly of proteins on nanoparticles.

Generally, the high diversity of protein properties necessitates the development of unique nanoparticle bio-conjugation methods, optimized for each different protein. Here we describe a universal bio-conjugation approach which makes use of a new recombinant fusion protein combining two distinct domains. The N-terminal part is Glutathione S-Transferase (GST) from Schistosoma japonicum, for which we identify and characterize the remarkable ability to bind gold nanoparticles (GNPs) by forming gold-sulfur bonds (Au-S). The C-terminal part of this multi-domain construct is the SpyCatcher from Streptococcus pyogenes, which provides the ability to capture recombinant proteins encoding a SpyTag. Here we show that SpyCatcher can be immobilized covalently on GNPs through GST without the loss of its full functionality. We then show that GST-SpyCatcher activated particles are able to covalently bind a SpyTag modified protein by simple mixing, through the spontaneous formation of an unusual isopeptide bond.