Low visibility and hot smoke environment under fire conditions can largely hamper the related fire rescue processes. Ultrasound obstacle avoidance technology is then useful for guidance. However, the biggest challenge of adopting ultrasound technology comes from accurate distance measurements under the disturbances of high temperature and soot particle concentration. It is critical to measure the propagation speed under the complicated fire conditions. Therefore, in this study, a baffle calibration method was proposed to improve the accuracy of distance measurement of an obstacle. The method is based on two ultrasound measurement systems, while one is used to calibrate the propagation speed of ultrasound based on the fixed distanced baffle and the other is for the dynamic measurement of obstacle distance based on the calibrated speed. The viability of this method on the guided vehicle was confirmed based on the experiments. From its comparison to those existing methods, such as constant speed and temperature compensation methods, it was known from that the proposed baffle calibration method provides the best prediction. It was obtained that the maximum errors based on the baffle calibration method are 2.75% and 2.62% under the two representative fire scenarios, respectively, which are much lower than those of constant speed (7.81% and 8.4%) and temperature compensation methods (10.4% and 5.12%).

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Gametogenesis is an essential step for malaria parasite transmission and is activated in mosquito by signals including temperature drop, pH change, and mosquito-derived xanthurenic acid (XA). Recently, a membrane protein gametogenesis essential protein 1 (GEP1) was found to be responsible for sensing these signals and interacting with a giant guanylate cyclase α (GCα) to activate the cGMP-PKG-Ca2+ signaling pathway for malaria parasite gametogenesis. However, the molecular mechanisms for this process remain unclear. In this study, we used AlphaFold2 to predict the structure of GEP1 and found that it consists of a conserved N-terminal helical domain and a transmembrane domain that adopts a structure similar to that of cationic amino acid transporters. Molecular docking results showed that XA binds to GEP1 via a pocket similar to the ligand binding sites of known amino acid transporters. In addition, truncations of this N-terminal sequence significantly enhanced the expression, solubility, and stability of GEP1. In addition, we found that GEP1 interacts with GCα via its C-terminal region, which is interrupted by mutations of a few conserved residues. These findings provide further insights into the molecular mechanism for the XA recognition by GEP1 and the activation of the gametogenesis of malaria parasites through GEP1-GCα interaction.