Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector

Rice stripe virus (RSV) is the type member of the genus Tenuivirus, which relies on the small brown planthopper (Laodelphax striatellus Fallén) for its transmission in a persistent, circulative-propagative manner. To be transmitted, virus must cross the midgut and salivary glands epithelial barriers in a transcytosis mechanism where vector receptors interact with virions, and as propagative virus, RSV need utilize host components to complete viral propagation in vector cells. At present, these mechanisms remain unknown. In this paper, we screened L. striatellus proteins, separated by two-dimensional electrophoresis (2-DE), as potential RSV binding molecules using a virus overlay assay of protein blots. The results, five L. striatellus proteins that bound to purified RSV particles in vitro were resolved and identified using mass spectrometry. The virus-binding capacities of five proteins were further elucidated in yeast two-hybrid screen (YTHS) and virus-binding experiments of expressed proteins. Among five proteins, the receptor for activated protein kinase C (RACK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH3) did not interact with RSV nucleocapsid protein (NCP) in YTHS and in far-Western blot, and three ribosomal proteins (RPL5, RPL7a and RPL8) had specific interactions with RSV. In dot immunobinding assay (DIBA), all five proteins were able to bind to RSV particles. The five proteins' potential contributions to the interactions between RSV and L. striatellus were discussed. We proposed that RACK and GAPDH3 might be involved in the epithelial transcytosis of virus particles, and three ribosomal proteins probably played potential crucial roles in the infection and propagation of RSV in vector cells

Fault Tolerant Free Gait and Footstep Planning for Hexapod Robot Based on Monte-Carlo Tree

Legged robots can pass through complex field environments by selecting gaits and discrete footholds carefully. Traditional methods plan gait and foothold separately and treat them as the single-step optimal process. However, such processing causes its poor passability in a sparse foothold environment. This paper novelly proposes a coordinative planning method for hexapod robots that regards the planning of gait and foothold as a sequence optimization problem with the consideration of dealing with the harshness of the environment as leg fault. The Monte Carlo tree search algorithm(MCTS) is used to optimize the entire sequence. Two methods, FastMCTS, and SlidingMCTS are proposed to solve some defeats of the standard MCTS applicating in the field of legged robot planning. The proposed planning algorithm combines the fault-tolerant gait method to improve the passability of the algorithm. Finally, compared with other planning methods, experiments on terrains with different densities of footholds and artificially-designed challenging terrain are carried out to verify our methods. All results show that the proposed method dramatically improves the hexapod robot's ability to pass through sparse footholds environment

Generation and Bioenergetic Profiles of Cybrids with East Asian mtDNA Haplogroups

Human mitochondrial DNA (mtDNA) variants and haplogroups may contribute to susceptibility to various diseases and pathological conditions, but the underlying mechanisms are not well understood. To address this issue, we established a cytoplasmic hybrid (cybrid) system to investigate the role of mtDNA haplogroups in human disease; specifically, we examined the effects of East Asian mtDNA genetic backgrounds on oxidative phosphorylation (OxPhos). We found that mtDNA single nucleotide polymorphisms such as m.489T>C, m.10398A>G, m.10400C>T, m.C16223T, and m.T16362C affected mitochondrial function at the level of mtDNA, mtRNA, or the OxPhos complex. Macrohaplogroup M exhibited higher respiratory activity than haplogroup N owing to its higher mtDNA content, mtRNA transcript levels, and complex III abundance. Additionally, haplogroup M had higher reactive oxygen species levels and NAD+/NADH ratios than haplogroup N, suggesting difference in mitonuclear interactions. Notably, subhaplogroups G2, B4, and F1 appeared to contribute significantly to the differences between haplogroups M and N. Thus, our cybrid-based system can provide insight into the mechanistic basis for the role of mtDNA haplogroups in human diseases and the effect of mtDNA variants on mitochondrial OxPhos function. In addition, studies of mitonuclear interaction using this system can reveal predisposition to certain diseases conferred by variations in mtDNA

Magnon-mediated interlayer coupling in an all-antiferromagnetic junction

The interlayer coupling mediated by fermions in ferromagnets brings about parallel and anti-parallel magnetization orientations of two magnetic layers, resulting in the giant magnetoresistance, which forms the foundation in spintronics and accelerates the development of information technology. However, the interlayer coupling mediated by another kind of quasi-particle, boson, is still lacking. Here we demonstrate such a static interlayer coupling at room temperature in an antiferromagnetic junction Fe2O3/Cr2O3/Fe2O3, where the two antiferromagnetic Fe2O3 layers are functional materials and the antiferromagnetic Cr2O3 layer serves as a spacer. The N\'eel vectors in the top and bottom Fe2O3 are strongly orthogonally coupled, which is bridged by a typical bosonic excitation (magnon) in the Cr2O3 spacer. Such an orthogonally coupling exceeds the category of traditional collinear interlayer coupling via fermions in ground state, reflecting the fluctuating nature of the magnons, as supported by our magnon quantum well model. Besides the fundamental significance on the quasi-particle-mediated interaction, the strong coupling in an antiferromagnetic magnon junction makes it a realistic candidate for practical antiferromagnetic spintronics and magnonics with ultrahigh-density integration.Comment: 19 pages, 4 figure

Formation of Complexes at Plasmodesmata for Potyvirus Intercellular Movement Is Mediated by the Viral Protein P3N-PIPO

Intercellular transport of viruses through cytoplasmic connections, termed plasmodesmata (PD), is essential for systemic infection in plants by viruses. Previous genetic and ultrastructural data revealed that the potyvirus cyclindrical inclusion (CI) protein is directly involved in cell-to-cell movement, likely through the formation of conical structures anchored to and extended through PD. In this study, we demonstrate that plasmodesmatal localization of CI in N. benthamiana leaf cells is modulated by the recently discovered potyviral protein, P3N-PIPO, in a CI:P3N-PIPO ratio-dependent manner. We show that P3N-PIPO is a PD-located protein that physically interacts with CI in planta. The early secretory pathway, rather than the actomyosin motility system, is required for the delivery of P3N-PIPO and CI to PD. Moreover, CI mutations that disrupt virus cell-to-cell movement compromise PD-localization capacity. These data suggest that the CI and P3N-PIPO complex coordinates the formation of PD-associated structures that facilitate the intercellular movement of potyviruses in infected plants

Formation of Complexes at Plasmodesmata for Potyvirus Intercellular Movement Is Mediated by the Viral Protein P3N-PIPO

Intercellular transport of viruses through cytoplasmic connections, termed plasmodesmata (PD), is essential for systemic infection in plants by viruses. Previous genetic and ultrastructural data revealed that the potyvirus cyclindrical inclusion (CI) protein is directly involved in cell-to-cell movement, likely through the formation of conical structures anchored to and extended through PD. In this study, we demonstrate that plasmodesmatal localization of CI in N. benthamiana leaf cells is modulated by the recently discovered potyviral protein, P3N-PIPO, in a CI:P3N-PIPO ratio-dependent manner. We show that P3N-PIPO is a PD-located protein that physically interacts with CI in planta. The early secretory pathway, rather than the actomyosin motility system, is required for the delivery of P3N-PIPO and CI to PD. Moreover, CI mutations that disrupt virus cell-to-cell movement compromise PD-localization capacity. These data suggest that the CI and P3N-PIPO complex coordinates the formation of PD-associated structures that facilitate the intercellular movement of potyviruses in infected plants