Development of Magnetic-Based Navigation by Constructing Maps Using Machine Learning for Autonomous Mobile Robots in Real Environments.

Localization is fundamental to enable the use of autonomous mobile robots. In this work, we use magnetic-based localization. As Earth's geomagnetic field is stable in time and is not affected by nonmagnetic materials, such as a large number of people in the robot's surroundings, magnetic-based localization is ideal for service robotics in supermarkets, hotels, etc. A common approach for magnetic-based localization is to first create a magnetic map of the environment where the robot will be deployed. For this, magnetic samples acquired a priori are used. To generate this map, the collected data is interpolated by training a Gaussian Process Regression model. Gaussian processes are nonparametric, data-drive models, where the most important design choice is the selection of an adequate kernel function. These models are flexible and generate mean predictions as well as the confidence of those predictions, making them ideal for their use in probabilistic approaches. However, their computational and memory cost scales poorly when large datasets are used for training, making their use in large-scale environments challenging. The purpose of this study is to: (i) enable magnetic-based localization on large-scale environments by using a sparse representation of Gaussian processes, (ii) test the effect of several kernel functions on robot localization, and (iii) evaluate the accuracy of the approach experimentally on different large-scale environments.

Color Changes in Ag Nanoparticle Aggregates Placed in Various Environments: Their Application to Air Monitoring.

Fresh Ag nanoparticles (NPs) dispersed on a transparent SiO2 exhibit an intense optical extinction band originating in localized surface plasmon resonance (LSPR) in the visible range. The intensity of the LSPR band weakened when the Ag NPs was stored in ambient air for two weeks. The rate of the weakening and the LSPR wavelength shift, corresponding to visual chromatic changes, strongly depended on the environment in which Ag NPs were set. The origin of a chromatic change was discussed along with both compositional and morphological changes. In one case, bluish coloring followed by a prompt discoloring was observed for Ag NPs placed near the ventilation fan in our laboratory, resulted from adsorption of large amounts of S and Cl on Ag NP surfaces as well as particle coarsening. Such color changes deduce the presence of significant amounts of S and Cl in the environment. In another case, a remarkable blue-shift of the LSPR band was observed for the Ag NPs stored in the desiccator made of stainless steel, originated in the formation of CN and/or HCN compounds and surface roughening. Their color changed from maroon to reddish, suggesting that such molecules were present inside the desiccator.

Putative Neural Network Within an Olfactory Sensory Unit for Nestmate and Non-nestmate Discrimination in the Japanese Carpenter Ant: The Ultra-structures and Mathematical Simulation.

Ants are known to use a colony-specific blend of cuticular hydrocarbons (CHCs) as a pheromone to discriminate between nestmates and non-nestmates and the CHCs were sensed in the basiconic type of antennal sensilla (S. basiconica). To investigate the functional design of this type of antennal sensilla, we observed the ultra-structures at 2D and 3D in the Japanese carpenter ant, Camponotus japonicus, using a serial block-face scanning electron microscope (SBF-SEM), and conventional and high-voltage transmission electron microscopes. Based on the serial images of 352 cross sections of SBF-SEM, we reconstructed a 3D model of the sensillum revealing that each S. basiconica houses > 100 unbranched dendritic processes, which extend from the same number of olfactory receptor neurons (ORNs). The dendritic processes had characteristic beaded-structures and formed a twisted bundle within the sensillum. At the "beads," the cell membranes of the processes were closely adjacent in the interdigitated profiles, suggesting functional interactions via gap junctions (GJs). Immunohistochemistry with anti-innexin (invertebrate GJ protein) antisera revealed positive labeling in the antennae of C. japonicus. Innexin 3, one of the five antennal innexin subtypes, was detected as a dotted signal within the S. basiconica as a sensory organ for nestmate recognition. These morphological results suggest that ORNs form an electrical network via GJs between dendritic processes. We were unable to functionally certify the electric connections in an olfactory sensory unit comprising such multiple ORNs; however, with the aid of simulation of a mathematical model, we examined the putative function of this novel chemosensory information network, which possibly contributes to the distinct discrimination of colony-specific blends of CHCs or other odor detection.

Purification of human and avian influenza viruses using cellulose sulfate ester (Cellufine Sulfate) in the process of vaccine production.

Affinity chromatography using sulfated, spherical cellulose beads (Cellufine Sulfate) was assessed for purification of influenza A and influenza B viruses. Recovery rates of viruses eluted from the beads were high for all tested virus strains. This method was also useful for removing chicken egg-derived impurities from allantoic fluids containing influenza viruses; the hemagglutination activity per amount of protein in the eluted sample was significantly higher than that in the applied sample. These results suggest that use of Cellufine Sulfate is a practical method for primary purification of influenza viruses in the process of influenza vaccine production.

A functional polymorphism in the 5' UTR of GDF5 is associated with susceptibility to osteoarthritis.

Osteoarthritis (MIM 165720), characterized by degeneration of articular cartilage, is the most common form of human arthritis and a major concern for aging societies worldwide. Epidemiological and genetic studies have shown that osteoarthritis is a polygenic disease. Here, we report that the gene encoding growth differentiation factor 5 (GDF5) is associated with osteoarthritis in Asian populations. A SNP in the 5' UTR of GDF5 (+104T/C; rs143383) showed significant association (P = 1.8 x 10(-13)) with hip osteoarthritis in two independent Japanese populations. This association was replicated for knee osteoarthritis in Japanese (P = 0.0021) and Han Chinese (P = 0.00028) populations. This SNP, located in the GDF5 core promoter, exerts allelic differences on transcriptional activity in chondrogenic cells, with the susceptibility allele showing reduced activity. Our findings implicate GDF5 as a susceptibility gene for osteoarthritis and suggest that decreased GDF5 expression is involved in the pathogenesis of osteoarthritis.

An odorant-binding protein facilitates odorant transfer from air to hydrophilic surroundings in the blowfly.

Chemical sense-related lipophilic ligand-binding protein (CRLBP) is an insect odorant-binding protein (OBP) found abundantly in the taste and olfactory organs of the blowfly, Phormia regina. Through computational construction, a three-dimensional molecular model of a CRLBP indicated good fitting to a fluorescent ligand, 7-hydroxycoumarin (7-HC), in its ligand-binding pocket. By showing that the fluorescence of 7-HC bound to CRLBP migrated in a native electrophoresis gel, we confirmed that CRLBP formed a stable complex with 7-HC. In an odorant-binding experiment, 7-HC vapor odor was introduced by aeration to the aquatic solution containing CRLBP and its binding to CRLBP fluorospectrometrically quantified. Because olfactory organs as well as taste organs of flies respond to vapors, we suggest that CRLBP effectively transfers odorants from the air into aquatic surroundings by forming stable complexes with airborne molecules in both chemosensory organs.

Rab11 mediates post-Golgi trafficking of rhodopsin to the photosensitive apical membrane of Drosophila photoreceptors.

In developing Drosophila photoreceptors, rhodopsin is trafficked to the rhabdomere, a specialized domain within the apical membrane surface. Rab11, a small GTPase implicated in membrane traffic, immunolocalizes to the trans-Golgi network, cytoplasmic vesicles and tubules, and the base of rhabdomeres. One hour after release from the endoplasmic reticulum, rhodopsin colocalizes with Rab11 in vesicles at the base of the rhabdomere. When Rab11 activity is reduced by three different genetic procedures, rhabdomere morphogenesis is inhibited and rhodopsin-bearing vesicles proliferate within the cytosol. Rab11 activity is also essential for development of MVB endosomal compartments; this is probably a secondary consequence of impaired rhabdomere development. Furthermore, Rab11 is required for transport of TRP, another rhabdomeric protein, and for development of specialized membrane structures within Garland cells. These results establish a role for Rab11 in the post-Golgi transport of rhodopsin and of other proteins to the rhabdomeric membranes of photoreceptors, and in analogous transport processes in other cells.

Immunohistochemical localization of Papilio RBP in the eye of butterflies.

We recently identified a novel retinoid binding protein, Papilio RBP, in the soluble fraction of the eye homogenate of the butterfly Papilio xuthus, and demonstrated that the protein is involved in the visual cycle. We now have localized the protein in the Papilio eye by light and electron microscopic immunohistochemistry using a monospecific antiserum produced against artificially expressed Papilio RBP. We found strong immunoreactivity in the primary as well as secondary pigment cells and in the tracheal cells. The pigment cells have long been regarded as an important site of the visual cycle, and this view is further supported by the present result. Interestingly, the cytoplasm and nuclei of these cells were equally labeled, indicating that the protein exists in both the cytoplasm and the nucleus. We conducted a survey for the existence of the Papilio RBP-like proteins in other insects including several species of butterflies, dragonflies, cicadas, grasshoppers and honeybees. Anti-Papilio RBP immunoreactivity was confirmed in the proteins isolated only from butterflies belonging to the superfamily Papilionoidea and not from other species. In all insects tested, however, fluorescing proteins were clearly detected, suggesting that these insects also have similar retinol-binding proteins.

An essential role of Rab5 in uniformity of synaptic vesicle size.

Rab5 small GTPase is a famous regulator of endocytic vesicular transport from plasma membrane to early endosomes. In neurons, Rab5 is found not only on endocytic vesicles in cell bodies but also on synaptic vesicles in nerve terminals. However, the function of Rab5 on synaptic vesicles remains unclear. Here, we elucidate the function of Rab5 on synaptic vesicles with in vivo and in vitro experiments using Drosophila photoreceptor cells. Functional inhibition of Rab5 with Rab5N142I, a dominant negative version of Drosophila Rab5, induced enlargement of synaptic vesicles. This enlargement was, however, suppressed by enhancing synaptic vesicle recycling under light illumination. In addition, synaptic vesicles prepared from Rab5N142I-expressing flies exhibited homotypic fusion in vitro. These results indicate that Rab5 functions to keep the size of synaptic vesicles uniform by preventing their homotypic fusion. By contrast, Rab5 was not involved in the endocytic reformation of synaptic vesicles, contrary to expectation from its conventional function. Furthermore, we electrophysiologically and behaviourally showed that the function of Rab5 is essential for efficient signal transmission across synapses.

A novel retinol-binding protein in the retina of the swallowtail butterfly, Papilio xuthus.

Retinoid-binding proteins are indispensable for visual cycles in both vertebrate and invertebrate retinas. These proteins stabilize and transport hydrophobic retinoids in the hydrophilic environment of plasma and cytoplasm, and allow regeneration of visual pigments. Here, we identified a novel retinol-binding protein in the eye of a butterfly, Papilio xuthus. The protein that we term Papilio retinol-binding protein (Papilio RBP) is a major component of retinal soluble proteins and exclusively binds 3-hydroxyretinol, and emits fluorescence peaking at 480 nm under ultraviolet (UV) illumination. The primary structure, deduced from the nucleotide sequence of the cDNA, shows no similarity to any other lipophilic ligand-binding proteins. The molecular mass and isoelectric point of the protein estimated from the amino-acid sequence are 26.4 kDa and 4.92, respectively. The absence of any signal sequence for secretion in the N-terminus suggests that the protein exists in the cytoplasmic matrix. All-trans 3-hydroxyretinol is the major ligand of the Papilio RBP in dark-adapted eyes. Light illumination of the eyes increases the 11-cis isomer of the ligand and induces redistribution of the Papilio RBP from the proximal to the distal part of the photoreceptor layer. These results suggest that the Papilio RBP is involved in visual pigment turnover.

Molecular and functional characterization of a unique Rab protein, RABRP1, containing the WDIAGQE sequence in a GTPase motif.

Rab proteins of the small G-protein superfamily are known to be involved in intracellular vesicle transport. Here, we describe the unique characteristics of a novel Rab protein, RABRP1 (Rab-Related Protein 1). The Drosophila RabRP1 gene is mainly transcribed in the eyes and testes, where the 3-kb and 1.5-kb mRNAs, respectively, are the predominant gene products. The amino-acid sequence deduced from the longer cDNA indicated that the C-terminal 1/3 of the sequence shares homology with Rab proteins, whereas the rest of the peptide shows no significant homology with any other proteins. Immunoblot analysis using antiserum against the Rab-domain indicated that the multiple translates (94 k, 53 k, 30 k, 29 k and 27 k) were expressed in the eyes. In contrast, only smaller peptides (30 k, 29 k and 27 k) were identified in the testes. Molecular phylogenetic analysis revealed that RABRP1 forms a subgroup with Dictiostelium RabE and mammalian Rab29, Rab32, Rab38 proteins, whose functions have not been identified yet. RABRP1 and its relatives were characterized by the amino acid substitution occurring in the conserved GTP-binding motifs. Immunohistochemical studies demonstrated that RABRP1 was localized on the subrhabdomeric cisternae of photoreceptor cells and on the pigment granules in photoreceptor and pigment cells in the retina. The expression of the dominant negative RABRP1 caused the abnormal accumulation of autophagosome-like vesicles. These data suggest that RABRP1 is involved in the lysosomal vesicle transport pathway, including the biogenesis or degradation of pigment granules.

DN-cadherin is required for spatial arrangement of nerve terminals and ultrastructural organization of synapses.

We studied roles of DN-cadherin, the Drosophila major neuronal cadherin, in neuronal connections in the visual system. In DN-cadherin mutants, axon terminals of a large subset of photoreceptor cells reached and associated with their target interneurons, but their characteristic spatial arrangement was disrupted as synaptogenesis proceeded. Although synapses were formed at contact sites between the axon terminals and target neurons, underlying cytoplasmic structures were not fully specialized at both pre- and postsynaptic terminals and synaptic vesicles appeared to accumulate at the presynapses. These results suggest that the cadherin adhesion system is required for interaction between pre- and postsynaptic terminals and for generation of the mature synaptic structures.