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Traffic accidents resulting from driving behavior and road conditions are crucial problems for drivers. The causes and responses to traffic accidents have been widely studied by researchers. Whereas several approaches have been proposed to ease these problems, most works entail high computational costs or rigid hardware conditions. To address these challenges, we propose Health Driving, a smartphone-based system for detecting driving events and road conditions solely with a built-in smartphone acceleration sensor. More specifically, we first collect acceleration data from the acceleration sensor of a smartphone on a vehicle, and then utilize an acceleration reorientation calibration algorithm to convert the obtained acceleration data from the smartphone to acceleration data of the vehicle. Finally, we exploit Health Driving to detect driving events and road conditions, and evaluate the seriousness of the road conditions and driving events by using an efficient scoring mechanism based on the ISO 2631 standard. An extensive evaluation demonstrates that Health Driving operates successfully with an ordinary smartphone, and operates with a low computational cost compared with other methods. Copyright © 2016 John Wiley & Sons, Ltd. [ABSTRACT FROM AUTHOR]

MicroRNAs (miRNAs) can impact viral infections by binding to sequences with partial complementarity on viral RNA transcripts, usually resulting in the repression of virus replication. In the present study, we identified a potential binding site for miR-130 in the 5′ untranslated region (bps 155-162) of the porcine reproductive and respiratory syndrome virus (PRRSV) genome. We found that the delivery of multiple miR-130 family mimics, especially miR-130b, resulted in inhibition of PRRSV replication in vitro. miR-130 was effective in inhibiting the replication of multiple type 2 PRRSV strains, but not against vSHE, a classical type 1 strain. miR-130 over-expression did not induce IFN-α or TNF-α expression in either uninfected or PRRSV-infected porcine alveolar macrophages. Results from luciferase reporter assays indicated that miR-130 directly targeted the PRRSV 5′ UTR. Intranasal inoculation of piglets with miR-130b exhibited antiviral activity in vivo and partially protected piglets from an otherwise lethal challenge with HP-PRRSV strain vJX143. Overall, these results demonstrate the importance of the miR-130 family in modulating PRRSV replication and also provide a scientific basis for using cellular miRNAs in anti-PRRSV therapies. [ABSTRACT FROM AUTHOR]

The African clawed frog, Xenopus laevis , is a model species for amphibians. Before metamorphosis, tadpoles do not efficiently express the single classical MHC class I (MHC-I) molecule Xela -UAA, but after metamorphosis, adults express this molecule in abundance. To elucidate the Ag-presenting mechanism of Xela -UAA, in this study, the Xela -UAA structure complex (p Xela -UAAg) bound with a peptide from a synthetic random peptide library was determined. The amino acid homology between the Xela -UAA and MHC-I sequences of different species is <45%, and these differences are fully reflected in the three-dimensional structure of p Xela -UAAg. Because of polymorphisms and interspecific differences in amino acid sequences, p Xela -UAAg forms a distinct peptide-binding groove and presents a unique peptide profile. The most important feature of p Xela -UAAg is the two-amino acid insertion in the α2-helical region, which forms a protrusion of ∼3.8 Å that is involved in TCR docking. Comparison of peptide-MHC-I complex (pMHC-I) structures showed that only four amino acids in β2-microglobulin that were bound to MHC-I are conserved in almost all jawed vertebrates, and the most unique feature in nonmammalian pMHC-I molecules is that the AB loop bound β2-microglobulin. Additionally, the binding distance between pMHC-I and CD8 molecules in nonmammals is different from that in mammals. These unique features of p Xela -UAAg provide enhanced knowledge of T cell immunity and bridge the knowledge gap regarding the coevolutionary progression of the MHC-I complex from aquatic to terrestrial species., (Copyright © 2019 by The American Association of Immunologists, Inc.)