Recombinant HEV NS3 protein (Ochlerotatus)

This paper presents a sub-optimal energy management strategy, based on Stochastic Dynamic Programming (SDP), for efficient powersplit of a Hybrid Electric Vehicle (HEV). An optimal energy management strategy is proposed, permitting to have simultaneous speed profile and powersplit optimization of the HEV. Formulated as a multi-objective optimization problem, an epsilon-constraint method has been used to find the Pareto front of the energy optimization task. Traffic conditions and driver behavior could be assimilated to a stochastic nature, thus, it is proposed in this paper to address the vehicle power as Markov Decision Process. A Stochastic Database is used to store Transition Probability and Reward Matrices, corresponding to suitable vehicle actions w.r.t. specific states. They are used afterwards to calculate sub-optimal powersplit policy for the vehicle via an infinite-horizon SDP approach. Simulation results demonstrate the effectiveness of the proposed approach compared to a deterministic strategy given in [1]. The present work is conducted on a dedicated high-fidelity model of the HEV that was developed on MATLAB/TruckMaker software.

Understanding the dynamics of host innate immune responses against a pathogen marks the first step toward developing intervention strategies against the pathogen. The cytosolic pattern recognition receptor retinoic acid-inducible gene I (RIG-I) has been shown to be the major innate immune sensor for hepatitis E virus (HEV). Here, we show that HEV capsid protein (ORF2), a 660 amino acid long protein, interferes with the RIG-I signaling. Interestingly, only the full length ORF2 protein but not the 112-608 ORF2 protein inhibited RIG-I dependent interferon response. Both synthetic agonist and virus induced RIG-I activation was modulated by ORF2. Interference of interferon response was confirmed by reporter assays involving different interferon inducible promoters, qRT PCR, ELISA, and immunofluorescence microscopy. Neither glycosylation nor dimerization of the ORF2 protein had any effect on the observed inhibition. Further analyses revealed that the ORF2 protein antagonized Toll-like receptor (TLR) pathways as well. ORF2 inhibited signaling by RIG-I and TLR adapters, IPS-1, MyD88, and TRIF but was unable to inhibit activation by ectopically expressed IRF3 suggesting that it may be acting at a site upstream of IRF3 and downstream of adapter proteins. Our data uncover a new mechanism by which HEV may interfere with the host antiviral signaling.