From foot-draggers to strategic counter-partners : the dynamics of U.S. and Chinese policies for tackling climate change

As can been seen from the U.S.'s non-ratification of the Kyoto Protocol, together with the negotiations toward the post-Kyoto Protocol framework, the U.S. and China have been quarrelling over their responsibilities and have contradicted one another over the introduction of compulsory domestic greenhouse gases emission reduction targets. Therefore, for a long time, it has been argued that the controversy between the two countries has hindered the process of forging an international agreement to deal with climate change. On the other hand, Sino-U.S. bilateral cooperation on climate change has significantly increased in recent years in summit talks and their Strategic & Economic Dialogue (S&ED), especially after the 15th Conference of Parties (COP) of the United Nations Framework Convention on Climate Change (UNFCCC) in Copenhagen, one of whose aims was to facilitate positive negotiations for the post-Kyoto Protocol agreement. Analyzing this in the light of recent developments, we find that the U.S. and China have tended to address climate change and related issues from a pluralistic viewpoint and approach, by regarding the achievement of bilateral cooperation and global agreements as their common strategic objective.

PDR with a foot-mounted IMU and ramp detection

The localization of persons in indoor environments is nowadays an open problem. There are partial solutions based on the deployment of a network of sensors (Local Positioning Systems or LPS). Other solutions only require the installation of an inertial sensor on the person’s body (Pedestrian Dead-Reckoning or PDR). PDR solutions integrate the signals coming from an Inertial Measurement Unit (IMU), which usually contains 3 accelerometers and 3 gyroscopes. The main problem of PDR is the accumulation of positioning errors due to the drift caused by the noise in the sensors. This paper presents a PDR solution that incorporates a drift correction method based on detecting the access ramps usually found in buildings. The ramp correction method is implemented over a PDR framework that uses an Inertial Navigation algorithm (INS) and an IMU attached to the person’s foot. Unlike other approaches that use external sensors to correct the drift error, we only use one IMU on the foot. To detect a ramp, the slope of the terrain on which the user is walking, and the change in height sensed when moving forward, are estimated from the IMU. After detection, the ramp is checked for association with one of the existing in a database. For each associated ramp, a position correction is fed into the Kalman Filter in order to refine the INS-PDR solution. Drift-free localization is achieved with positioning errors below 2 meters for 1,000-meter-long routes in a building with a few ramps.

Accurate pedestrian indoor navigation by tightly coupling foot-mounted IMU and RFID measurements

We present a new method to accurately locate persons indoors by fusing inertial navigation system (INS) techniques with active RFID technology. A foot-mounted inertial measuring units (IMUs)-based position estimation method, is aided by the received signal strengths (RSSs) obtained from several active RFID tags placed at known locations in a building. In contrast to other authors that integrate IMUs and RSS with a loose Kalman filter (KF)-based coupling (by using the residuals of inertial- and RSS-calculated positions), we present a tight KF-based INS/RFID integration, using the residuals between the INS-predicted reader-to-tag ranges and the ranges derived from a generic RSS path-loss model. Our approach also includes other drift reduction methods such as zero velocity updates (ZUPTs) at foot stance detections, zero angular-rate updates (ZARUs) when the user is motionless, and heading corrections using magnetometers. A complementary extended Kalman filter (EKF), throughout its 15-element error state vector, compensates the position, velocity and attitude errors of the INS solution, as well as IMU biases. This methodology is valid for any kind of motion (forward, lateral or backward walk, at different speeds), and does not require an offline calibration for the user gait. The integrated INS+RFID methodology eliminates the typical drift of IMU-alone solutions (approximately 1% of the total traveled distance), resulting in typical positioning errors along the walking path (no matter its length) of approximately 1.5 m.

A retro-inverso peptide corresponding to the GH loop of foot-and-mouth disease virus elicits high levels of long-lasting protective neutralizing antibodies

Peptides corresponding to the immunodominant loop located at residues 135–158 on capsid protein VP1 of foot-and-mouth disease virus (FMDV) generally elicit high levels of anti-peptide and virus-neutralizing antibodies. In some instances, however, the level of neutralizing antibodies is low or even negligible, even though the level of anti-peptide antibodies is high. We have shown previously that the antigenic activity of peptide 141–159 of VP1 of a variant of serotype A can be mimicked by a retro-inverso (all-d retro or retroenantio) peptide analogue. This retro-inverso analogue induced greater and longer-lasting antibody titers than did the corresponding l-peptide. We now show that a single inoculation of the retro-inverso analogue elicits high levels of neutralizing antibodies that persist longer than those induced against the corresponding l-peptide and confer substantial protection in guinea pigs challenged with the cognate virus. In view of the high stability to proteases of retro-inverso peptide analogues and their enhanced immunogenicity, these results have practical relevance in designing potential peptide vaccines.

Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus.

To gain entry into cells, viruses utilize a variety of different cell-surface molecules. Foot-and-mouth disease virus (FMDV) binds to cell-surface integrin molecules via an arginine-glycine-aspartic acid (RGD) sequence in capsid protein VP1. Binding to this particular cell-surface molecule influences FMDV tropism, and virus/receptor interactions appear to be responsible, in part, for selection of antigenic variants. To study early events of virus-cell interaction, we engineered an alternative and novel receptor for FMDV. Specifically, we generated a new receptor by fusing a virus-binding, single-chain antibody (scAb) to intracellular adhesion molecule 1 (ICAM1). Cells that are normally not susceptible to FMDV infection became susceptible after being transfected with DNA encoding the scAb/ICAM1 protein. An escape mutant (B2PD.3), derived with the mAb used to generate the genetically engineered receptor, was restricted for growth on the scAb/ICAM1 cells, but a variant of B2PD.3 selected by propagation on scAb/ICAM1 cells grew well on these cells. This variant partially regained wild-type sequence in the epitope recognized by the mAb and also regained the ability to be neutralize by the mAb. Moreover, RGD-deleted virions that are noninfectious in animals and other cell types grew to high titers and were able to form plaques on scAb/ ICAM1 cells. These studies demonstrate the first production of a totally synthetic cell-surface receptor for a virus. This novel approach will be useful for studying virus reception and for the development of safer vaccines against viral pathogens of animals and humans.

Equine rhinovirus 1 is more closely related to foot-and-mouth disease virus than to other picornaviruses.

Equine rhinovirus 1 (ERhV1) is a respiratory pathogen of horses which has an uncertain taxonomic status. We have determined the nucleotide sequence of the ERhV1 genome except for a small region at the 5' end. The predicted polyprotein was encoded by 6741 nucleotides and possessed a typical picornavirus proteolytic cleavage pattern, including a leader polypeptide. The genomic structure and predicted amino acid sequence of ERhV1 were more similar to those of foot-and-mouth disease viruses (FMDVs), the only members of the aphthovirus genus, than to those of other picornaviruses. Features which were most similar to FMDV included a 16-amino acid 2A protein which was 87.5% identical in sequence of FMDV 2A, a leader (L) protein similar in size to FMDV Lab and the possibility of a truncated L protein similar in size to FMDV Lb, and a 3C protease which recognizes different cleavage sites. However, unlike FMDV, ERhV1 had only one copy of the 3B (VPg) polypeptide. The phylogenetic relationships of the ERhV1 sequence and nucleotide sequences of representative species of the five genera of the family Picornaviridae were examined. Nucleotide sequences coding for the complete polyprotein, the RNA polymerase, and VP1 were analyzed separately. The phylogenetic trees confirmed that ERhV1 was more closely related to FMDV than to other picornaviruses and suggested that ERhV1 may be a member, albeit very distant, of the aphthovirus genus.