Spirituality in the work of Theodore Roszak : implications for contemporary ecopsychology

Despite the recent flourishing of ecopsychology research, risks may be involved if ecopsychology remains a loosely defined paradigm. We suggest that drawing from some of the central themes of Theodore Roszak’s The Voice of the Earth (1992), a seminal text of ecopsychology, may help to elucidate the unique contribution of ecopsychology and its sustained relevance for environmentally focused psychologies. To provide a comprehensive review, we consider The Voice of the Earth by placing this text in the context of Roszak’s broader body of literature, discussing his earlier and more recent works. We particularly focus on the theme of spiritual experience throughout Roszak’s literature, as we believe that this is one of the more unique and important aspects of his work that has implications for the future development of ecopsychology as a paradigm and social movement. In conclusion, we suggest that Roszak’s emphasis on the value of a spiritual or animistic experience of nature, as a means of fostering empathy toward the natural world, may assist in providing meaningful focus to contemporary ecopsychology

“Savage beasts,” “great companions”: the first dogs to winter on the Antarctic continent

By investigating the nature of the social interactions between “sledge dogs” and explorers in the first land-based exploration in Antarctica, this research contributes to an animal-human perspective in Antarctic historical studies. Consideration of the interspecies interactions provide further insight into attitudes to nonhuman animal welfare, including towards wildlife, at the turn of the twentieth century. The companionship of favored animals appeared to have alleviated some of the stresses of isolation and confinement in the inhospitable Antarctic environment

A pan-influenza antibody inhibiting neuraminidase via receptor mimicry

Acknowledgements: We thank NanoImaging Services for some of the Cryo-EM data collection and processing; S. A. Kristian and R. Ray (GSK) for their critical reading and scientific insights; the NIBSC and IRR for providing seasonal influenza viruses; and X. Yang, D. E. Root and O. Bare at the Genetic Perturbation Platform (GPP) of the Broad Institute of MIT and Harvard for assistance with the deep mutational scanning library construction, sequencing and variant calling.Rapidly evolving influenza A viruses (IAVs) and influenza B viruses (IBVs) are major causes of recurrent lower respiratory tract infections. Current influenza vaccines elicit antibodies predominantly to the highly variable head region of haemagglutinin and their effectiveness is limited by viral drift1 and suboptimal immune responses2. Here we describe a neuraminidase-targeting monoclonal antibody, FNI9, that potently inhibits the enzymatic activity of all group 1 and group 2 IAVs, as well as Victoria/2/87-like, Yamagata/16/88-like and ancestral IBVs. FNI9 broadly neutralizes seasonal IAVs and IBVs, including the immune-evading H3N2 strains bearing an N-glycan at position 245, and shows synergistic activity when combined with anti-haemagglutinin stem-directed antibodies. Structural analysis reveals that D107 in the FNI9 heavy chain complementarity-determinant region 3 mimics the interaction of the sialic acid carboxyl group with the three highly conserved arginine residues (R118, R292 and R371) of the neuraminidase catalytic site. FNI9 demonstrates potent prophylactic activity against lethal IAV and IBV infections in mice. The unprecedented breadth and potency of the FNI9 monoclonal antibody supports its development for the prevention of influenza illness by seasonal and pandemic viruses

A pan-influenza antibody inhibiting neuraminidase via receptor mimicry.

Acknowledgements: We thank NanoImaging Services for some of the Cryo-EM data collection and processing; S. A. Kristian and R. Ray (GSK) for their critical reading and scientific insights; the NIBSC and IRR for providing seasonal influenza viruses; and X. Yang, D. E. Root and O. Bare at the Genetic Perturbation Platform (GPP) of the Broad Institute of MIT and Harvard for assistance with the deep mutational scanning library construction, sequencing and variant calling.Rapidly evolving influenza A viruses (IAVs) and influenza B viruses (IBVs) are major causes of recurrent lower respiratory tract infections. Current influenza vaccines elicit antibodies predominantly to the highly variable head region of haemagglutinin and their effectiveness is limited by viral drift1 and suboptimal immune responses2. Here we describe a neuraminidase-targeting monoclonal antibody, FNI9, that potently inhibits the enzymatic activity of all group 1 and group 2 IAVs, as well as Victoria/2/87-like, Yamagata/16/88-like and ancestral IBVs. FNI9 broadly neutralizes seasonal IAVs and IBVs, including the immune-evading H3N2 strains bearing an N-glycan at position 245, and shows synergistic activity when combined with anti-haemagglutinin stem-directed antibodies. Structural analysis reveals that D107 in the FNI9 heavy chain complementarity-determinant region 3 mimics the interaction of the sialic acid carboxyl group with the three highly conserved arginine residues (R118, R292 and R371) of the neuraminidase catalytic site. FNI9 demonstrates potent prophylactic activity against lethal IAV and IBV infections in mice. The unprecedented breadth and potency of the FNI9 monoclonal antibody supports its development for the prevention of influenza illness by seasonal and pandemic viruses

A pan-influenza antibody inhibiting neuraminidase via receptor mimicry

Acknowledgements: We thank NanoImaging Services for some of the Cryo-EM data collection and processing; S. A. Kristian and R. Ray (GSK) for their critical reading and scientific insights; the NIBSC and IRR for providing seasonal influenza viruses; and X. Yang, D. E. Root and O. Bare at the Genetic Perturbation Platform (GPP) of the Broad Institute of MIT and Harvard for assistance with the deep mutational scanning library construction, sequencing and variant calling.Rapidly evolving influenza A viruses (IAVs) and influenza B viruses (IBVs) are major causes of recurrent lower respiratory tract infections. Current influenza vaccines elicit antibodies predominantly to the highly variable head region of haemagglutinin and their effectiveness is limited by viral drift1 and suboptimal immune responses2. Here we describe a neuraminidase-targeting monoclonal antibody, FNI9, that potently inhibits the enzymatic activity of all group 1 and group 2 IAVs, as well as Victoria/2/87-like, Yamagata/16/88-like and ancestral IBVs. FNI9 broadly neutralizes seasonal IAVs and IBVs, including the immune-evading H3N2 strains bearing an N-glycan at position 245, and shows synergistic activity when combined with anti-haemagglutinin stem-directed antibodies. Structural analysis reveals that D107 in the FNI9 heavy chain complementarity-determinant region 3 mimics the interaction of the sialic acid carboxyl group with the three highly conserved arginine residues (R118, R292 and R371) of the neuraminidase catalytic site. FNI9 demonstrates potent prophylactic activity against lethal IAV and IBV infections in mice. The unprecedented breadth and potency of the FNI9 monoclonal antibody supports its development for the prevention of influenza illness by seasonal and pandemic viruses