Building the Leviathan : voluntary centralisation of punishment power sustains cooperation in humans

The prevalence of cooperation among humans is puzzling because cooperators can be exploited by free riders. Peer punishment has been suggested as a solution to this puzzle, but cumulating evidence questions its robustness in sustaining cooperation. Amongst others, punishment fails when it is not powerful enough, or when it elicits counter-punishment. Existing research, however, has ignored that the distribution of punishment power can be the result of social interactions. We introduce a novel experiment in which individuals can transfer punishment power to others. We find that while decentralised peer punishment fails to overcome free riding, the voluntary transfer of punishment power enables groups to sustain cooperation. This is achieved by non-punishing cooperators empowering those who are willing to punish in the interest of the group. Our results show how voluntary power centralisation can efficiently sustain cooperation, which could explain why hierarchical power structures are widespread among animals and humans

Dogs (Canis familiaris), but Not Chimpanzees (Pan troglodytes), Understand Imperative Pointing

Chimpanzees routinely follow the gaze of humans to outside targets. However, in most studies using object choice they fail to use communicative gestures (e.g. pointing) to find hidden food. Chimpanzees' failure to do this may be due to several difficulties with this paradigm. They may, for example, misinterpret the gesture as referring to the opaque cup instead of the hidden food. Or perhaps they do not understand informative communicative intentions. In contrast, dogs seem to be skilful in using human communicative cues in the context of finding food, but as of yet there is not much data showing whether they also use pointing in the context of finding non-food objects. Here we directly compare chimpanzees' (N = 20) and dogs' (N = 32) skills in using a communicative gesture directed at a visible object out of reach of the human but within reach of the subject. Pairs of objects were placed in view of and behind the subjects. The task was to retrieve the object the experimenter wanted. To indicate which one she desired, the experimenter pointed imperatively to it and directly rewarded the subject for handing over the correct one. While dogs performed well on this task, chimpanzees failed to identify the referent. Implications for great apes' and dogs' understanding of human communicative intentions are discussed

Clearance of Genotype 1b Hepatitis C Virus in Chimpanzees in the Presence of Vaccine-Induced E1-Neutralizing Antibodies

Accumulating evidence indicates that neutralizing antibodies play an important role in protection from chronic hepatitis C virus (HCV) infection. Efforts to elicit such responses by immunization with intact heterodimeric E1E2 envelope proteins have met with limited success. To determine whether antigenic sites, which are not exposed by the combined E1E2 heterodimer structure, are capable of eliciting neutralizing antibody responses, we expressed and purified each as separate recombinant proteins E1 and E2, from which the immunodominant hypervariable region (HVR-1) was deleted. Immunization of chimpanzees with either E1 or E2 alone induced antigen-specific T-helper cytokines of similar magnitude. Unexpectedly, the capacity to neutralize HCV was observed in E1 but not in animals immunized with E2 devoid of HVR-1. Furthermore, in vivo only E1-vaccinated animals exposed to the heterologous HCV-1b inoculum cleared HCV infection

The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90

Tetratricopeptide (TPR) domains are known protein interaction domains. We show that the TPR domain of FKBP8 selectively binds Hsp90, and interactions upstream of the conserved MEEVD motif are critical for tight binding. In contrast FKBP8 failed to bind intact Hsp70. The PPIase domain was not essential for the interaction with Hsp90 and binding was completely encompassed by the TPR domain alone. The conformation adopted by Hsp90 peptides, containing the conserved MEEVD motif, in the crystal structure were similar to that seen for the TPR domains of CHIP, AIP and Tah1. The carboxylate clamp interactions with bound Hsp90 peptide were a critical component of the interaction and mutation of Lys 307, involved in the carboxylate clamp, completely disrupted the interaction with Hsp90. FKBP8 binding to Hsp90 did not substantially influence its ATPase activity

Space Charge at Nanoscale: Probing Injection and Dynamic Phenomena Under Dark/Light Configurations by Using KPFM and C-AFM

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