Anthropologie générale

Jean Jamin et Jean-Marie Schaeffer, directeurs d’étudesavec François Flahault, directeur de recherche au CNRS Anthropologie générale : qu’est-ce qu’un être humain ? Le séminaire, qui s’est ouvert cette année, a pour but de contrebalancer la logique de spécialisation qui aboutit à évacuer la question « Qu’est-ce que l’homme ? », celle-ci apparaissant trop générale pour les sciences humaines et trop empirique pour la philosophie. Contrebalancer également l’idée qu’« il n’y a pas de nature humai..

'My first 48 hours out' : drug users’ perspectives on challenges and strategies upon release from prison

Background Prisoners report much higher prevalence rates of drug use and more harmful consumption patterns than the general population. People who use drugs have above-average experiences with the criminal justice system in general, and the prison system and subsequent release situations in particular. Release from prison is associated with increased mortality rates among drug users due to the risk of overdose. The EU-funded project 'My first 48 hours out' aimed to address the gaps in continuity of care for long-term drug users in prison and upon release, with a special focus on drug user's perspectives on needs and challenges upon release. Methods A multi-country (Belgium, France, Germany and Portugal) qualitative study was set up to explore drug users' perceptions of drug use and risk behaviour upon prison release, experiences of incarceration and release, and strategies to avoid risks when being released. In total, 104 prisoners and recently released persons with a history of drug use participated in semi-structured interviews and focus groups discussions on these topics. Results Respondents pointed out that there are numerous challenges for people who use drugs when released from prison. Lack of stable housing and employment support were frequently mentioned, as well as complex administrative procedures regarding access to services, health insurance and welfare benefits. Besides structural challenges, individual issues may challenge social reintegration like 'old habits', mental health problems and disrupted social networks. As a result, (ex-)prisoners adopt individual strategies to cope with the risks and challenges at release. Conclusion Measures to prepare prisoners for release often do not focus on the individual and specific challenges of persons who use drugs. Psychosocial and medical support need to be improved and adjusted to drug users' needs inside and outside prison. To improve the quality and continuity of care around release, the perspectives and coping strategies of people who use drugs should be used to better address their needs and barriers to treatment

Orthoparamyxovirinae C Proteins Have a Common Origin and a Common Structural Organization

The protein C is a small viral protein encoded in an overlapping frame of the P gene in the subfamily Orthoparamyxovirinae. This protein, expressed by alternative translation initiation, is a virulence factor that regulates viral transcription, replication, and production of defective interfering RNA, interferes with the host-cell innate immunity systems and supports the assembly of viral particles and budding. We expressed and purified full-length and an N-terminally truncated C protein from Tupaia paramyxovirus (TupV) C protein (genus Narmovirus). We solved the crystal structure of the C-terminal part of TupV C protein at a resolution of 2.4 Å and found that it is structurally similar to Sendai virus C protein, suggesting that despite undetectable sequence conservation, these proteins are homologous. We characterized both truncated and full-length proteins by SEC-MALLS and SEC-SAXS and described their solution structures by ensemble models. We established a mini-replicon assay for the related Nipah virus (NiV) and showed that TupV C inhibited the expression of NiV minigenome in a concentration-dependent manner as efficiently as the NiV C protein. A previous study found that the Orthoparamyxovirinae C proteins form two clusters without detectable sequence similarity, raising the question of whether they were homologous or instead had originated independently. Since TupV C and SeV C are representatives of these two clusters, our discovery that they have a similar structure indicates that all Orthoparamyxovirine C proteins are homologous. Our results also imply that, strikingly, a STAT1-binding site is encoded by exactly the same RNA region of the P/C gene across Paramyxovirinae, but in different reading frames (P or C), depending on which cluster they belong to.French Agence Nationale de la RechercheFond de la Recherche Médicale (FRM)Grenoble Instruct-ERIC centerFRISBIUniversity Grenoble Alpes graduate school (Ecoles Universitaires de Recherche)Peer Reviewe

Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins

The high-molecular-mass penicillin-binding proteins (HMM-PBPs), present in the cytoplasmic membranes of all eubacteria, are involved in important physiological events such as cell elongation, septation or shape determination. Up to now it has, however, been very difficult or impossible to study the catalytic properties of the HMM-PBPs in vitro. With simple substrates, we could demonstrate that several of these proteins could catalyse the hydrolysis of some thioesters or the transfer of their acyl moiety on the amino group of a suitable acceptor nucleophile. Many of the acyl-donor substrates were hippuric acid or benzoyl-D-alanine derivatives, and their spectroscopic properties enabled a direct monitoring of the enzymic reaction. In their presence, the binding of radioactive penicillin to the PBPs was also inhibited