REVIEW: Downhome: Dispatches from Dixie

Review of the non-fiction book Downhome: Dispatches from Dixie, by Bob Dart

Participatory development projects in the Andes - looking for empowerment with Q-Methodology

This is about the first steps in a study on poverty alleviation and the question whether participatory interventions make a significant contribution to the empowerment of poor Andean farmers. Participatory methods of intervention have been applied now for many years in many development projects, based on the philosophy that development will not be sustainable if the “end-users” of so called “beneficiaries” are not appropriately involved and participating in the projects. The process of active participation is supposed to empower the people involved and improve their personal development which at the same time is often considered to be as important for poverty alleviation as a good economic return of a development project. Q-Methodology is used in order to achieve better insight into the subjective nature of this famous factor “empowerment”, which is considered important even by the World Bank now. (Narayan D., 2002) The subjective reality of a person is a functional reality, it is often much more functional than the external “objective” reality, because it is what people perceive and what makes up their life. With Q-Methodology people can be grouped into “factors” (groups of people) with different functional realities, with different perceptions of “reality”, with different reactions within certain situations. The thesis is that if people get “empowered” by an intervention of a project, at least their inner, subjective reality is supposed to change, even if their external reality might not change substantially yet. Therefore people in several different places in the Peruvian Andes are assessed with Q-Methodology before and after intervention of two different types of projects and changes shall be tracked. At this stage there only exist the data “before-intervention”, the interviews “after-intervention” will take place next. The projects mentioned are FAO Farmer Field Schools near Huancayo, central part of Peru and the Rural Sanitation Program SANBASUR near Cusco, more in the South of Peru. In Huancayo the study includes 88 persons, 51 project participants and 37 test persons (non participants); in Cusco the study is including 77 project participants and 77 nonparticipants. First analyses of the baseline data are on the way

The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5alpha

Rhesus TRIM5alpha (rhTRIM5alpha) potently restricts replication of human immunodeficiency virus type 1 (HIV-1). Restriction is mediated through direct binding of the C-terminal B30.2 domain of TRIM5alpha to the assembled HIV-1 capsid core. This host-pathogen interaction involves multiple capsid molecules within the hexagonal HIV-1 capsid lattice. However, the molecular details of this interaction and the precise site at which the B30.2 domain binds remain largely unknown. The human orthologue of TRIM5alpha (hsTRIM5alpha) fails to block infection by HIV-1 both in vivo and in vitro This is thought to be due to differences in binding to the capsid lattice. To map the species-specific binding surface on the HIV-1 capsid lattice, we used microscale thermophoresis and dual-focus fluorescence correlation spectroscopy to measure binding affinity of rhesus and human TRIM5alpha B30.2 domains to a series of HIV-1 capsid variants that mimic distinct capsid arrangements at each of the symmetry axes of the HIV-1 capsid lattice. These surrogates include previously characterized capsid oligomers, as well as a novel chemically cross-linked capsid trimer that contains cysteine substitutions near the 3-fold axis of symmetry. The results demonstrate that TRIM5alpha binding involves multiple capsid molecules along the 2-fold and 3-fold interfaces between hexamers and indicate that the binding interface at the 3-fold axis contributes to the well-established differences in restriction potency between TRIM5alpha orthologues. IMPORTANCE TRIM5alpha is a cellular protein that fends off infection by retroviruses through binding to the viruses\u27 protein shell surrounding its genetic material. This shell is composed of several hundred capsid proteins arranged in a honeycomb-like hexagonal pattern that is conserved across retroviruses. By binding to the complex lattice formed by multiple capsid proteins, rather than to a single capsid monomer, TRIM5alpha restriction activity persists despite the high mutation rate in retroviruses such as HIV-1. In rhesus monkeys, but not in humans, TRIM5alpha confers resistance to HIV-1. By measuring the binding of human and rhesus TRIM5alpha to a series of engineered HIV-1 capsid mimics of distinct capsid lattice interfaces, we reveal the HIV-1 capsid surface critical for species-specific binding by TRIM5alpha

In vivo and in vitro protein ligation by naturally occurring and engineered split DnaE inteins

Peer reviewe