Finishing the euchromatic sequence of the human genome

The sequence of the human genome encodes the genetic instructions for human physiology, as well as rich information about human evolution. In 2001, the International Human Genome Sequencing Consortium reported a draft sequence of the euchromatic portion of the human genome. Since then, the international collaboration has worked to convert this draft into a genome sequence with high accuracy and nearly complete coverage. Here, we report the result of this finishing process. The current genome sequence (Build 35) contains 2.85 billion nucleotides interrupted by only 341 gaps. It covers ∼99% of the euchromatic genome and is accurate to an error rate of ∼1 event per 100,000 bases. Many of the remaining euchromatic gaps are associated with segmental duplications and will require focused work with new methods. The near-complete sequence, the first for a vertebrate, greatly improves the precision of biological analyses of the human genome including studies of gene number, birth and death. Notably, the human enome seems to encode only 20,000-25,000 protein-coding genes. The genome sequence reported here should serve as a firm foundation for biomedical research in the decades ahead

Proceedings of the Thirteenth International Society of Sports Nutrition (ISSN) Conference and Expo

Meeting Abstracts: Proceedings of the Thirteenth International Society of Sports Nutrition (ISSN) Conference and Expo Clearwater Beach, FL, USA. 9-11 June 201

Antigenic variation in the outer membrane proteins of Neisseria meningitidis and the suitability of the H.8 antigen for use in immunisation against meningococcal disease

Inter- and intra-strain variation in the surface-exposed proteins of N. meningitidis was investigated in order to compare the variability with that which had been reported for the closely-related N. gonorrhoeae and to identify antigens possessing conserved epitopes which were stably expressed by the bacteria. Radioimmune precipitation, SDS-PAGE of surface radioiodinated disease isolates and isolated outer membrane vesicles, and western blotting techniques demonstrated variability in the major outer membrane proteins and pilin both between strains and during the course of infection. Several monoclonal antibodies recognised an antigen which was common to all pathogenic Neisseriae, and absent from most commensal organisms. The stable expression of this antigen suggested that it might have an important role in pathogenesis and made it an attractive choice for further study. The pathogenic Neisseria antigen was shown to have unusual properties which, together with its peculiarity to pathogenic species and apparent molecular mass range, it shared with the H.8 antigen found by Cannon and coworkers (Infection and Immunity, (1984), 43 ,994-999). Further similarities have confirmed that these are the same protein. Two published methods for purification of the antigen were investigated: Gel filtration followed by ion exchange chromatography, or extraction into phenol, precipitation of lipopolysaccharide, and lipophilic gel filtration followed by reverse-phase HPLC. However, better results were obtained after development of an affinity chromatography system with an anti-H.8 monoclonal antibody immobilised on a cyanogen bromide-sepharose column. Due to difficulties in staining the antigen after SDS-PAGE a quantitative spot blot assay was developed for its detection, based on the ELISA principle. Amino acid analysis showed the antigen to be rich in alanine, glutamine, and proline and lacking in sulphur-containing amino acids. Immunisation of mice with purified antigen from one strain of meningococcus produced antisera reactive with the H.8 antigens of the homologous and heterologous strains. However, this serum and the H.8-directed monoclonal antibodies were ineffective in an in vitro complement-mediated bactericidal assay. Initial experiments showed poor opsonic activity for a monoclonal antibody. Synthetic oligopeptides corresponding to regions of the primary sequence of the H.8 antigen were used to define the epitopes recognised by the serum and monoclonal antibodies. Since neither polyclonal sera nor monoclonal antibodies directed against a variety of epitopes showed biological activity it appears that immunisation with the H.8 antigen would not elicit protection against meningococcal disease.</p

European Radioisotope Thermoelectric Generators (RTGs) and Radioisotope Heater Units (RHUs) for Space Science and Exploration

Radioisotope power systems utilising americium-241 as a source of heat have been under development in Europe as part of a European Space Agency funded programme since 2009. The aim is to develop all of the building blocks that would enable Europe to launch and operate deep space and planetary missions in environments where use of solar power or alternative power generation technologies is challenging. Although some technical and policy work activity predate the ESA programme, the maturity of the technology has now reached a level that it can be incorporated in mission studies and roadmaps targeting the period from the mid 2020s onwards. This paper describes the state of the art in European radioisotope thermoelectric generators and radioisotope heater units. This paper includes: the evolution of the technical programme in detail; descriptions of the design; evolution of RTG and RHU devices from laboratory prototypes to more advanced fully functional systems; and experimental data obtained to date. This paper also outlines the technical challenges and multidisciplinary skills required to develop what is a world leading, original, significant and transformative technology solution for planetary science and exploration missions from the mid 2020s onwards.JRC.G.I.3-Nuclear Fuel Safet