Structure solution of hydrogen bonded molecular solids from powder diffraction data

The crystal structures of 2,4,6-triisopropylbenzenesulfonamide and the 1:1 adduct of hexamethylenetetramine and 1,2,3-trihydroxybenzene have been solved from synchrotron and laboratory X-ray powder diffraction data respectively. The structures were solved by application of a direct space structure solution approach using the Monte Carlo method and confirmed by Rietveld refinement. In the sulfonamide. the molecules are linked by N-H . . .O hydrogen bonds into two-dimensional sheets built from alternating eight and twenty-membered rings. In the cocrystal the molecules are linked by O-H . . .N hydrogen bonds to form puckered molecular ribbons that are in rum linked into a continuous 3D framework by C-H . . . pi (arene) interactions.</p

Antibody responses and protective immunity to recombinant vaccinia virus-expressed bluetongue virus antigens

The role of individual viral proteins in the immune response to bluetongue virus (BTV) is not clearly understood. To investigate the contributions of the outer capsid proteins, VP2 and VP5, and possible interactions between them, these proteins were expressed from recombinant vaccinia viruses either as individual proteins or together in double recombinants, or with the core protein VP7 in a triple recombinant. Comparison of the immunogenicity of the vaccinia expressed proteins with BTV expressed proteins was carried out by inoculation of rabbits and sheep. Each of the recombinants was capable of stimulating an anti-BTV antibody response, although there was a wide range in the level of response between animals and species. Vaccinia-expressed VP2 was poorly immunogenic, particularly in rabbits. VP5, on the whole, stimulated higher ELISA titers in rabbits and sheep and in some animals in both species was able to stimulate virus neutralizing antibodies. When the protective efficacy of VP2 and VP5 was tested in sheep, vaccinia-expressed VP2, VP5 and VP2 + VP5 were protective, with the most consistent protection being in groups immunized with both proteins. (C) 1997 Elsevier Science B.V