In order to overcome these drawbacks, we rearranged the genome of an avian H9N2 influenza virus and expressed the entire H5 hemagglutinin open reading frame (ORF) from the segment 8 viral RNA. These vectors had reduced polymerase activities as well as viral replication in vitro and excellent safety profiles in vivo. Immunization with the dual H9-H5 influenza virus resulted in protection against lethal H5N1 challenge in mice and ferrets,

and also against a potentially pandemic H9 virus. Our studies demonstrate that rearranging the influenza virus genome has great potential for the development of improved vaccines against influenza virus E7080 as well as other pathogens.”
“The burden of medical comorbidity in individuals with Alzheimer’s disease MLN2238 is greater than that observed in matched individuals without dementia. This has important implications for all clinicians and healthcare providers who deal with this common condition. The prevalence of vascular risk factors and vascular disease is particularly high. Additionally, associations with a number of other chronic medical conditions have been described, including thyroid disorders,

sleep apnoea, osteoporosis and glaucoma. This review gives an overview of evidenced medical (non-psychiatric) comorbidity associated with Alzheimer’s disease and briefly explores the underlying mechanisms that may account for these associations.”
“The structure of single-stranded DNA (ssDNA) packaging H-1 parvovirus Benzatropine (H-1PV), which is being developed as an antitumor gene delivery vector, has been determined for wild-type (wt) virions and noninfectious (empty) capsids to 2.7- and 3.2-angstrom resolution, respectively, using X-ray crystallography. The capsid viral protein (VP) structure consists of an alpha-helix and an eight-stranded

anti-parallel beta-barrel with large loop regions between the strands. The beta-barrel and loops form the capsid core and surface, respectively. In the wt structure, 600 nucleotides are ordered in an interior DNA binding pocket of the capsid. This accounts for similar to 12% of the H-1PV genome. The wt structure is identical to the empty capsid structure, except for side chain conformation variations at the nucleotide binding pocket. Comparison of the H-1PV nucleotides to those observed in canine parvovirus and minute virus of mice, two members of the genus Parvovirus, showed both similarity in structure and analogous interactions. This observation suggests a functional role, such as in capsid stability and/or ssDNA genome recognition for encapsulation. The VP structure differs from those of other parvoviruses in surface loop regions that control receptor binding, tissue tropism, pathogenicity, and antibody recognition, including VP sequences reported to determine tumor cell tropism for oncotropic rodent parvoviruses.