Abstract: Compounds, methods and pharmaceutical compositions for treating viral infections, by administering certain novel compounds in therapeutically effective amounts are disclosed. Methods for preparing the compounds and methods of using the compounds and pharmaceutical compositions thereof are also disclosed. In particular, the treatment and prophylaxis of viral infections such as caused by hemorrhagic fever viruses is disclosed, i.e., including but not limited to, Arenaviridae (Junin, Machupo, Guanarito, Sabia, Lassa, Tacaribe, Pichinde, and LCMV), Filoviridae (Ebola and Marburg viruses), Flaviviridae (yellow fever, Omsk hemorrhagic fever and Kyasanur Forest disease viruses), and Bunyaviridae (Rift Valley fever).

Abstract: The focus of the present invention is an effective anti-poxvirus drug for use in treating or preventing human disease caused by pathogenic poxviruses. More particularly, the present invention relates to antiviral drugs that target the poxvirus proteinase responsible for core protein maturation, a step which is absolutely essential for the production and spread of infectious virions.

Abstract: The present invention provides two new chromosomal integration sites for expression of foreign genes have been developed in Streptococcus gordonii (S. gordonii). One integration site is intergenic between orfA and orfB in an operon of unknown function. The other site is intragenic within the lacG gene, which encodes phospho-?-galactosidase, and is part of the lactose (lac) operon. The emm6 gene from Streptococcus pyogenes was integrated in a stable configuration into the chromosome of S. gordonii at each of these integration sites, and in both cases the recombinant bacteria expressed the M6 protein on their surface. Furthermore, expression from the lacG site within the lactose operon was shown to be regulated by growth on lactose. Identification of these new chromosomal insertion sites provides the ability to express multiple foreign genes from the same recombinant and the potential for modulating expression in vitro or in vivo by the use of a biosynthetic metabolite.

Abstract: A novel system for cloning and expression of genes in gram-positive bacteria. The expression system is based on the finding that many gram-positive bacteria sort proteins to their cell surface through cis-acting N-terminal signal sequences and C-terminal anchor regions. In particular, the cell sorting signals of the streptococcal M6 protein, a well-known surface molecule, are used to construct a gram-positive expression system, designated SPEX (Streptococcal Protein Expression). Expression is achieved by cloning the gene of interest into an appropriate SPEX cassette which is then stably introduced into a bacterial host, such as the human commensal Streptococcus gordonii. Depending on the SPEX vector used, recombinant proteins can be anchored to the cell wall prior to release by specific endoproteolytic cleavage or secreted into the culture medium during bacterial growth. The use of host bacteria lacking extracellular proteases should protect secreted proteins from proteolytic degradation.