Abstract: A pegylated, circularly permuted construct of the CapD enzyme (a gamma glutamyl transferase enzyme acting as a hydrolase specific to poly-?-D-glutamic acid) is used to treat anthrax and other bacterial infections, including but not limited to infection with strains that are resistant to available antibiotics.

Abstract: A pegylated, circularly permuted construct of the CapD enzyme (a gamma glutamyl transferase enzyme acting as a hydrolase specific to poly-?-D-glutamic acid) is used to treat anthrax and other bacterial infections, including but not limited to infection with strains that are resistant to available antibiotics.

Abstract: Proteases of Group IV (+)ssRNA viruses were found to act on a human sequences in addition to the viral sequences. The identity of the cleavable human sequences is disclosed. Detection of these sequences can act as a diagnostic of infection. It is contemplated that these findings could be employed to facilitate post-translational silencing at the level of protein (e.g., removal of existing proteins), thus serving as a protein analog to CRISPR/Cas9 and RNAi/RISC, and further to enable sequence-specific silencing of host functions without the modification of the host genome.

Abstract: A protease of the Venezuelan equine encephalitis virus (VEEV) was found to act on a host substrate in addition to the viral substrate. It is contemplated that these findings could be employed to facilitate post-translational silencing at the level of protein (removal of existing proteins) as a protein analog to CRISPR/Cas9 and RNAi/RISC, and further to enable detection of viral infection.

Abstract: A protease of the Venezuelan equine encephalitis virus (VEEV) was found to act on a host substrate in addition to the viral substrate. It is contemplated that these findings could be employed to facilitate post-translational silencing at the level of protein (removal of existing proteins) as a protein analog to CRISPR/Cas9 and RNAi/RISC, and further to enable detection of viral infection.

Abstract: Disclosed herein ricin toxin A chain polypeptides having an engineered disulfide bond ((SS)RTA) and compositions thereof. The disclosed (SS)RTA polypeptides retain the immunological epitope of wild type RTA, lack detectable N-glycosidase activity or exhibit reduced N-glycosidase activity as compared to controls, and exhibit increased solubility, thermal stability and a lower tendency to self-aggregate as compared to RTA 198 and/or RTA 1-33/44-198. Also disclosed are immunogenic compositions that may be used to immunize a subject against ricin intoxication. Methods of immunizing against, treating, inhibiting, reducing and/and preventing ricin intoxication are disclosed.

Abstract: Disclosed herein ricin toxin A chain polypeptides having an engineered disulfide bond ((SS)RTA) and compositions thereof. The disclosed (SS)RTA polypeptides retain the immunological epitope of wild type RTA, lack detectable N-glycosidase activity or exhibit reduced N-glycosidase activity as compared to controls, and exhibit increased solubility, thermal stability and a lower tendency to self-aggregate as compared to RTA 198 and/or RTA 1-33/44-198. Also disclosed are immunogenic compositions that may be used to immunize a subject against ricin intoxication. Methods of immunizing against, treating, inhibiting, reducing and/and preventing ricin intoxication are disclosed.