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Fentanyl is a synthetic opioid drug approved by the Food and Drug Administration for use as an analgesic (pain relief) and anesthetic. However, synthetic opioids, such as fentanyl, are prone to abuse and are the primary drivers of overdose related deaths in the United States. As little as two milligrams of fentanyl can be lethal. Furthermore, structural variants of fentanyl, often mixed with other drugs or counterfeit pills are illegally distributed without the user’s knowledge.

The technology described is a sophisticated and high-throughput luciferase immunoprecipitation system (LIPS) assay designed to detect antibodies specific to Varicella-zoster virus (VZV) glycoprotein E (gE). By transfecting cells with VZV protein-Renilla luciferase fusion protein constructs and subsequently performing immunoprecipitations with protein A/G beads, this innovative assay enables the quantitative measurement of VZV gE antibody levels in blood serum samples.

This technology represents a significant advancement in the field of rabies prevention, focusing on the development of highly potent rabies-neutralizing monoclonal antibodies (mAbs) for use in postexposure prophylaxis (PEP). With two mAbs, F2 and G5a, displaying exceptional neutralizing titers of 1154 and 3462 International Units (IUs) per milligram, respectively, these antibodies have the potential to offer enhanced protection against rabies when administered alongside rabies vaccines.

The technology focuses on the development of a tetravalent bispecific antibody effective against Bacillus anthracis, the bacterium responsible for anthrax. This antibody combines the specificities of two monoclonal antibodies (mAbs): one targeting anthrax protective antigen (PA) and the other targeting the bacterial capsule. The anti-PA mAb shows potent toxin-neutralizing activity, while the anti-capsule mAb efficiently kills anthrax bacteria.

This technology includes a rat monoclonal antibody termed mAb11 was generated against the human alpha-5 integrin subunit and can provide immunological characterizations without disrupting integrin adhesive function. It permits characterization of its localization even if the receptor is bound to its fibronectin ligand. The antibody is commercially available from Millipore Sigma.

Malaria is one of the worlds deadliest infectious diseases, causing an estimated 249 million cases and 608,000 deaths annually, with children in the regions of Africa and South Asia being most vulnerable. Approx 2,000 cases of malaria are reported in the United States each year, by travelers from malaria-risk countries. Malaria is a mosquito-borne parasitic disease transmitted through the bite of infected female mosquitoes, which introduces Plasmodium sporozoites into the bloodstream of the human host.

249 million people were afflicted with malaria in 2022. There are five Plasmodium parasite species that cause malaria in humans. Of the five, Plasmodium falciparum causes most of the incidence of human disease. Most advanced malaria vaccine candidates can confer only partial, short-term protection in malaria-endemic areas. The pathogenesis of malaria is associated with blood-stage infection and antibodies specific to the parasite blood-stage antigens may be able to control parasitemia.

Current influenza vaccines mainly induce antibodies against the surface glycoprotein hemagglutinin (HA) that block viral attachment to its host receptors and viral membrane fusion to the host cell. The immunodominant head region of HA undergoes antigenic drift and antibodies directed to the head confer little cross-protections between strains or subtypes.