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       West Nile virus (WNV) is a mosquito-borne flavivirus that can cause fever and, in some cases, severe neurologic disease. There is no approved human vaccine or specific antiviral treatment for WNV.

In 2023, the World Health Organization (WHO) reported roughly 3 to 5 million cases of severe influenza worldwide, resulting in approximately 290,000 to 650,000 deaths. Given the high disease burden, the needs for both prophylactic and therapeutic influenza strategies remain significant. However, current treatments for influenza are susceptible to resistance and are useful for only a limited post-infection period.    

CDC NIOSH researchers have developed a simple and rapid detection technique for Stachybotrys chartarum (a type of mold that commonly grows on wet building materials) by producing monoclonal antibodies which reacts with proteins in Stachybotrys chartarum. These antibodies can be used in immunologic detection assays to detect and possibly quantify Stachybotrys chartarum in environmental samples, and to our knowledge, they do not cross react with other fungi.

The technology includes modifying the Plasmodium falciparum Pfs48/45 Domain III protein sequence to enhance its stability and efficacy to aid in malaria vaccine development. This approach successfully overcomes previous production challenges by increasing the thermostability of the antigen and eliminating the need for additional modifications that could impair vaccine effectiveness. Crucially, the technology maintains the essential neutralizing epitope of Pfs48/45, ensuring its effectiveness in preventing malaria transmission as a transmission-blocking vaccine.

       Antibody therapies that target human B cells are a promising way to treat diseases like B-cell cancers and autoimmune conditions like lupus and multiple sclerosis. Traditionally, these antibodies are made in animals and modified to resemble human antibodies to reduce immune rejection.

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.

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.