Main Menu

The technology involves the development of monoclonal antibodies produced by hybridomas, including cell lines such as 10G3, 3E6, 10D4, 10G4, 1D8, 13D10, 9E5, and 9F10, which specifically react with Bacillus anthracis Lethal Factor (LF). These monoclonal antibodies offer valuable applications in anthrax detection, therapeutic intervention, and research into the biology of Bacillus anthracis and its lethal toxin. This advancement provides promising tools for mitigating the impact of anthrax infections and advancing our understanding of this deadly pathogen.

This technology includes a large panel of monoclonal antibodies (mAbs) against the spike glycoprotein, capable of recognizing intact SARS-CoV-2 virions with high affinity. Data to support SARS-CoV-2-specific binding include ELISA and label-free (biolayer interferometry) binding measurements using recombinant proteins, immunofluorescence in culture, immunofluorescence staining of tissue from infected patients, and virus neutralization assays.

This technology includes human F(ab’)2 fragments specific for anthrax lethal factor for the development of a lateral flow immunoassay for Bacillus anthracis Lethal Factor. The F(ab’)2 fragments are generated from a Human Combinatorial Antibody Library (HuCAL) and are highly specific with high affinity. A multi-step process was utilized beginning by screening a phage display library with over 45 billion functional human antibody specificities. The primary screen against Bacillus anthracis Lethal Factor (LF) generated 360 positive clones.

This technology includes eight mouse monoclonal antibodies (mAb) and their corresponding hybridomas used for the Enzyme Linked Immunosorbent Assay (ELISA) detection and identification of Marburg (3) and Lassa (5) virus antigens. Lateral flow assays for hemorrhagic fevers are being developed in response to the Ebola outbreak. Our cocktail can identify different proteins for each virus; Marburg viral proteins 35 and 40 (VP35, VP40) and Lassa nucleoprotein (NP) and glycoprotein (G2). All known Marburg and Lassa viruses can be captured in the ELISA assay.

This technology includes a murine IgG1 monoclonal antibody (mAb), 1C7, for the detection of Chaetomium globosum. The development of mAb-based detection methods may provide a standardized approach to quantify the target organism(s) using rapid immunoassay platforms. To date, mAbs are not available for Chaetomium species. C. globosum enolase was selected as a candidate biomarker for the detection of this species due to its presence within the cytosol and cell wall. C. globosum enolase was cloned and a recombinant expressed in Escherichia coli for the production of mAbs.

This technology includes a novel application of chimeric monoclonal antibodies (i.e.animal-human) as substitutes for patient /organism specimens to create standardized training (TP), proficiency testing (PT), quality control (QC), lot-to-lot validation, and new serologic test evaluation and validation panels to support the implementation of quality management systems (QMS) of serology-based tests.

The Ligand Epitope Antigen Presentation System (LEAPS) represents a breakthrough in immunotherapeutic technology developed by CEL-SCI Corporation. This technology employs a novel approach to boost the immune system's response to influenza, aiming to treat, manage, or even prevent the illness. By combining LEAPS with a specific peptide from the influenza virus, and administering it intravenously in mice, there's a marked improvement in the immune system's ability to fight off the virus.

The discovery outlined in the Employee Discovery and Invention Report represents a significant advancement in veterinary vaccine technology, specifically targeting the bovine respiratory syncytial virus (bRSV). This innovation involves a "DS2" version of the bRSV F vaccine, which has been engineered to enhance immunogenicity through a prefusion-stabilized form of the F protein, absent of the fusion peptide and reinforced by cavity-filling mutations and inter-protomer disulfides.

Norovirus is a leading cause of vomiting, diarrhea, and foodborne illness worldwide, with 700 million cases and 200,000 deaths occurring each year. Despite decades of work in the field, there are no preventive or therapeutic strategies specifically approved for even the most prevalent forms of human norovirus (i.e., GI, GII genogroups), which are highly contagious and carry an increased risk of severe complications in children, older adults, and those with immunocompromising conditions. 

The described technology pertains to the development of bispecific antibodies targeting the Ebola virus glycoprotein. These antibodies, mAb114 and either S1-4-A09 or its engineered variant S1-4-A09 A80P, demonstrate specificity towards the Ebola virus (EBOV) glycoproteins from different strains, including Kikwit and Bundibugyo. The variant S1-4-A09 A80P retains binding specificity and activity but lacks a glycosylation motif, enhancing manufacturability without compromising function.