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The VRC01-class of potent, broadly neutralizing antibodies (bnAbs) targets the conserved CD4-binding site (CD4bs) of HIV-1 Env which has been a major target of HIV-vaccine design. The current best priming immunogen to engage the VRC01-class germline precursors is the eOD-GT8 60mer, which elicits VRC01-class precursors in multiple transgenic mouse models. However, a large proportion of the antibodies elicited by eOD-GT8 60mer are non-CD4bs or “off-target” antibodies, undermining its effectiveness in eliciting the VRC01-class bnAb precursors.

Ebola virus (EBOV) hemorrhagic fever is one of the most lethal viral infections and lacks a licensed vaccine. EBOV is transmitted by contact with body fluids from infected individuals including droplets or aerosols. Aerosolized EBOV could also be exploited for intentional virus spread. Therefore, vaccines that protect against mucosal and systemic exposure are needed.

The inventors have created a reverse genetics system for RSV strain B1 of antigenic subgroup B encoding a replication-competent recombinant RSV that contains a codon-optimized G ORF and expresses enhanced green fluorescence protein (GFP). There are two antigenic subgroups of RSV, subgroups A and B, and most of the available information and reagents are for subgroup A. Immunity against either subgroup has reduced effectiveness in restricting the heterologous subgroup, suggesting that an effective RSV vaccine might need to contain both subgroups.

In pursuit of an effective vaccine to end the global HIV-1/AIDS pandemic, researchers at the Vaccine Research Center (“VRC”) continue to study the structure of HIV-1. Recently, these researchers have determined the three-dimensional structure of the HIV-1 Envelope trimeric ectodomain (“Env”), comprised of three gp120 and three gp41 subunits, in its prefusion, mature, closed conformation.

This technology provides a new set of hybridoma cell lines each expressing a single monoclonal antibody against human respiratory syncytial virus (RSV) nonstructural protein 1 (NS1). These antibodies have variously been shown to detect NS1 protein in an enzyme-linked immunosorbent assay (ELISA), Western blot assay, immunofluorescence microscopy of paraformaldehyde-fixed cells, and flow cytometry. The various antibodies can vary in their efficiency in each of these assays.

RSV is the most important viral agent of severe respiratory tract disease worldwide, especially in infants and young children, and it also causes severe disease in the elderly and in immunocompromised individuals. There are no licensed vaccines or antivirals suitable for routine use.

Middle East Respiratory Syndrome coronavirus (MERS-CoV) causes a highly lethal pulmonary infection with ~35% mortality. Currently there are no prophylactic measures or effective therapies. Inventors at the Vaccine Research Center of the National Institute of Allergy and Infectious Diseases have identified and developed neutralizing monoclonal antibodies (nMAbs) against the MERS-CoV. This invention describes antibodies that target the Spike (S) glycoprotein on the coronavirus surface, which mediates viral entry into host cells.

This technology is a set of influenza virus enrichment probes developed to increase the sensitivity of sequence-based, universal detection of all influenza viruses. This universal influenza enrichment probe set contains a unique set of 46,953 biotin-labeled, RNA probes, each 120 base-pairs long, that can be used to enrich for any influenza sequences without prior knowledge of type or subtype.

Streptococcus pneumoniae (S. pneumoniae) bacteria, or pneumococcus, can cause many types of illnesses. These range from ear and sinus infections to life-threatening conditions such as pneumonia, bloodstream infections, and meningitis. Pneumococci are surrounded by a polysaccharide capsule, which is thought to help it evade the immune system. Presently, over 90 known serotypes of S. pneumoniae have been identified, of which only a minority produce the majority of pneumococcal infections; a serotype is defined by a unique pneumococcal capsule structure.

Anthrax, whether resulting from natural or bioterrorist-associated exposure, is a constant threat to human health. Bacillus anthracis is the causative agent of anthrax. It is surrounded by a polypeptide capsule of poly-gamma-D-glutamic acid (gamma-D-PGA), which is essential for virulence, is poorly immunogenic and has anti-phagocytic properties. Antibodies to the capsule have been shown to enhance phagocytosis and killing of encapsulated bacilli.