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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.

Human metapneumovirus (hMPV), a negative, single-stranded RNA virus, accounts for approximately 5-15% of infant respiratory tract infections and poses a severe risk of disease and hospitalization in both the elderly and the immunocompromised. Investigators at the Vaccine Research Center (VRC) of the National Institute of Allergy and Infectious Diseases (NIAID) have generated an hMPV fusion glycoprotein (“F protein”) stabilized in a prefusion conformation.

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.

Scientists at the National Institute of Allergy and Infectious Diseases (NIAID) recently discovered a human neutralizing antibody, 10E8, that binds to the GP41 protein of HIV-1 and prevents infection by HIV-1. 10E8 potently neutralizes up to 98% of genetically diverse HIV-1 strains.

By engineering the 10E8 antibody, NIAID scientists have improved the properties of 10E8 that affect manufacturability, such as solubility, while preserving its neutralizing breadth and potency.

An effective human immunodeficiency virus type 1 (HIV-1) vaccine has long been sought to contend with the Acquired Immunodeficiency Syndrome (AIDS) pandemic.

One approach researchers have taken to elicit broadly neutralizing antibodies against HIV-1 is to stabilize the structurally flexible HIV-1 envelope (Env) trimer. Researchers stabilized the Env trimer in a conformation that displays predominantly broadly neutralizing epitopes and few non-neutralizing epitopes. Currently, BG505 DS-SOSIP is a leading vaccine candidate with the desired conformation and antigenicity.

Nipah virus is an emerging pathogenic paramyxovirus responsible for sporadic and isolated outbreaks of severe respiratory and neurologic disease in Southern Asia. As a zoonotic virus, disease can manifest in both animals and human with indigenous fruit bats acting as natural reservoirs of the virus. The effects of viral infection vary from acute respiratory distress to fatal encephalitis.

Currently, fed-batch processes are the most commonly used bioprocesses in transient gene expression (TGE) vaccine manufacturing. However, because fed-batch processes keep all the cells and protein product in the vessel throughout the run, some limitations are intrinsic. First, waste products like cell debris or other unwanted small molecules accumulate in the vessel with a potential to disrupt the cell growth, protein production, and the stability of the generated protein of interest.

Ebola virus is a large, negative-strand RNA virus composed of 7 genes encoding viral proteins, including a single glycoprotein (GP). The virus is responsible for causing Ebola virus disease (EVD), formerly known as Ebola hemorrhagic fever (EHF), in humans. In particular, Bundibugyo (BDBV), Zaire (EBOV), and Sudan (SUDV) species have been associated with large outbreaks of EVD in Africa and reported case fatality rates of up to 90%. Transmission of Ebola virus to humans is not yet fully understood but is likely due to incidental exposure to infected animals.