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Millions of people are infected with HIV-1 worldwide, and 2.5 to 3 million new infections have been estimated to occur yearly. Although effective antiretroviral therapies are available, millions succumb to AIDS every year, especially in Sub-Saharan Africa, underscoring the need to develop measures to prevent the spread of this disease.

The respiratory syncytial virus (RSV) fusion (F) glycoprotein is the primary target of neutralizing antibodies. The F glycoprotein exists in at least two conformations, a meta-stable prefusion state, and an extremely stable postfusion state. Both states share several epitopes targeted by neutralizing antibodies, but it has been demonstrated that the prefusion conformation of F contains at least one epitope not present in the postfusion conformation.

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.

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.