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Sponsor contentNIAID researchers developed a recombinant HIV-1 trimer immunogen that utilizes a closed conformation of trimeric gp120 to stabilize epitopes for broadly neutralizing antibodies. The recombinant Env ectodomain trimers can induce higher neutralizing antibody titers than wild type Env trimers.
Collaborative Research and Licensing Opportunity for a Research Material: A Potent, Broadly-neutralizing, Anti-HIV Antibody (35O22) that Binds a Novel Epitope35O22 is a potent anti-HIV antibody that binds a novel HIV epitope. This antibody neutralizes at least 80% of HIV isolates tested so far. The unique binding of 35O22 makes it an attractive candidate to combine with other HIV antibodies or antivirals in treating or preventing HIV infection.Sponsor content
Collaborative Research and Licensing Opportunity: HIV targets CD62L on central memory T cells through viral envelope glycans for adhesion and induces selectin shedding for viral releaseNIAID researchers have shown that inhibition of CD62L shedding dramatically reduced HIV-1 infection and viral release from both viremic and aviremic CD4+ T cells. Therefore, inhibitors for CD62L sheddase can function as an anti-HIV treatment that may be effective alone or in combination with existing therapeutics.Sponsor content
Collaborative Research and Licensing Opportunity: Broadly Neutralizing Antibodies against HIV-1 Directed to the CD4 Binding Site of HIV Envelope ProteinScientists at the NIAID Vaccine Research Center have isolated and characterized neutralizing antibodies (VRC01, 02, 03, and 07) that bind to the CD4 binding site of HIV-1 envelope glycoprotein gp120. These human monoclonal antibodies can be used as a therapeutic to: (1) treat an HIV infection, (2) decrease and prevent HIV-transmission from mother to infant, and (3) be effectively combined with anti-retroviral drug therapy.Sponsor content
Collaborative Research and Licensing Opportunity: Development of a Transferrable Norwalk Virus Epitope and Detector Monoclonal AntibodyThe development of monoclonal antibodies (MAbs) against norovirus virus-like particles (VLPs) has allowed the identification and characterization of key antigenic sites of the virus capsid and facilitated the development of diagnostic assays.
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