Technology ID

Antibodies With Potent and Broad Neutralizing Activity Against Antigenically Diverse and Highly Transmissible SARS-CoV-2 Variants

Lead Inventor
Misasi, John (NIAID)
Wang, Lingshu (NIAID)
Mascola, John (ModeX Therapeutics, Inc)
Douek, Daniel (NIAID)
Sullivan, Nancy (NIAID)
Koup, Richard (NIAID)
Chen, Man (NIAID)
Shi, Wei (NIAID)
Zhang, Yi (NIAID)
Yang, Eun (NIAID)
Doria-Rose, Nicole (NIAID)
Schramm, Chaim (NIAID)
Birungi-Huff, Kevina (National Institute of Allergy and Infectious Diseases (NIAID/NIH))
Bush, Sabrina (NIAID)
Musayev, Maryam (National Institute of Allergy and Infectious Diseases)
Development Stages
Pre-clinical (in vivo)
Development Status
Preclinical Research
Lead IC

       Emergence of highly transmissible SARS-CoV-2 variants of concern that are resistant to current therapeutic antibodies highlights the need for continuing discovery of broadly reactive antibodies.
       Scientists at the Vaccine Research Center of the National Institute of Allergy and Infectious Diseases have identified multiple antibodies that ultra-potently neutralize SARS-CoV-2, including the highly transmissible BA.4, BA.5, BQ.1.1 and XBB subvariants of Omicron, as shown in a pseudovirus neutralization assay.  These antibodies target several epitopes in the receptor binding domain of the spike protein that are not impacted by spike mutations that knockout binding to other therapeutic antibodies, including, K417N, N439K, N440K, K444T, V445P, G446S, L452R, Y453F, N460K, S477N, E484A/K, F486S/V and Q498R.  Several of the antibodies are able to simultaneously bind to the spike protein and are compatible for use in combination therapies. 
      This technology is available for licensing for commercial development in accordance with 35 U.S.C. § 209 and 37 CFR Part 404.

Commercial Applications
  • Treatment of SARS-CoV-2 infection
Competitive Advantages
  • Ultra-potent neutralization of currently identified SARS-CoV-2 variants including Omicron subvariants BQ.1.1 and XBB
  • Mechanism of Action – Some antibodies directly bind to and block ACE2 receptor binding to the SARS CoV-2 spike protein
Licensing Contact: