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Journal article
IMM-BCP-01, a patient-derived anti-SARS-CoV-2 antibody cocktail, is active across variants of concern including Omicron BA.1 and BA.2
Science immunology, v 7(75), pp eabl9943-eabl9943
30 Jun 2022
PMID: 35771946
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Monoclonal antibodies are an efficacious therapy against SARS-CoV-2. However, rapid viral mutagenesis, led to escape from most of these therapies, outlining the need for an antibody cocktail with a broad neutralizing potency. Using an unbiased interrogation of the memory B cell repertoire of convalescent COVID-19 patients, we identified human antibodies with broad antiviral activity in vitro and efficacy in vivo against all tested SARS-CoV-2 variants of concern, including Delta, Omicron BA.1 and BA.2. Here, we describe an antibody cocktail IMM-BCP-01, that consists of three patient-derived broadly neutralizing antibodies directed at non-overlapping surfaces on the SARS-CoV-2 spike protein. Two antibodies, IMM20184 and IMM20190, directly blocked Spike binding to the ACE2 receptor. Binding of the third antibody, IMM20253, to its cryptic epitope on the outer surface of RBD, altered the conformation of the Spike Trimer, promoting release of Spike monomers. These antibodies decreased Omicron SARS-CoV-2 infection in the lungs of Syrian golden hamsters in vivo, and potently induced antiviral effector response in vitro, including phagocytosis, ADCC, and complement pathway activation. Our pre-clinical data demonstrated that the three antibody cocktail IMM-BCP-01 could be a promising means for preventing or treating infection of SARS-CoV-2 variants of concern, including Omicron BA.1 and BA.2, in susceptible individuals.
IMM-BCP-01 is efficacious against Omicron, induces dissociation of Spike protein and triggers a potent effector response.
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Details
- Title
- IMM-BCP-01, a patient-derived anti-SARS-CoV-2 antibody cocktail, is active across variants of concern including Omicron BA.1 and BA.2
- Creators
- Pavel A. Nikitin - Immunome (United States)Jillian M. DiMuzio - Immunome (United States)John P. Dowling - Immunome (United States)Nirja B. Patel - Immunome (United States)Jamie L. Bingaman-Steele - Immunome, Inc., Exton, PA, U.S.ABaron C. Heimbach - Immunome (United States)Noeleya Henriquez - Immunome (United States)Chris Nicolescu - Immunome (United States)Antonio Polley - Immunome (United States)Eden L. Sikorski - Immunome (United States)Raymond J. Howanski - Immunome (United States)Mitchell Nath - Immunome (United States)Halley Shukla - Immunome (United States)Suzanne M. Scheaffer - Washington University in St. LouisJames P. Finn - Immunome (United States)Li-Fang Liang - Immunome (United States)Todd Smith - Immunome (United States)Nadia Storm - Boston UniversityLindsay G. A. McKay - Boston UniversityRebecca I. Johnson - Boston UniversityLauren E. Malsick - Boston UniversityAnna N. Honko - Boston UniversityAnthony Griffiths - Boston UniversityMichael S. Diamond - Washington University in St. LouisPurnanand Sarma - Immunome (United States)Dennis H. Geising - Immunome (United States)Michael J. Morin - Immunome (United States)Matthew K. Robinson - Immunome (United States)Lindsay A Steele - School of Biomedical Engineering, Science, and Health Systems (1997-)
- Publication Details
- Science immunology, v 7(75), pp eabl9943-eabl9943
- Publisher
- American Association for the Advancement of Science
- Grant note
- W911QY2090019 / ;
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems; Physician Assistant; Drexel University
- Web of Science ID
- WOS:000933998800006
- Scopus ID
- 2-s2.0-85138127774
- Other Identifier
- 991019356494904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Immunology