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TitleIMM-BCP-01, a patient-derived anti-SARS-CoV-2 antibody cocktail, is active across variants of concern including Omicron BA.1 and BA.2.
Journal, issue, pagesSci Immunol, Vol. 7, Issue 75, Page eabl9943, Year 2022
Publish dateSep 9, 2022
AuthorsPavel A Nikitin / Jillian M DiMuzio / John P Dowling / Nirja B Patel / Jamie L Bingaman-Steele / Baron C Heimbach / Noeleya Henriquez / Chris Nicolescu / Antonio Polley / Eden L Sikorski / Raymond J Howanski / Mitchell Nath / Halley Shukla / Suzanne M Scheaffer / James P Finn / Li-Fang Liang / Todd Smith / Nadia Storm / Lindsay G A McKay / Rebecca I Johnson / Lauren E Malsick / Anna N Honko / Anthony Griffiths / Michael S Diamond / Purnanand Sarma / Dennis H Geising / Michael J Morin / Matthew K Robinson /
PubMed AbstractMonoclonal antibodies are an efficacious therapy against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, rapid viral mutagenesis led to escape from most of these therapies, ...Monoclonal antibodies are an efficacious therapy against severe acute respiratory syndrome coronavirus 2 (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 patients with convalescent COVID-19, 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 and 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 nonoverlapping 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 the 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 preclinical 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.
External linksSci Immunol / PubMed:35771946 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 8.31 Å
Structure data

EMDB-27081: IMM20184 and IMM20253 Fabs in ternary complex with SARS-CoV-2 receptor binding domain
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-27192: IMM20253 Fab complex with Trimer Spike protein of SARS-CoV-2 virus
Method: EM (single particle) / Resolution: 7.96 Å

EMDB-27193: IMM20253 Fab complex with Spike monomer
Method: EM (single particle) / Resolution: 8.01 Å

EMDB-27203: IMM20190 Fab complex with SARS-CoV-2 Spike Trimer
Method: EM (single particle) / Resolution: 6.87 Å

EMDB-27204: IMM20184 Fab complex with SARS-CoV-2 Spike Trimer
Method: EM (single particle) / Resolution: 8.31 Å

Source
  • Severe acute respiratory syndrome coronavirus
  • Homo sapiens (human)
  • Severe acute respiratory syndrome coronavirus 2

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