Invivyd provides virology data, analysis of SARS-CoV-2 structural biology

Invivyd provided detailed virology data supporting previously communicated neutralization activity results, along with a genetic and structural analysis of past and present SARS-CoV-2 variant spike proteins, including the established molecular target of pemivibart. As part of Invivyd’s ongoing monitoring of antiviral activity, Invivyd contracts with LabCorp’s Monogram Biosciences lab to provide independent, robust virology assessments in a consistent lineal chain that allows for consideration of potential changing pemivibart potency as SARS-CoV-2 evolves. Pemivibart potency against contemporary viruses KP.3.1.1 and LB.1 remains in-line with the totality of predominant variants dating back to 2022, including isolates identified during the conduct of the CANOPY Phase 3 clinical trial from late 2023 to early 2024. “Quantitative neutralization assays exhibit marked intrinsic variability. Since discovery, pemivibart has exhibited impressively stable neutralization results across a wide range of SARS-CoV-2 variants, including and through contemporary variants tested,” said Robert Allen, Ph.D., Chief Scientific Officer of Invivyd. “The values we observe thus far generally fall within the expected variability of the assay systems we employ.” Invivyd also provided an update to ongoing structural analysis showing no meaningful mutational change in the pemivibart binding site since the Omicron shift late in 2021.The pemivibart binding site is defined as a region of amino acid residues on the spike protein within 5 angstroms of the interaction between pemivibart and spike protein in a crystal structure and consists of 19 key amino acids. Invivyd’s ongoing genetic and structural analyses of these residues provide the underlying biological rationale for the company’s ongoing expectation for neutralization activity of pemivibart in the face of constant and convergent mutation in the SARS-CoV-2 spike protein. Analysis to date of all 19 amino acids presented below shows de minimis mutational change with ongoing stability to the binding site since the Omicron shift.