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TitleDNA-delivered antibody cocktail exhibits improved pharmacokinetics and confers prophylactic protection against SARS-CoV-2.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5886, Year 2022
Publish dateOct 6, 2022
AuthorsElizabeth M Parzych / Jianqiu Du / Ali R Ali / Katherine Schultheis / Drew Frase / Trevor R F Smith / Jiayan Cui / Neethu Chokkalingam / Nicholas J Tursi / Viviane M Andrade / Bryce M Warner / Ebony N Gary / Yue Li / Jihae Choi / Jillian Eisenhauer / Igor Maricic / Abhijeet Kulkarni / Jacqueline D Chu / Gabrielle Villafana / Kim Rosenthal / Kuishu Ren / Joseph R Francica / Sarah K Wootton / Pablo Tebas / Darwyn Kobasa / Kate E Broderick / Jean D Boyer / Mark T Esser / Jesper Pallesen / Dan W Kulp / Ami Patel / David B Weiner /
PubMed AbstractMonoclonal antibody therapy has played an important role against SARS-CoV-2. Strategies to deliver functional, antibody-based therapeutics with improved in vivo durability are needed to supplement ...Monoclonal antibody therapy has played an important role against SARS-CoV-2. Strategies to deliver functional, antibody-based therapeutics with improved in vivo durability are needed to supplement current efforts and reach underserved populations. Here, we compare recombinant mAbs COV2-2196 and COV2-2130, which compromise clinical cocktail Tixagevimab/Cilgavimab, with optimized nucleic acid-launched forms. Functional profiling of in vivo-expressed, DNA-encoded monoclonal antibodies (DMAbs) demonstrated similar specificity, broad antiviral potency and equivalent protective efficacy in multiple animal challenge models of SARS-CoV-2 prophylaxis compared to protein delivery. In PK studies, DNA-delivery drove significant serum antibody titers that were better maintained compared to protein administration. Furthermore, cryo-EM studies performed on serum-derived DMAbs provide the first high-resolution visualization of in vivo-launched antibodies, revealing new interactions that may promote cooperative binding to trimeric antigen and broad activity against VoC including Omicron lineages. These data support the further study of DMAb technology in the development and delivery of valuable biologics.
External linksNat Commun / PubMed:36202799 / PubMed Central
MethodsEM (single particle)
Resolution4.1 - 4.2 Å
Structure data

27254

8d8q

EMDB-27254, PDB-8d8q:
SARS-CoV-2 Spike RBD in complex with DMAbs 2130 and 2196
Method: EM (single particle) / Resolution: 4.2 Å

27255

8d8r

EMDB-27255, PDB-8d8r:
SARS-CoV-2 Spike RBD in complex with DMAb 2196
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / COVID-19 / SARS-CoV-2 / Spike / RBD / IgG / DMAb / antibody cocktail / VIRAL PROTEIN-IMMUNE SYSTEM complex

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