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Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2.
Cornish, Katy; Huo, Jiandong; Jones, Luke; Sharma, Parul; Thrush, Joseph W; Abdelkarim, Sahar; Kipar, Anja; Ramadurai, Siva; Weckener, Miriam; Mikolajek, Halina; Liu, Sai; Buckle, Imogen; Bentley, Eleanor; Kirby, Adam; Han, Ximeng; Laidlaw, Stephen M; Hill, Michelle; Eyssen, Lauren; Norman, Chelsea; Le Bas, Audrey; Clarke, John; James, William; Stewart, James P; Carroll, Miles; Naismith, James H; Owens, Raymond J.
Affiliation
  • Cornish K; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Huo J; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Jones L; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford , Oxford, UK.
  • Sharma P; Nuffield Department of Medicine, Pandemic Sciences Institute, University of Oxford , Oxford, UK.
  • Thrush JW; Wellcome Centre for Human Genetics, University of Oxford , Oxford, UK.
  • Abdelkarim S; Department of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
  • Kipar A; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Ramadurai S; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Weckener M; Department of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
  • Mikolajek H; Vetsuisse Faculty, Laboratory for Animal Model Pathology, Institute of Veterinary Pathology, University of Zurich , Zurich, Switzerland.
  • Liu S; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Buckle I; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Bentley E; Diamond Light Source Ltd, Harwell Science Campus , Didcot, UK.
  • Kirby A; James & Lillian Martin Centre, Sir William Dunn School of Pathology, University of Oxford , Oxford, UK.
  • Han X; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Laidlaw SM; Department of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
  • Hill M; Department of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
  • Eyssen L; Department of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
  • Norman C; Nuffield Department of Medicine, Pandemic Sciences Institute, University of Oxford , Oxford, UK.
  • Le Bas A; Wellcome Centre for Human Genetics, University of Oxford , Oxford, UK.
  • Clarke J; James & Lillian Martin Centre, Sir William Dunn School of Pathology, University of Oxford , Oxford, UK.
  • James W; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Stewart JP; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Carroll M; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Naismith JH; Structural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
  • Owens RJ; James & Lillian Martin Centre, Sir William Dunn School of Pathology, University of Oxford , Oxford, UK.
Open Biol ; 14(6): 230252, 2024 Jun.
Article in En | MEDLINE | ID: mdl-38835241
ABSTRACT
The Omicron strains of SARS-CoV-2 pose a significant challenge to the development of effective antibody-based treatments as immune evasion has compromised most available immune therapeutics. Therefore, in the 'arms race' with the virus, there is a continuing need to identify new biologics for the prevention or treatment of SARS-CoV-2 infections. Here, we report the isolation of nanobodies that bind to the Omicron BA.1 spike protein by screening nanobody phage display libraries previously generated from llamas immunized with either the Wuhan or Beta spike proteins. The structure and binding properties of three of these nanobodies (A8, H6 and B5-5) have been characterized in detail providing insight into their binding epitopes on the Omicron spike protein. Trimeric versions of H6 and B5-5 neutralized the SARS-CoV-2 variant of concern BA.5 both in vitro and in the hamster model of COVID-19 following nasal administration. Thus, either alone or in combination could serve as starting points for the development of new anti-viral immunotherapeutics.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Antibodies, Neutralizing / Single-Domain Antibodies / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 / Antibodies, Viral Limits: Animals / Humans Language: En Journal: Open Biol Year: 2024 Document type: Article Country of publication:
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Antibodies, Neutralizing / Single-Domain Antibodies / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 / Antibodies, Viral Limits: Animals / Humans Language: En Journal: Open Biol Year: 2024 Document type: Article Country of publication: