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TitleA potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 5469, Year 2021
Publish dateSep 22, 2021
AuthorsJiandong Huo / Halina Mikolajek / Audrey Le Bas / Jordan J Clark / Parul Sharma / Anja Kipar / Joshua Dormon / Chelsea Norman / Miriam Weckener / Daniel K Clare / Peter J Harrison / Julia A Tree / Karen R Buttigieg / Francisco J Salguero / Robert Watson / Daniel Knott / Oliver Carnell / Didier Ngabo / Michael J Elmore / Susan Fotheringham / Adam Harding / Lucile Moynié / Philip N Ward / Maud Dumoux / Tessa Prince / Yper Hall / Julian A Hiscox / Andrew Owen / William James / Miles W Carroll / James P Stewart / James H Naismith / Raymond J Owens /
PubMed AbstractSARS-CoV-2 remains a global threat to human health particularly as escape mutants emerge. There is an unmet need for effective treatments against COVID-19 for which neutralizing single domain ...SARS-CoV-2 remains a global threat to human health particularly as escape mutants emerge. There is an unmet need for effective treatments against COVID-19 for which neutralizing single domain antibodies (nanobodies) have significant potential. Their small size and stability mean that nanobodies are compatible with respiratory administration. We report four nanobodies (C5, H3, C1, F2) engineered as homotrimers with pmolar affinity for the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Crystal structures show C5 and H3 overlap the ACE2 epitope, whilst C1 and F2 bind to a different epitope. Cryo Electron Microscopy shows C5 binding results in an all down arrangement of the Spike protein. C1, H3 and C5 all neutralize the Victoria strain, and the highly transmissible Alpha (B.1.1.7 first identified in Kent, UK) strain and C1 also neutralizes the Beta (B.1.35, first identified in South Africa). Administration of C5-trimer via the respiratory route showed potent therapeutic efficacy in the Syrian hamster model of COVID-19 and separately, effective prophylaxis. The molecule was similarly potent by intraperitoneal injection.
External linksNat Commun / PubMed:34552091 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.5 - 3.0 Å
Structure data

12777

7oan

EMDB-12777, PDB-7oan:
Nanobody C5 bound to Spike
Method: EM (single particle) / Resolution: 3.0 Å

PDB-7oao:
Nanobody C5 bound to RBD
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-7oap:
Nanobody H3 AND C1 bound to RBD
Method: X-RAY DIFFRACTION / Resolution: 1.901 Å

PDB-7oaq:
Nanobody H3 AND C1 bound to RBD with Kent mutation
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-7oau:
Nanobody C5 bound to Kent variant RBD (N501Y)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-7oay:
Nanobody F2 bound to RBD
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-CIT:
CITRIC ACID

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • severe acute respiratory syndrome coronavirus 2
  • vicugna pacos (alpaca)
  • lama glama (llama)
KeywordsANTIVIRAL PROTEIN / Spike / nanobody / high affinity / RBD

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