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8OYU

Stabilised BA.1 SARS-CoV-2 spike with H6 nanobodies in '2 up 1 down' RBD conformation

This is a non-PDB format compatible entry.
Summary for 8OYU
Entry DOI10.2210/pdb8oyu/pdb
EMDB information17296
DescriptorSpike glycoprotein,Fibritin, H6 nanobody, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsnanobody, complex, sars-cov-2, spike, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains5
Total formula weight453656.75
Authors
Weckener, M.,Naismith, J.H.,Owens, R.J. (deposition date: 2023-05-05, release date: 2024-05-15, Last modification date: 2024-10-16)
Primary citationCornish, K.,Huo, J.,Jones, L.,Sharma, P.,Thrush, J.W.,Abdelkarim, S.,Kipar, A.,Ramadurai, S.,Weckener, M.,Mikolajek, H.,Liu, S.,Buckle, I.,Bentley, E.,Kirby, A.,Han, X.,Laidlaw, S.M.,Hill, M.,Eyssen, L.,Norman, C.,Le Bas, A.,Clarke, J.,James, W.,Stewart, J.P.,Carroll, M.,Naismith, J.H.,Owens, R.J.
Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2.
Open Biology, 14:230252-230252, 2024
Cited by
PubMed 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 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.
PubMed: 38835241
DOI: 10.1098/rsob.230252
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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PDB entries from 2024-11-20

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