6waq: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6waq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6waq OCA], [https://pdbe.org/6waq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6waq RCSB], [https://www.ebi.ac.uk/pdbsum/6waq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6waq ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6waq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6waq OCA], [https://pdbe.org/6waq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6waq RCSB], [https://www.ebi.ac.uk/pdbsum/6waq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6waq ProSAT]</span></td></tr> | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 11:26, 17 October 2024
Crystal structure of the SARS-CoV-1 RBD bound by the cross-reactive single-domain antibody SARS VHH-72Crystal structure of the SARS-CoV-1 RBD bound by the cross-reactive single-domain antibody SARS VHH-72
Structural highlights
Publication Abstract from PubMedCoronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies.,Wrapp D, De Vlieger D, Corbett KS, Torres GM, Wang N, Van Breedam W, Roose K, van Schie L, Hoffmann M, Pohlmann S, Graham BS, Callewaert N, Schepens B, Saelens X, McLellan JS Cell. 2020 Apr 29. pii: S0092-8674(20)30494-3. doi: 10.1016/j.cell.2020.04.031. PMID:32375025[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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