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7PHG

MaP OF P5C3RBD Interface

Summary for 7PHG
Entry DOI10.2210/pdb7phg/pdb
EMDB information13415
DescriptorSurface glycoprotein, Heavy ChaIn variable, Light ChaIn (3 entities in total)
Functional Keywordsrbd, antibody, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
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Total number of polymer chains3
Total formula weight47055.47
Authors
Perez, L. (deposition date: 2021-08-17, release date: 2021-10-13, Last modification date: 2024-10-23)
Primary citationFenwick, C.,Turelli, P.,Perez, L.,Pellaton, C.,Esteves-Leuenberger, L.,Farina, A.,Campos, J.,Lana, E.,Fiscalini, F.,Raclot, C.,Pojer, F.,Lau, K.,Demurtas, D.,Descatoire, M.,Joo, V.S.,Foglierini, M.,Noto, A.,Abdelnabi, R.,Foo, C.S.,Vangeel, L.,Neyts, J.,Du, W.,Bosch, B.J.,Veldman, G.,Leyssen, P.,Thiel, V.,LeGrand, R.,Levy, Y.,Trono, D.,Pantaleo, G.
A highly potent antibody effective against SARS-CoV-2 variants of concern.
Cell Rep, 37:109814-109814, 2021
Cited by
PubMed Abstract: Control of the ongoing SARS-CoV-2 pandemic is endangered by the emergence of viral variants with increased transmission efficiency, resistance to marketed therapeutic antibodies, and reduced sensitivity to vaccine-induced immunity. Here, we screen B cells from COVID-19 donors and identify P5C3, a highly potent and broadly neutralizing monoclonal antibody with picomolar neutralizing activity against all SARS-CoV-2 variants of concern (VOCs) identified to date. Structural characterization of P5C3 Fab in complex with the spike demonstrates a neutralizing activity defined by a large buried surface area, highly overlapping with the receptor-binding domain (RBD) surface necessary for ACE2 interaction. We further demonstrate that P5C3 shows complete prophylactic protection in the SARS-CoV-2-infected hamster challenge model. These results indicate that P5C3 opens exciting perspectives either as a prophylactic agent in immunocompromised individuals with poor response to vaccination or as combination therapy in SARS-CoV-2-infected individuals.
PubMed: 34599871
DOI: 10.1016/j.celrep.2021.109814
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

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