Antibody-protein interaction


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Structural characterization of SARS-CoV-2 spike glycoprotein (RBD to S2 double mutant (rS2d)) constructs. And determing its binding with the antibody CR3022 and human cell receptor ACE2. The spike glycoprotein mutant constructs (rS2d) with double mutation S383C, D985C were developed. The RBD in the rS2d construct is locked in the 'down ' state conformation.
32699321
(Nat Struct Mol Biol)
PMID
32699321
Date of Publishing: 2020 Oct
Title Controlling the SARS-CoV-2 spike glycoprotein conformation
Author(s) nameHenderson R, Edwards RJ et al.
Journal Nat Struct Mol Biol
Impact factor
9.8
Citation count: 43


Structural characterization of SARS-CoV-2 spike glycoprotein (subdomain 1 to S2 quadruple mutant (u1S2q 1 Up RBD)) construct. And determing its binding with the antibody CR3022 and human cell receptor ACE2. The spike glycoprotein mutant construct (u1S2q) with mutation A570L,T572I, F855Y, N856I were developed. The u1S2q 1 Up RBD Spike Protein Trimer were docked with the CR3022 Fab - RBD complex (PDB 6YLA) and potential clashes were observed in between.
32699321
(Nat Struct Mol Biol)
PMID
32699321
Date of Publishing: 2020 Oct
Title Controlling the SARS-CoV-2 spike glycoprotein conformation
Author(s) nameHenderson R, Edwards RJ et al.
Journal Nat Struct Mol Biol
Impact factor
9.8
Citation count: 43


Structural characterization of SARS-CoV-2 spike glycoprotein (subdomain 1 to S2 quadruple mutant (u1S2q 2 Up RBD state)) construct and determing its binding with the antibody CR3022 human cell receptor ACE2 The spike glycoprotein mutant construct (u1S2q) with mutation A570L,T572I, F855Y, N856I were developed. The u1S2q 2 Up RBD Spike Protein Trimer were docked with the CR3022 Fab - RBD complex (PDB 6YLA) and potential clashes were observed in between.
32699321
(Nat Struct Mol Biol)
PMID
32699321
Date of Publishing: 2020 Oct
Title Controlling the SARS-CoV-2 spike glycoprotein conformation
Author(s) nameHenderson R, Edwards RJ et al.
Journal Nat Struct Mol Biol
Impact factor
9.8
Citation count: 43


Crystal structure of the SARS-CoV-2 receptor binding domain in complex with CR3022 Fab The spike protein is an attractive candidate for both vaccine development and immunotherapy. As monoclonal antibodies are recognised as potential antivirals,the results in this study suggest that CR3022 could be of immediate utility because the mechanism of neutralization will be unusually resistant to virus escape.
32585135
(Cell Host Microbe)
PMID
32585135
Date of Publishing: 2020 Sep 9
Title Neutralization of SARS-CoV-2 by destruction of the Prefusion Spike
Author(s) nameHuo J, Zhao Y et al.
Journal Cell Host Microbe
Impact factor
10.45
Citation count: 39


Structural characterisation of the SARS-CoV-2 receptor binding domain in complex with CR3022 Fab (crystal form 1) The binding of ACE2 to the RBD is perturbed by the presence of CR3022.
32585135
(Cell Host Microbe)
PMID
32585135
Date of Publishing: 2020 Sep 9
Title Neutralization of SARS-CoV-2 by destruction of the Prefusion Spike
Author(s) nameHuo J, Zhao Y et al.
Journal Cell Host Microbe
Impact factor
10.45
Citation count: 39


SARS-CoV-2 is neutralized by the binding of CR3022. CR3022 epitope on binding results in fusion-incompetent post-fusion state of the S-protein. CR3022 epitope can be used as a major target for therapeutic antibodies.
32585135
(Cell Host Microbe)
PMID
32585135
Date of Publishing: 2020 Sep 9
Title Neutralization of SARS-CoV-2 by destruction of the Prefusion Spike
Author(s) nameHuo J, Zhao Y et al.
Journal Cell Host Microbe
Impact factor
10.45
Citation count: 39


CR3022 interacts with a conserved epitope away from the receptor binding site when any two RBDs on the trimeric S-protein are in the "up" conformation and slightly rotated. This results in cross reactive binding between SARS-CoV-2 and SARS-CoV. SARS-CoV-2 has a conserved, epitope shared between SARS-CoV-2 and SARS-CoV. The availability of conserved epitopes would allow structure-based design of a SARS-CoV-2 vaccine and also of cross-protective antibody responses against future coronavirus epidemics and pandemics.
32245784
(Science)
PMID
32245784
Date of Publishing: 2020 May 8
Title A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Author(s) nameYuan M, Wu NC et al.
Journal Science
Impact factor
20.57
Citation count: 269