scholarly journals Potent Neutralization of MERS-CoV by Human Neutralizing Monoclonal Antibodies to the Viral Spike Glycoprotein

2014 ◽  
Vol 6 (234) ◽  
pp. 234ra59-234ra59 ◽  
Author(s):  
L. Jiang ◽  
N. Wang ◽  
T. Zuo ◽  
X. Shi ◽  
K.-M. V. Poon ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Spike Glycoprotein ◽  
Potent Neutralization

scholarly journals Identification of Novel Neutralizing Monoclonal Antibodies against SARS-CoV-2 Spike Glycoprotein

2021 ◽  
Author(s):  
Devivasha Bordoloi ◽  
Ziyang Xu ◽  
Michelle Ho ◽  
Mansi Purwar ◽  
Pratik Bhojnagarwala ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Spike Glycoprotein

scholarly journals Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Antoni G. Wrobel ◽  
Donald J. Benton ◽  
Saira Hussain ◽  
Ruth Harvey ◽  
Stephen R. Martin ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibodies ◽  
Antibody Binding ◽  
Spike Glycoprotein ◽  
Cryo Electron Microscopy

Abstract The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.

scholarly journals Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529

2021 ◽  
Author(s):  
Tongqing Zhou ◽  
Lingshu Wang ◽  
John Misasi ◽  
Amarendra Pegu ◽  
Yi Zhang ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Structural Basis ◽  
Resistance Mutations ◽  
Binding Surface ◽  
New Variant ◽  
Rapid Spread ◽  
Structural Mechanisms ◽  
The Impact ◽  
Insight Into ◽  
Potent Neutralization

With B.1.1.529 SARS-CoV-2 variant's rapid spread and substantially increased resistance to neutralization by vaccinee and convalescent sera, monoclonal antibodies with potent neutralization are eagerly sought. To provide insight into effective neutralization, we determined cryo-EM structures and evaluated potent receptor-binding domain (RBD) antibodies for their ability to bind and neutralize this new variant. B.1.1.529 RBD mutations altered 16% of the RBD surface, clustering on a ridge of this domain proximal to the ACE2-binding surface and reducing binding of most antibodies. Significant inhibitory activity was retained, however, by select monoclonal antibodies including A19-58.1, B1-182.1, COV2-2196, S2E12, A19-46.1, S309 and LY-CoV1404, which accommodated these changes and neutralized B.1.1.529 with IC50s between 5.1-281 ng/ml, and we identified combinations of antibodies with potent synergistic neutralization. Structure-function analyses delineated the impact of resistance mutations and revealed structural mechanisms for maintenance of potent neutralization against emerging variants.

scholarly journals Towards a solution to MERS: protective human monoclonal antibodies targeting different domains and functions of the MERS-coronavirus spike glycoprotein

2019 ◽  
Vol 8 (1) ◽  
pp. 516-530 ◽  
Author(s):  
Ivy Widjaja ◽  
Chunyan Wang ◽  
Rien van Haperen ◽  
Javier Gutiérrez-Álvarez ◽  
Brenda van Dieren ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Spike Glycoprotein ◽  
Human Monoclonal Antibodies

scholarly journals Potent Neutralization Antibodies Induced by a Recombinant Trimeric Spike Protein Vaccine Candidate Containing PIKA Adjuvant for COVID-19

Vaccines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 296
Author(s):  
Jiao Tong ◽  
Chenxi Zhu ◽  
Hanyu Lai ◽  
Chunchao Feng ◽  
Dapeng Zhou
Keyword(s):  
Monoclonal Antibodies ◽  
Vaccine Candidate ◽  
Spike Protein ◽  
Heptad Repeat ◽  
Peptide Array ◽  
Receptor Binding Domain ◽  
Protein Vaccine ◽  
Direct Binding ◽  
Linear Epitopes ◽  
Potent Neutralization

The structures of immunogens that elicit the most potent neutralization antibodies to prevent COVID-19 infection are still under investigation. In this study, we tested the efficacy of a recombinant trimeric Spike protein containing polyI:C (PIKA) adjuvant in mice immunized by a 0–7–14 day schedule. The results showed that a Spike protein-specific antibody was induced at Day 21 with titer of above 50,000 on average, as measured by direct binding. The neutralizing titer was above 1000 on average, as determined by a pseudo-virus using monoclonal antibodies (40592-MM57 and 40591-MM43) with IC50 at 1 μg/mL as standards. The protein/peptide array-identified receptor-binding domain (RBD) was considered as immunodominant. No linear epitopes were found in the RBD, although several linear epitopes were found in the C-terminal domain right after the RBD and heptad repeat regions. Our study supports the efficacy of a recombinant trimeric Spike protein vaccine candidate for COVID-19 that is safe and ready for storage and distribution in developing countries.

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