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A broadly-neutralizing antibody against glycoprotein that potentiates the breadth and neutralization potency of other antibodies.

作者信息

Donnellan Francesca R, Rayaprolu Vamseedhar, Rijal Pramila, O'Dowd Victoria, Parvate Amar, Callaway Heather, Hariharan Chitra, Parekh Dipti, Hui Sean, Shaffer Kelly, Avalos Ruben Diaz, Hastie Kathryn, Schimanski Lisa, Müller-Kräuter Helena, Strecker Thomas, Balaram Ariane, Halfmann Peter, Saphire Erica Ollmann, Lightwood Daniel J, Townsend Alain R, Draper Simon J

机构信息

Department of Biochemistry, University of Oxford, Dorothy Crowfoot Hodgkin Building, Oxford, OX1 3QU, UK.

Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, University of Oxford, Oxford, OX1 3QU, UK.

出版信息

bioRxiv. 2024 Jun 25:2024.06.21.600001. doi: 10.1101/2024.06.21.600001.

DOI:10.1101/2024.06.21.600001
PMID:38979279
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11230233/
Abstract

Ebolavirus disease (EVD) is caused by multiple species of . Monoclonal antibodies (mAbs) against the virus glycoprotein (GP) are the only class of therapeutic approved for treatment of EVD caused by (EBOV). Therefore, mAbs targeting multiple species may represent the next generation of EVD therapeutics. Broadly reactive anti-GP mAbs were produced; among these, mAbs 11886 and 11883 were broadly neutralizing . A 3.0 Å cryo-electron microscopy structure of EBOV GP bound to both mAbs shows that 11886 binds a novel epitope bridging the glycan cap (GC), 3 pocket and GP2 N-terminus, whereas 11883 binds the receptor binding region (RBR) and GC. , 11886 synergized with a range of mAbs with epitope specificities spanning the RBR/GC, including 11883. Notably, 11886 increased the breadth of neutralization by partner mAbs against different species. These data provide a strategic route to design improved mAb-based next-generation EVD therapeutics.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/335babefbc47/nihpp-2024.06.21.600001v1-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/fa08dcdde621/nihpp-2024.06.21.600001v1-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/8edd17ef3946/nihpp-2024.06.21.600001v1-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/b53a25cd0a45/nihpp-2024.06.21.600001v1-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/955f98e30661/nihpp-2024.06.21.600001v1-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/24d109d165f2/nihpp-2024.06.21.600001v1-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/32daacf7ef38/nihpp-2024.06.21.600001v1-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/335babefbc47/nihpp-2024.06.21.600001v1-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/fa08dcdde621/nihpp-2024.06.21.600001v1-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/8edd17ef3946/nihpp-2024.06.21.600001v1-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/b53a25cd0a45/nihpp-2024.06.21.600001v1-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/955f98e30661/nihpp-2024.06.21.600001v1-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/24d109d165f2/nihpp-2024.06.21.600001v1-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/32daacf7ef38/nihpp-2024.06.21.600001v1-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7d8d/11230233/335babefbc47/nihpp-2024.06.21.600001v1-f0007.jpg

相似文献

[1]
A broadly-neutralizing antibody against glycoprotein that potentiates the breadth and neutralization potency of other antibodies.

bioRxiv. 2024-6-25

[2]
Mapping of Ebolavirus Neutralization by Monoclonal Antibodies in the ZMapp Cocktail Using Cryo-Electron Tomography and Studies of Cellular Entry.

J Virol. 2016-8-12

[3]
Proteo-Genomic Analysis Identifies Two Major Sites of Vulnerability on Ebolavirus Glycoprotein for Neutralizing Antibodies in Convalescent Human Plasma.

Front Immunol. 2021

[4]
Development and Characterization of Neutralizing Antibodies Against Zaire Ebolavirus Glycoprotein and Protein 40.

Cell Physiol Biochem. 2018

[5]
Mechanism of Binding to Ebola Virus Glycoprotein by the ZMapp, ZMAb, and MB-003 Cocktail Antibodies.

J Virol. 2015-11

[6]
Novel Cross-Reactive Monoclonal Antibodies against Ebolavirus Glycoproteins Show Protection in a Murine Challenge Model.

J Virol. 2017-7-27

[7]
Antibody-Mediated Protective Mechanisms Induced by a Trivalent Parainfluenza Virus-Vectored Ebolavirus Vaccine.

J Virol. 2019-2-5

[8]
Improving neutralization potency and breadth by combining broadly reactive HIV-1 antibodies targeting major neutralization epitopes.

J Virol. 2015-3

[9]
Analysis of a Therapeutic Antibody Cocktail Reveals Determinants for Cooperative and Broad Ebolavirus Neutralization.

Immunity. 2020-2-4

[10]
Structural Basis of Pan-Ebolavirus Neutralization by a Human Antibody against a Conserved, yet Cryptic Epitope.

mBio. 2018-9-11

本文引用的文献

[1]
Analysis of the diverse antigenic landscape of the malaria protein RH5 identifies a potent vaccine-induced human public antibody clonotype.

Cell. 2024-9-5

[2]
Perspectives on Advancing Countermeasures for Filovirus Disease: Report From a Multisector Meeting.

J Infect Dis. 2023-11-13

[3]
A review of broadly protective monoclonal antibodies to treat Ebola virus disease.

Curr Opin Virol. 2023-8

[4]
Structure of the Inmazeb cocktail and resistance to Ebola virus escape.

Cell Host Microbe. 2023-2-8

[5]
Development and Structural Analysis of Antibody Therapeutics for Filoviruses.

Pathogens. 2022-3-18

[6]
Asymmetric and non-stoichiometric glycoprotein recognition by two distinct antibodies results in broad protection against ebolaviruses.

Cell. 2022-3-17

[7]
Cocktail party: Low-dose antibody combinations deliver pan-ebolavirus protection.

Cell. 2022-3-17

[8]
Cross-Neutralisation of Novel Bombali Virus by Ebola Virus Antibodies and Convalescent Plasma Using an Optimised Pseudotype-Based Neutralisation Assay.

Trop Med Infect Dis. 2021-8-25

[9]
Ansuvimab: First Approval.

Drugs. 2021-4

[10]
Atypical Ebola Virus Disease in a Nonhuman Primate following Monoclonal Antibody Treatment Is Associated with Glycoprotein Mutations within the Fusion Loop.

mBio. 2021-1-12

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