About: Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization

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About: Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization
Creator	Pizzorno, Andrés Rosa-Calatrava, Manuel Terrier, Olivier Maurer-Stroh, Sebastian Cheng, Yifan Wang, Bei Craik, Charles Hanson, Brendon Tan, Hwee Bohn, Markus Lee, Wen-Hsin Renia, Laurent Wang, Cheng-I Lyon, Bernard Asarnow, Daniel Bulkley, David Faust, Bryan Hu, Yuanyu Huang, Ching-Wen Lee, Chia Manglik, Aashish Minhat, Rabiatul Teo, Frannie Gek, Shirley Miang, Patricia Ng, Lon Seah, Kheng Soh, Kuen Xian, Eve Yeap, Chin Yee, Yvonne
Source	BioRxiv; Medline; PMC
abstract	In vitro antibody selection against pathogens from naïve combinatorial libraries can yield various classes of antigen-specific binders that are distinct from those evolved from natural infection(1–4). Also, rapid neutralizing antibody discovery can be made possible by a strategy that selects for those interfering with pathogen and host interaction(5). Here we report the discovery of antibodies that neutralize SARS-CoV-2, the virus responsible for the COVID-19 pandemic, from a highly diverse naïve human Fab library. Lead antibody 5A6 blocks the receptor binding domain (RBD) of the viral spike from binding to the host receptor angiotensin converting enzyme 2 (ACE2), neutralizes SARS-CoV-2 infection of Vero E6 cells, and reduces viral replication in reconstituted human nasal and bronchial epithelium models. 5A6 has a high occupancy on the viral surface and exerts its neutralization activity via a bivalent binding mode to the tip of two neighbouring RBDs at the ACE2 interaction interface, one in the “up” and the other in the “down” position, explaining its superior neutralization capacity. Furthermore, 5A6 is insensitive to several spike mutations identified in clinical isolates, including the D614G mutant that has become dominant worldwide. Our results suggest that 5A6 could be an effective prophylactic and therapeutic treatment of COVID-19.
has issue date	2020-07-15(xsd:dateTime)
bibo:doi	10.1101/2020.07.14.203414
bibo:pmid	32699850
has license	cc-by-nc-nd
sha1sum (hex)	970be954199e69daf74ea7a503ed35ff7b04ec88
schema:url	https://doi.org/10.1101/2020.07.14.203414
resource representing a document's title	Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization
has PubMed Central identifier	PMC7373131
has PubMed identifier	32699850
schema:publication	bioRxiv
resource representing a document's body	covid:970be954199e69daf74ea7a503ed35ff7b04ec88#body_text
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