About: Elicitation of potent neutralizing antibody responses by designed protein nanoparticle vaccines for SARS-CoV-2

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About: Elicitation of potent neutralizing antibody responses by designed protein nanoparticle vaccines for SARS-CoV-2 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Elicitation of potent neutralizing antibody responses by designed protein nanoparticle vaccines for SARS-CoV-2
Creator	Kellam, Paul Baric, Ralph Gralinski, Lisa Schäfer, Alexandra Veesler, David Walls, Alexandra Gully, Kendra Sheahan, Timothy Murphy, Michael Dinnon, Kenneth Chu, Helen Leist, Sarah Palser, Anne Lee, Kelly Pham, Minh Fuller, Deborah King, Neil Brown, Brieann Carter, Lauren Chalk, Sara Chen, Chengbo Chow, Cameron Fiala, Brooke Fuller, Jim Guttman, Miklos Hodge, Edgar Kepl, Elizabeth Kraft, John Lee, E-Chiang Lewis, Thomas Miranda, Marcos Navarro, Mary O'connor, Megan Ogohara, Cassandra Pepper, Marion Pettie, Deleah Ravichandran, Rashmi Shehata, Laila Sydeman, Claire Tse, Longping Wrenn, Samuel
Source	BioRxiv; Medline; PMC
abstract	A safe, effective, and scalable vaccine is urgently needed to halt the ongoing SARS-CoV-2 pandemic. Here, we describe the structure-based design of self-assembling protein nanoparticle immunogens that elicit potent and protective antibody responses against SARS-CoV-2 in mice. The nanoparticle vaccines display 60 copies of the SARS-CoV-2 spike (S) glycoprotein receptor-binding domain (RBD) in a highly immunogenic array and induce neutralizing antibody titers roughly ten-fold higher than the prefusion-stabilized S ectodomain trimer despite a more than five-fold lower dose. Antibodies elicited by the nanoparticle immunogens target multiple distinct epitopes on the RBD, suggesting that they may not be easily susceptible to escape mutations, and exhibit a significantly lower binding:neutralizing ratio than convalescent human sera, which may minimize the risk of vaccine-associated enhanced respiratory disease. The high yield and stability of the protein components and assembled nanoparticles, especially compared to the SARS-CoV-2 prefusion-stabilized S trimer, suggest that manufacture of the nanoparticle vaccines will be highly scalable. These results highlight the utility of robust antigen display platforms for inducing potent neutralizing antibody responses and have launched cGMP manufacturing efforts to advance the lead RBD nanoparticle vaccine into the clinic.
has issue date	2020-08-12(xsd:dateTime)
bibo:doi	10.1101/2020.08.11.247395
bibo:pmid	32817941
has license	cc-by-nd
sha1sum (hex)	2cabc8217e21c56c8ca804afb5355e91805cc8d2
schema:url	https://doi.org/10.1101/2020.08.11.247395
resource representing a document's title	Elicitation of potent neutralizing antibody responses by designed protein nanoparticle vaccines for SARS-CoV-2
has PubMed Central identifier	PMC7430571
has PubMed identifier	32817941
schema:publication	bioRxiv
resource representing a document's body	covid:2cabc8217e21c56c8ca804afb5355e91805cc8d2#body_text
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