Evidence map›Paper›PMID 33236008›Full record

ArticlebioRxiv : the preprint server for biology2020

An engineered receptor-binding domain improves the immunogenicity of multivalent SARS-CoV-2 vaccines.

Brian D Quinlan, Wenhui He, Huihui Mou, Lizhou Zhang, Yan Guo, Jing Chang, Shoujiao Peng, Amrita Ojha, Rubens Tavora, Mark S Parcells and 5 more

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 5 institutions in 2 countries.

Brian D QuinlanDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Wenhui HeDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Huihui MouDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Lizhou ZhangDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Yan GuoDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Jing ChangDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Shoujiao PengDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Amrita OjhaDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Rubens TavoraDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Mark S ParcellsDepartment of Animal and Food Sciences, University of Delaware, Newark, DE 19716, USA.
Guangxiang LuoDepartment of Microbiology, University of Alabama at Birmingham School Of Medicine, Birmingham, AL 35294, USA.
Wenhui LiNational Institute of Biological Sciences, Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China.
Guocai ZhongScripps Research | SZBL Chemical Biology Institute, Shenzhen Bay Laboratory (SZBL), Shenzhen, China.
Hyeryun ChoeDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Michael FarzanDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Scripps Research Institute · USPeking University · CNTsinghua University · CNUniversity of Alabama at Birmingham · USUniversity of Delaware · US

Funding

Optimizing eCD4-Ig for eradication and a functional cureR01AI129868 · NIAID · UNIVERSITY OF FLORIDA · PI FARZAN, MICHAEL R. · 2017 to 2021
$5.2M
NIAID NIH HHS R01 AI129868
6 · The paper itself

Abstract

The SARS-coronavirus 2 (SARS-CoV-2) spike (S) protein mediates viral entry into cells expressing the angiotensin-converting enzyme 2 (ACE2). The S protein engages ACE2 through its receptor-binding domain (RBD), an independently folded 197-amino acid fragment of the 1273-amino acid S-protein protomer. The RBD is the primary SARS-CoV-2 neutralizing epitope and a critical target of any SARS-CoV-2 vaccine. Here we show that this RBD conjugated to each of two carrier proteins elicited more potent neutralizing responses in immunized rodents than did a similarly conjugated proline-stabilized S-protein ectodomain. Nonetheless, the native RBD expresses inefficiently, limiting its usefulness as a vaccine antigen. However, we show that an RBD engineered with four novel glycosylation sites (gRBD) expresses markedly more efficiently, and generates a more potent neutralizing responses as a DNA vaccine antigen, than the wild-type RBD or the full-length S protein, especially when fused to multivalent carriers such as an

Identifiers

PMID33236008
PMCPMC7685318
OpenAlexW3099050566

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.