Evidence map›Paper›PMID 34396040›Full record

ArticleAntibody therapeutics2021

Application of an integrated computational antibody engineering platform to design SARS-CoV-2 neutralizers.

Saleh Riahi, Jae Hyeon Lee, Shuai Wei, Robert Cost, Alessandro Masiero, Catherine Prades, Reza Olfati-Saber, Maria Wendt, Anna Park, Yu Qiu and 1 more

Open access · goldAbstract read
In one paragraph

Article in Antibody therapeutics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 20% of its field
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

6 citing papers in PubMed, 18 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Saleh RiahiLarge Molecule Research, Sanofi, Framingham, MA, United States.
Jae Hyeon LeeData & Data Science, Sanofi, Cambridge, MA, United States.
Shuai WeiLarge Molecule Research, Sanofi, Framingham, MA, United States.
Robert CostLarge Molecule Research, Sanofi, Framingham, MA, United States.
Alessandro MasieroLarge Molecule Research, Sanofi, Vitry-sur-Seine, France.
Catherine PradesLarge Molecule Research, Sanofi, Vitry-sur-Seine, France.
Reza Olfati-SaberData & Data Science, Sanofi, Cambridge, MA, United States.
Maria WendtLarge Molecule Research, Sanofi, Framingham, MA, United States.
Anna ParkLarge Molecule Research, Sanofi, Framingham, MA, United States.
Yu QiuLarge Molecule Research, Sanofi, Framingham, MA, United States.ORCID 0000-0002-2078-0513
Yanfeng ZhouLarge Molecule Research, Sanofi, Framingham, MA, United States.
Sanofi (United States) · USSanofi (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As the COVID-19 pandemic continues to spread, hundreds of new initiatives including studies on existing medicines are running to fight the disease. To deliver a potentially immediate and lasting treatment to current and emerging SARS-CoV-2 variants, new collaborations and ways of sharing are required to create as many paths forward as possible. Here, we leverage our expertise in computational antibody engineering to rationally design/engineer three previously reported SARS-CoV neutralizing antibodies and share our proposal towards anti-SARS-CoV-2 biologics therapeutics. SARS-CoV neutralizing antibodies, m396, 80R and CR-3022 were chosen as templates due to their diversified epitopes and confirmed neutralization potency against SARS-CoV (but not SARS-CoV-2 except for CR3022). Structures of variable fragment (Fv) in complex with receptor binding domain (RBD) from SARS-CoV or SARS-CoV-2 were subjected to our established in silico antibody engineering platform to improve their binding affinity to SARS-CoV-2 and developability profiles. The selected top mutations were ensembled into a focused library for each antibody for further screening. In addition, we convert the selected binders with different epitopes into the trispecific format, aiming to increase potency and to prevent mutational escape. Lastly, to avoid antibody-induced virus activation or enhancement, we suggest application of NNAS and DQ mutations to the Fc region to eliminate effector functions and extend half-life.

Indexed as

antibodymachine learningengineeringstructure-basedengineeringtri-specificSARS-CoV-2antibody

Identifiers

PMID34396040
PMCPMC8344454
OpenAlexW3173444702

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.