Evidence map›Paper›PMID 40919754›Full record

ArticleBiomacromolecules2025

Engineering a Coiled-Coil Protein for DARPin Presentation as a Potent SARS-CoV-2 Therapeutic.

Linh D Mai, Narayanaiah Cheedarla, Siamalan Krishnathas, Ishmamul H Sadab, Mikaela A Gray, Wei Lv, Anshul Dhankher, John D Roback, Andrew S Neish, Julie A Champion

Abstract read
In one paragraph

Article in Biomacromolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Linh D MaiSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Dr NW, Atlanta, Georgia 30332, United States.ORCID 0009-0002-4924-0876
Narayanaiah CheedarlaSchool of Medicine, Emory University, 100 Woodruff Circle, Atlanta, Georgia 30322, United States.
Siamalan KrishnathasSchool of Materials Science and Engineering, Georgia Institute of Technology, 771 Ferst Drive, Atlanta, Georgia 30332, United States.
Ishmamul H SadabSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Dr NW, Atlanta, Georgia 30332, United States.
Mikaela A GraySchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Dr NW, Atlanta, Georgia 30332, United States.ORCID 0000-0002-4814-1844
Wei LvSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Dr NW, Atlanta, Georgia 30332, United States.
Anshul DhankherSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Dr NW, Atlanta, Georgia 30332, United States.
John D RobackSchool of Medicine, Emory University, 100 Woodruff Circle, Atlanta, Georgia 30322, United States.
Andrew S NeishSchool of Medicine, Emory University, 100 Woodruff Circle, Atlanta, Georgia 30322, United States.
Julie A ChampionSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Dr NW, Atlanta, Georgia 30332, United States.ORCID 0000-0002-0260-9392

Funding

Project-004U54CA260563 · NCI · EMORY UNIVERSITY · PI DHODAPKAR, MADHAV V, SANZ, IGNACIO E. · 2020 to 2024
$10.2M
Design and evaluation of a multivalent nanobody construct for prevention or treatment of SARS-CoV-2R21EB031597 · NIBIB · GEORGIA INSTITUTE OF TECHNOLOGY · PI CHAMPION, JULIE · 2021 to 2021
$397k
NCI NIH HHS U54 CA260563NIBIB NIH HHS R21 EB031597
6 · The paper itself

Abstract

The COVID-19 pandemic has demonstrated the need for rapid, flexible, and readily adaptable treatment options for future pandemic preparedness. Due to the speed at which viruses like SARS-CoV-2 mutate, the customary approach of using highly specific monoclonal antibodies as neutralization therapies is challenging, given their size, production complexity, and cost. Here, we leveraged rational protein design to create fusion proteins from small, antibody-mimetic proteins, Designed Ankyrin Repeat Proteins (DARPins) and a self-assembling hexameric coiled coil (CC-HEX). The fusion proteins are modular, suitable to rapidly adapt to new variants or pathogens, and enable the incorporation of both viral and serum albumin-binding functions. We demonstrated potent neutralization by HEX-DARPins against multiple variants of the SARS-CoV-2 pseudovirus. Albumin binding prolonged serum concentration and improved delivery to the lungs in mice. This work establishes HEX-DARPin fusion proteins as potential therapeutics for the treatment of COVID-19 and as a platform for the development of drugs against future viral pathogens.

Indexed as

COVID-19 Drug TreatmentProtein EngineeringRecombinant Fusion ProteinsSARS-CoV-2AnimalsAnkyrin RepeatAntibodies, NeutralizingCOVID-19FemaleHumansMiceAntibodies, NeutralizingRecombinant Fusion Proteins

Identifiers

PMID40919754
PMCPMC12522135

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.