Evidence map›Paper›PMID 38077689›Full record

ArticlePNAS nexus2023

A pan-SARS-CoV-2-specific soluble angiotensin-converting enzyme 2-albumin fusion engineered for enhanced plasma half-life and needle-free mucosal delivery.

Sopisa Benjakul, Aina Karen Anthi, Anette Kolderup, Marina Vaysburd, Heidrun Elisabeth Lode, Donna Mallery, Even Fossum, Elisabeth Lea Vikse, Anna Albecka, Aleksandr Ianevski and 10 more

Open access · goldAbstract read
In one paragraph

Article in PNAS nexus, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

5 citing papers in PubMed, 6 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

20 authors at 6 institutions in 5 countries.

Sopisa BenjakulDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0003-3708-8125
Aina Karen AnthiDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0002-1725-4571
Anette KolderupDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0003-4019-8069
Marina VaysburdProtein and Nucleic Acid Chemistry Division, Medical Research Council, Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID https://orcid.org/0000-0001-7236-678X
Heidrun Elisabeth LodeDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.
Donna MalleryProtein and Nucleic Acid Chemistry Division, Medical Research Council, Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID https://orcid.org/0000-0003-2713-5215
Even FossumDepartment of Virology, Norwegian Institute of Public Health, Oslo 0213, Norway.ORCID https://orcid.org/0000-0001-7064-0327
Elisabeth Lea VikseDepartment of Virology, Norwegian Institute of Public Health, Oslo 0213, Norway.
Anna AlbeckaProtein and Nucleic Acid Chemistry Division, Medical Research Council, Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID https://orcid.org/0000-0002-3672-5498
Aleksandr IanevskiDepartment of Clinical and Molecular Medicine, Norwegian University of Science and Technology, Trondheim 7491, Norway.ORCID https://orcid.org/0000-0002-7780-482X
Denis KainovDepartment of Clinical and Molecular Medicine, Norwegian University of Science and Technology, Trondheim 7491, Norway.ORCID https://orcid.org/0000-0001-7716-6955
Karine Flem KarlsenDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.
Siri Aastedatter SakyaDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0002-5893-6771
Mari Nyquist-AndersenDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0002-5248-6722
Torleif Tollefsrud GjølbergDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0002-1719-7677
Morten C MoeDepartment of Ophthalmology, Oslo University Hospital and University of Oslo, Oslo 0450, Norway.
Magnar BjøråsDepartment of Virology, Norwegian Institute of Public Health, Oslo 0213, Norway.ORCID https://orcid.org/0000-0001-8759-1170
Inger SandlieDepartment of Biosciences, University of Oslo, Oslo 0371, Norway.ORCID https://orcid.org/0009-0005-8063-0145
Leo C JamesProtein and Nucleic Acid Chemistry Division, Medical Research Council, Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Jan Terje AndersenDepartment of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo 0372, Norway.ORCID https://orcid.org/0000-0003-1710-1628
Oslo University Hospital · NOMRC Laboratory of Molecular Biology · GBNorwegian Institute of Public Health · NONorwegian University of Science and Technology · NOUniversity of Helsinki · FIUniversity of Oslo · NO

Funding

Medical Research Council MC_U105181010
6 · The paper itself

Abstract

Immunocompromised patients often fail to raise protective vaccine-induced immunity against the global emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants. Although monoclonal antibodies have been authorized for clinical use, most have lost their ability to potently neutralize the evolving Omicron subvariants. Thus, there is an urgent need for treatment strategies that can provide protection against these and emerging SARS-CoV-2 variants to prevent the development of severe coronavirus disease 2019. Here, we report on the design and characterization of a long-acting viral entry-blocking angiotensin-converting enzyme 2 (ACE2) dimeric fusion molecule. Specifically, a soluble truncated human dimeric ACE2 variant, engineered for improved binding to the receptor-binding domain of SARS-CoV-2, was fused with human albumin tailored for favorable engagement of the neonatal fragment crystallizable receptor (FcRn), which resulted in enhanced plasma half-life and allowed for needle-free transmucosal delivery upon nasal administration in human FcRn-expressing transgenic mice. Importantly, the dimeric ACE2-fused albumin demonstrated potent neutralization of SARS-CoV-2 immune escape variants.

Indexed as

ACE2FcRnhalf-lifemucosal deliverySARS-CoV-2

Identifiers

PMID38077689
PMCPMC10703496
OpenAlexW4389084064

What OpenQuestion 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 OpenQuestion graph.