Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion protein

10 Nov 2021

Abstract excerpt

SARS-CoV-2 enters host cells after binding through its spike glycoprotein to the angiotensin-converting enzyme 2 (ACE2) receptor. Soluble ACE2 ectodomains bind and neutralize the virus, yet their short in vivo half-live limits their therapeutic use. This limitation can be overcome by fusing the fragment crystallizable (Fc) part of human immunoglobulin G (IgG) to the ACE2 ectodomain, but this bears the risk of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Complement system in diseases
Share to Monoclonal and Polyclonal Antibodies Research
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34774603
DOI: 10.1016/j.antiviral.2021.105197

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion proteinPMID 34774603Read ↗

Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion proteinSemantic proximity Read ↗

A tetrameric ACE2 protein broadly neutralizes SARS-CoV-2 spike variants of concern with elevated potency.Semantic proximity Read ↗

David versus goliath: ACE2-Fc receptor traps as potential SARS-CoV-2 inhibitorsSemantic proximity Read ↗

Characterization of a Novel ACE2-Based Therapeutic with Enhanced Rather than Reduced Activity against SARS-CoV-2 Variants.Semantic proximity Read ↗

ACE2-based decoy receptors for SARS coronavirus 2.Semantic proximity Read ↗

ACE2-IgG1 fusions with improved in vitro and in vivo activity against SARS-CoV-2Semantic proximity Read ↗

Engineered ACE2-Fc counters murine lethal SARS-CoV-2 infection through direct neutralization and Fc-effector activitiesSemantic proximity Read ↗

DESIGN OF A CHIMERIC ACE-2/Fc-SILENT FUSION PROTEIN WITH ULTRAHIGH AFFINITY AND NEUTRALIZING CAPACITY FOR SARS-CoV-2 VARIANTSSemantic proximity Read ↗

Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig.Semantic proximity Read ↗

SARS-CoV-2 receptor binding domain fusion protein efficiently neutralizes virus infectionSemantic proximity Read ↗

ACE2-Fc fusion protein overcomes viral escape by potently neutralizing SARS-CoV-2 variants of concernSemantic proximity Read ↗

Characterisation of a novel ACE2-based therapeutic with enhanced rather than reduced activity against SARS-CoV2 variantsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.