ArticleExploration (Beijing, China)2024
A novel nanobody broadly neutralizes SARS-CoV-2 via induction of spike trimer dimers conformation.
Article in Exploration (Beijing, China), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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.
Who cites it
13 citing papers in PubMed.
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- JMJD6-mediated epigenetic silencing of innate immunity promotes pseudorabies virus replication.Journal of virology · 2026Article
- Review
- Enhanced antibody response to the conformational non-RBD regionEmerging microbes & infections · 2025Article
- Design of MOFs-based spatially confined catalysis-driven intelligent responsive photoacoustic probe for deep-tissue HMikrochimica acta · 2025Article
- Antiviral nanomedicine: Advantages, mechanisms and advanced therapies.Bioactive materials · 2025Review
- Lycopene Inhibits PRRSV Replication by Suppressing ROS Production.International journal of molecular sciences · 2025Article
- GRP78 Nanobody-Directed Immunotoxin Activates Innate Immunity Through STING Pathway to Synergize Tumor Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Potent bivalent nanobody constructs that protect against the SARS-CoV-2 XBB variant.Npj viruses · 2025Article
- A cell-penetrating bispecific antibody suppresses hepatitis B virus replication and secretion.Virus research · 2025Article
- Identification of mpox M1R and B6R monoclonal and bispecific antibodies that efficiently neutralize authentic mpox virus.Emerging microbes & infections · 2024Article
- Reduced graphene oxide loaded with tetrahedral framework nucleic acids for combating orthodontically induced root resorption.Journal of nanobiotechnology · 2024Article
- A novel nanobody broadly neutralizes SARS-CoV-2 via induction of spike trimer dimers conformation.Exploration (Beijing, China) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ongoing mutations of the SARS-CoV-2 pose serious challenges to the efficacy of the available antiviral drugs, and new drugs with fantastic efficacy are always deserved investigation. Here, a nanobody called IBT-CoV144 is reported, which exhibits broad neutralizing activity against SARS-CoV-2 by inducing the conformation of spike trimer dimers. IBT-CoV144 was isolated from an immunized alpaca using the RBD of wild-type SARS-CoV-2, and it showed strong cross-reactive binding and neutralizing potency against diverse SARS-CoV-2 variants, including Omicron subvariants. Moreover, the prophylactically and therapeutically intranasal administration of IBT-CoV144 confers fantastic protective efficacy against the challenge of Omicron BA.1 variant in BALB/c mice model. The structure analysis of the complex between spike (S) protein, conducted using Cryo-EM, revealed a special conformation known as the trimer dimers. This conformation is formed by two trimers, with six RBDs in the "up" state and bound by six VHHs. IBT-CoV144 binds to the lateral region of the RBD on the S protein, facilitating the aggregation of S proteins. This aggregation results in steric hindrance, which disrupts the recognition of the virus by ACE2 on host cells. The discovery of IBT-CoV144 will provide valuable insights for the development of advanced therapeutics and the design of next-generation vaccines.
Indexed as
Identifiers
What Socratic holds
Registered trials
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.