ArticleThe Journal of biological chemistry2004
Structural characterization of the SARS-coronavirus spike S fusion protein core.
Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.
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129 citing papers in PubMed, 201 citations in OpenAlex.
- Mechanisms of antibody-dependent enhancement and its research progress in animal coronaviruses.Veterinary research · 2026Review
- CGM23 corresponds to a pan-coronavirus lipopeptide inhibitor potently inhibiting virion fusion.iScience · 2026Article
- The S2 subunit of spike encodes diverse targets for functional antibody responses to SARS-CoV-2.PLoS pathogens · 2024Article
- Molecular characterization of a novel variant of infectious bronchitis virus from field outbreaks in backyard chicken population of North East India.Virus genes · 2024Article
- Design and Assessment of a Novel In Silico Approach for Developing a Next-Generation Multi-Epitope Universal Vaccine Targeting Coronaviruses.Microorganisms · 2023Article
- Review
- Will Peptides Help to Stop COVID-19?Biochemistry. Biokhimiia · 2022Review
- Novel antiviral effects of chloroquine, hydroxychloroquine, and green tea catechins against SARS CoV-2 main protease (Mpro) and 3C-like protease for COVID-19 treatment.Clinical nutrition open science · 2022Review
- Perspective on the status and behaviour of SARS-CoV-2 in soil.Saudi journal of biological sciences · 2022Review
- Heptad stereotypy, S/Q layering, and remote origin of the SARS-CoV-2 fusion core.Virus evolution · 2022Article
- Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion.Science advances · 2021Article
- Cell Entry of Animal Coronaviruses.Viruses · 2021Review
- Biochemical composition, transmission and diagnosis of SARS-CoV-2.Bioscience reports · 2021Review
- Article
- Nanotherapeutics for treating coronavirus diseases.Journal of drug delivery science and technology · 2021Review
- Therapeutic approaches to coronavirus infection according to "One Health" concept.Research in veterinary science · 2021Review
- In Vitro Models for Studying Entry, Tissue Tropism, and Therapeutic Approaches of Highly Pathogenic Coronaviruses.BioMed research international · 2021Review
- SARS-COV-2 (COVID-19): Cellular and biochemical properties and pharmacological insights into new therapeutic developments.Cell biochemistry and function · 2021Review
- A Review of SARS-CoV2: Compared With SARS-CoV and MERS-CoV.Frontiers in medicine · 2021Review
- Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein,Frontiers in microbiology · 2021Article
69 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The spike (S) glycoprotein of coronaviruses mediates viral entry into host cells. It is a type 1 viral fusion protein that characteristically contains two heptad repeat regions, denoted HR-N and HR-C, that form coiled-coil structures within the ectodomain of the protein. Previous studies have shown that the two heptad repeat regions can undergo a conformational change from their native state to a 6-helix bundle (trimer of dimers), which mediates fusion of viral and host cell membranes. Here we describe the biophysical analysis of the two predicted heptad repeat regions within the severe acute respiratory syndrome coronavirus S protein. Our results show that in isolation the HR-N region forms a stable alpha-helical coiled coil that associates in a tetrameric state. The HR-C region in isolation formed a weakly stable trimeric coiled coil. When mixed together, the two peptide regions (HR-N and HR-C) associated to form a very stable alpha-helical 6-stranded structure (trimer of heterodimers). Systematic peptide mapping showed that the site of interaction between the HR-N and HR-C regions is between residues 916-950 of HR-N and residues 1151-1185 of HR-C. Additionally, interchain disulfide bridge experiments showed that the relative orientation of the HR-N and HR-C helices in the complex was antiparallel. Overall, the structure of the hetero-stranded complex is consistent with the structures observed for other type 1 viral fusion proteins in their fusion-competent state.
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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.