ArticleJournal of molecular biology2009
Structural insights into immune recognition of the severe acute respiratory syndrome coronavirus S protein receptor binding domain.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Biophysics of SARS-CoV-2 spike protein's receptor-binding domain interaction with ACE2 and neutralizing antibodies: from computation to functional insights.Biophysical reviews · 2025Review
- Effect of Hard- and Soft-Density Insoles on the Postural Control of Adults over 65 Years of Age: A Cross over Clinical Trial.Bioengineering (Basel, Switzerland) · 2024Article
- Design of the SARS-CoV-2 RBD vaccine antigen improves neutralizing antibody response.Science advances · 2022Article
- An Insight Into Detection Pathways/Biosensors of Highly Infectious Coronaviruses.Molecular biotechnology · 2022Review
- Review
- In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies.Cell · 2021Article
- Computational design and modeling of nanobodies toward SARS-CoV-2 receptor binding domain.Chemical biology & drug design · 2021Article
- Review of COVID-19 Antibody Therapies.Annual review of biophysics · 2021Article
- Population Dynamics and Structural Effects at Short and Long Range Support the Hypothesis of the Selective Advantage of the G614 SARS-CoV-2 Spike Variant.Molecular biology and evolution · 2021Article
- Nano-size dependence in the adsorption by the SARS-CoV-2 spike protein over gold colloid.Colloids and surfaces. A, Physicochemical and engineering aspects · 2021Article
- Potential neutralizing antibodies discovered for novel corona virus using machine learning.Scientific reports · 2021Article
- A high-throughput liquid bead array assay confirms strong correlation between SARS-CoV-2 antibody level and COVID-19 severity.iScience · 2021Article
- Structural Analysis of Neutralizing Epitopes of the SARS-CoV-2 Spike to Guide Therapy and Vaccine Design Strategies.Viruses · 2021Review
- SAS: A Platform of Spike Antigenicity for SARS-CoV-2.Frontiers in cell and developmental biology · 2021Article
- Comparative Immunomodulatory Evaluation of the Receptor Binding Domain of the SARS-CoV-2 Spike Protein; a Potential Vaccine Candidate Which Imparts Potent Humoral and Th1 Type Immune Response in a Mouse Model.Frontiers in immunology · 2021Article
- Spectroscopic investigation on the affinity of SARS-CoV-2 spike protein to gold nano-particles.Colloid and interface science communications · 2021Article
- A novel rapid detection for SARS-CoV-2 spike 1 antigens using human angiotensin converting enzyme 2 (ACE2).Biosensors & bioelectronics · 2021Article
- Could SARS-CoV-2-induced lung injury be attenuated by vitamin D?International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2021Article
- Genetic Risk Factors for the Development of COVID-19 Coronavirus Infection.Russian journal of genetics · 2021Article
- Immunotherapeutic approaches to curtail COVID-19.International immunopharmacology · 2020Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for host cell attachment and fusion of the viral and host cell membranes. Within S the receptor binding domain (RBD) mediates the interaction with angiotensin-converting enzyme 2 (ACE2), the SARS-CoV host cell receptor. Both S and the RBD are highly immunogenic and both have been found to elicit neutralizing antibodies. Reported here is the X-ray crystal structure of the RBD in complex with the Fab of a neutralizing mouse monoclonal antibody, F26G19, elicited by immunization with chemically inactivated SARS-CoV. The RBD-F26G19 Fab complex represents the first example of the structural characterization of an antibody elicited by an immune response to SARS-CoV or any fragment of it. The structure reveals that the RBD surface recognized by F26G19 overlaps significantly with the surface recognized by ACE2 and, as such, suggests that F26G19 likely neutralizes SARS-CoV by blocking the virus-host cell interaction.
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