ArticleInternational journal of molecular sciences2021
Does the SARS-CoV-2 Spike Protein Receptor Binding Domain Interact Effectively with the DPP4 (CD26) Receptor? A Molecular Docking Study.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- SARS-CoV-2 cell entry beyond the ACE2 receptor.Molecular biology reports · 2022Pooled it
- The role of DPP4 in viral infections: from receptor biology to antiviral target.Archives of virology · 2026Review
- Role of the DPP4 Receptor in SARS-CoV Entry: Insights From Docking and Molecular Dynamics Simulations.Proteins · 2025Article
- Potential Effects of Hyperglycemia on SARS-CoV-2 Entry Mechanisms in Pancreatic Beta Cells.Viruses · 2024Review
- Review
- Bioinformatic characterization of ENPEP, the gene encoding a potential cofactor for SARS-CoV-2 infection.PloS one · 2024Article
- Article
- Changes in Adenosine Deaminase Activity and Endothelial Dysfunction after Mild Coronavirus Disease-2019.International journal of molecular sciences · 2023Article
- Changes in intestinal morphology, number of mucus-producing cells and expression of coronavirus receptors APN, DPP4, ACE2 and TMPRSS2 in pigs with aging.Veterinary research · 2023Article
- Integrative network pharmacology and in silico analyses identify the anti-omicron SARS-CoV-2 potential of eugenol.Heliyon · 2023Article
- Effect of DPP4/CD26 expression on SARS‑CoV‑2 susceptibility, immune response, adenosine (derivatives mInternational journal of oncology · 2023Article
- Rebound increase in circulating dipeptidyl peptidase 4 (DPP4) enzyme activity after acute COVID-19.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Role of Dipeptidyl Peptidase-4 (DPP4) on COVID-19 Physiopathology.Biomedicines · 2022Review
- Methodology-Centered Review of Molecular Modeling, Simulation, and Prediction of SARS-CoV-2.Chemical reviews · 2022Review
- Going viral in the islet: mediators of SARS-CoV-2 entry beyond ACE2.Journal of molecular endocrinology · 2022Review
- Reply to "New-onset bullous pemphigoid after inactivated Covid-19 vaccine: Synergistic effect of the Covid-19 vaccine and vildagliptin".Dermatologic therapy · 2022Article
- Human Identical Sequences, hyaluronan, and hymecromone ─ the new mechanism and management of COVID-19.Molecular biomedicine · 2022Review
- Article
- Decreased circulating dipeptidyl peptidase-4 enzyme activity is prognostic for severe outcomes in COVID-19 inpatients.Biomarkers in medicine · 2022Observational
- Immune response and potential therapeutic strategies for the SARS-CoV-2 associated with the COVID-19 pandemic.International journal of biological sciences · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ACE2 has been established as the main receptor for SARS-CoV-2. Since other human coronaviruses are known to use co-receptors for viral cell entry, it has been suggested that DPP4 (CD26) could be a potential additional binding target or co-receptor, supported by early molecular docking simulation studies. However, recent biophysical studies have shown this interaction to be very weak. We have conducted detailed molecular docking simulations to predict the potential binding interactions between the receptor binding domain (RBD) of the spike protein of SARS-CoV-2 and DPP4 and compare them with the interactions observed in the experimentally determined structure of the complex of MERS-CoV with DPP4. Whilst the overall binding mode of the RBD of SARS-CoV-2 to DPP4 is predicted to be similar to that observed in the MERS-CoV-DPP4 complex, including a number of equivalent interactions, important differences in the amino acid sequences of SARS-CoV-2 and MERS-CoV result in substantially weakened interactions with DPP4. This is shown to arise from differences in the predicted proximity, nature and secondary structure at the binding interface on the RBD of SARS-CoV-2. These findings do not support DPP4 being a significant receptor for SARS-CoV-2.
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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 OpenQuestion graph.