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Related Concept Videos

G Protein-coupled Receptors01:15

G Protein-coupled Receptors

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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Regulation of Nuclear Protein Sorting01:45

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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High-throughput Confocal Imaging of Quantum Dot-Conjugated SARS-CoV-2 Spike Trimers to Track Binding and Endocytosis in HEK293T Cells
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SARS-Cov2 S Protein Features Potential Estrogen Binding Site.

Ante Tomasović1, Damir Stanzer1, Ivan Krešimir Svetec1

  • 1Faculty of Food Technology and Biotechnology, University of Zagreb, Pierottijeva 6, 10000 Zagreb, Croatia.

Food Technology and Biotechnology
|June 4, 2021
PubMed
Summary

Estrogen may directly impact SARS-CoV-2 infectivity by binding to the virus's S protein. This preliminary finding suggests a potential therapeutic target for reducing COVID-19 severity in men.

Keywords:
S proteinSARS-CoV2coronavirusestradiolestrogenestrogen binding site

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Area of Science:

  • Virology
  • Molecular Biology
  • Endocrinology

Background:

  • Sex-based differences in COVID-19 severity are observed, with women generally experiencing milder symptoms.
  • Estrogen's role in immune response modulation is known, prompting investigation into its direct effects on SARS-CoV-2.

Purpose of the Study:

  • To investigate the potential for estrogen to bind directly to the SARS-CoV-2 surface glycoprotein (S protein).
  • To explore if estrogen binding to the S protein could influence viral infectivity.

Main Methods:

  • Comparative sequence analysis using BLAST and HHpred between SARS-CoV-2 S protein and human estrogen receptor beta (ER β).
  • 3D structural visualization and comparison of potential estrogen binding sites on the S protein and the active site of ER β using PyMOL.
  • Control comparison with the human androgen receptor.

Main Results:

  • Identification of a potential estrogen binding site on the SARS-CoV-2 S protein.
  • Structural similarities were found between the potential estrogen binding site on the S protein and the active site of ER β.
  • No similar binding sites were identified when comparing the S protein to the human androgen receptor.

Conclusions:

  • The SARS-CoV-2 S protein possesses a potential estrogen binding site, structurally similar to the estrogen receptor.
  • This binding site is located in the S2 superfamily domain, crucial for viral entry.
  • Further research is warranted to confirm estrogen binding and its impact on SARS-CoV-2 infectivity and disease severity.