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Coronaviruses and Integrin αvβ3: Does Thyroid Hormone Modify the Relationship?

Paul J DavisHung-Yun LinAleck HercbergsKelly A KeatingShaker A Mousa
Published in: Endocrine research (2020)
The viral binding domain of the integrin is near the Arg-Gly-Asp (RGD) peptide-binding site and RGD molecules can affect virus binding. In this same locale on integrin αvβ3 is the receptor for thyroid hormone analogues, particularly, L-thyroxine (T4). By binding to the integrin, T4 has been shown to modulate the affinity of the integrin for other proteins, to control internalization of αvβ3 and to regulate the expression of a panel of cytokine genes, some of which are components of the 'cytokine storm' of viral infections. If T4 does influence coronavirus uptake by target cells, other thyroid hormone analogues, such as deaminated T4 and deaminated 3,5,3'-triiodo-L-thyronine (T3), are candidate agents to block the virus-relevant actions of T4 at integrin αvβ3 and possibly restrict virus uptake.
Keyphrases
  • sars cov
  • cell adhesion
  • cell migration
  • poor prognosis
  • induced apoptosis
  • molecular docking
  • oxidative stress
  • genome wide
  • cell proliferation
  • gene expression
  • long non coding rna
  • transcription factor
  • cell death