Login / Signup

Lactoferrin Binds through Its N-Terminus to the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein.

Patrik BabulicOndrej CehlárGabriela OndrovičováTetiana MoskaletsRostislav SkrabanaVladimir Leksa
Published in: Pharmaceuticals (Basel, Switzerland) (2024)
Since Coronavirus disease 2019 (COVID-19) still presents a considerable threat, it is beneficial to provide therapeutic supplements against it. In this respect, glycoprotein lactoferrin (LF) and lactoferricin (LFC), a natural bioactive peptide yielded upon digestion from the N-terminus of LF, are of utmost interest, since both have been shown to reduce infections of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the virus responsible for COVID-19, in particular via blockade of the virus priming and binding. Here, we, by means of biochemical and biophysical methods, reveal that LF directly binds to the S-protein of SARS-CoV-2. We determined thermodynamic and kinetic characteristics of the complex formation and mapped the mutual binding sites involved in this interaction, namely the N-terminal region of LF and the receptor-binding domain of the S-protein (RBD). These results may not only explain many of the observed protective effects of LF and LFC in SARS-CoV-2 infection but may also be instrumental in proposing potent and cost-effective supplemental tools in the management of COVID-19.
Keyphrases
  • sars cov
  • respiratory syndrome coronavirus
  • coronavirus disease
  • binding protein
  • protein protein
  • amino acid
  • gene expression
  • single cell
  • dna methylation
  • small molecule
  • anti inflammatory