A research team at the Queensland University of Technology (QUT) in Australia has discovered a new binding site on the SARS-CoV-2 spike (S) protein, which could be used as a target for anticoagulant drugs.
To infect and enter a cell, the virus initially attaches the CoV-2 spike protein to heparan sulphate (HS) present on cell surfaces.
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The university noted that various studies focused on analysing HS interaction on the receptor-binding domain (RBD) and furin cleavage site of the S protein of the virus. These sites usually attach various therapies, vaccines and antibodies.
The newly detected binding site is on the N-terminal domain (NTD), which is a different region of the virus’s spike protein that aids in HS binding.
In addition, the NTD is a part of the spike protein that often mutates. Certain antibodies in the blood that neutralise the viruses attach to the same area of the NTD.
Targeting the NTD site using molecules such as the common anticoagulant drug, heparin or heparin mimetics could potentially hinder the viral attachment to cells and stop resultant infection, QUT noted.
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By GlobalDataHeparin or heparin mimetics are identical to HS.
QUT Centre for Genomics and Personalised Health Dr Neha Gandhi said that Covid-19 vaccines are not broadly accessible even though they are successful globally.
Gandhi said: “We need alternative antiviral strategies to prevent the spread of Covid-19 and treat infected people.”
Several SARS-CoV-2 variants have a positively charged mutation in the S protein.
As heparin or its mimetics are negatively charged, these molecules could help treat severe Covid-19 patients and against emerging viral variants.
In a separate development, ARCA biopharma has signed a patent assignment agreement with the University Medical Center of Johannes Gutenberg University Mainz in Germany.
According to the deal, ARCA will gain access to exclusive global patent rights to use recombinant protein therapy, rNAPc2, as a potential Covid-19 treatment and for other indications.
