CALGARY, Alberta, March 24, 2020 (GLOBE NEWSWIRE) -- Resverlogix Corp. ("Resverlogix" or the "Company") (TSX:RVX) is pleased to announce a March 23, 2020 bioRxiv publication that has shown apabetalone to inhibit specialized proteins – called bromodomain and extraterminal domain (BET) proteins – from interacting with a SARS-CoV-2 viral protein, with potential for limiting viral reproduction in human cells.

The article titled: “A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing” by Gordon et al, identified BRD2/4 as a binding partner of viral protein E. Apabetalone was shown to disrupt this interaction. A paragraph in the publication states the following about Bromodomain proteins: 

SARS-CoV-2 envelope interacts with bromodomain proteins

Surprisingly, we find that the transmembrane protein E binds to the bromodomain-containing proteins BRD2 and BRD4, potentially disrupting BRD-histone binding by mimicking histone structure. BRD2 is a member of the bromodomain and extra-terminal (BET) domain family whose members bind acetylated histones to regulate gene transcription. The N-terminus of histone 2A shares local sequence similarity over an alpha-helix of approximately 15 residues, some of which are in a transmembrane segment, of Protein E (Gordon et al., 2020, p.7).

“This novel research is certainly very encouraging and warrants additional testing of apabetalone, our investigational phase 3 clinical candidate with safety data in more than 4,000 subjects,” said Donald McCaffrey, President and CEO of Resverlogix. “Harnessing epigenetic modulation may be a potent tool in slowing down COVID-19 virus spread and disease severity, and as we announced yesterday, we would like to collaborate quickly with anyone who is testing drugs for COVID-19 in preclinical and clinical studies.”

Interested COVID-19 collaborators can contact:

Donald McCaffrey, President & CEO
don@resverlogix.com
1-587-390-7888