Compounds in hemp block COVID-19 from entering human cells, study says. - https://okcfox.com/news/nation-world/compounds-in-hemp-block-covid-19-from-entering-human-cells-study-says
CORVALLIS, Ore. (KVAL) — Compounds found in hemp "show the ability to prevent the virus that causes COVID-19 from entering human cells," Oregon State University says.
New OSU research on hemp and COVID-19 was published Tuesday in the Journal of Natural Products. Richard van Breemen, a researcher with Oregon State’s Global Hemp Innovation Center in the College of Pharmacy and Linus Pauling Institute, led the study.
Van Breemen and collaborators, including scientists at Oregon Health & Science University, found that a pair of cannabinoid acids bind to the SARS-CoV-2 spike protein, blocking a critical step in the process the virus uses to infect people.
The compounds are cannabigerolic acid, or CBGA, and cannabidiolic acid, CBDA, and the spike protein is the same drug target used in COVID-19 vaccines and antibody therapy. A drug target is any molecule critical to the process a disease follows, meaning its disruption can thwart infection or disease progression.
“These cannabinoid acids are abundant in hemp and in many hemp extracts,” van Breemen said. “They are not controlled substances like THC, the psychoactive ingredient in marijuana, and have a good safety profile in humans. And our research showed the hemp compounds were equally effective against variants of SARS-CoV-2, including variant B.1.1.7, which was first detected in the United Kingdom, and variant B.1.351, first detected in South Africa.”
Characterized by crown-like protrusions on its outer surface, SARS-CoV-2 features RNA strands that encode its four main structural proteins – spike, envelope, membrane and nucleocapsid – as well as 16 nonstructural proteins and several “accessory” proteins, van Breemen said.
“Any part of the infection and replication cycle is a potential target for antiviral intervention, and the connection of the spike protein’s receptor binding domain to the human cell surface receptor ACE2 is a critical step in that cycle,” he said. “That means cell entry inhibitors, like the acids from hemp, could be used to prevent SARS-CoV-2 infection and also to shorten infections by preventing virus particles from infecting human cells. They bind to the spike proteins so those proteins can’t bind to the ACE2 enzyme, which is abundant on the outer membrane of endothelial cells in the lungs and other organs.”
Van Breem said, "using compounds that block virus-receptor interaction has been helpful for patients with other viral infections" including HIV-1 and hepatitis.
The ligand-receptor complexes are then filtered from the non-binding molecules using one of several methods.
“We identified several cannabinoid ligands and ranked them by affinity to the spike protein,” van Breemen said. “The two cannabinoids with the highest affinities for the spike protein were CBDA and CGBA, and they were confirmed to block infection.
“One of the primary concerns in the pandemic is the spread of variants, of which there are many, and B.1.1.7 and B.1.351 are among the most widespread and concerning,” he added. “These variants are well known for evading antibodies against early lineage SARS-CoV-2, which is obviously concerning given that current vaccination strategies rely on the early lineage spike protein as an antigen. Our data show CBDA and CBGA are effective against the two variants we looked at, and we hope that trend will extend to other existing and future variants.”
Van Breemen noted that "resistant variants could still arise amid widespread use of cannabinoids but that the combination of vaccination and CBDA/CBGA treatment should make for a much more challenging environment for SARS-CoV-2."
“Our earlier research reported on the discovery of another compound, one from licorice, that binds to the spike protein too,” he said. “However, we did not test that compound, licochalcone A, for activity against the live virus yet. We need new funding for that.”
Read full study here - https://pubmed.ncbi.nlm.nih.gov/35007072/