Removal of clinically relevant SARS-CoV-2 variants by an affinity resin containing Galanthus nivalis agglutinin

The Coronavirus -19 (COVID-19) pandemic due to the SARS-CoV-2 virus has now exceeded two years in duration. The pandemic has been characterized by the development of a succession of variants containing mutations in the spike protein affecting infectiousness, virulence and efficacy of vaccines and monoclonal antibodies. Resistance to vaccination and limitations in the current treatments available require the ongoing development of therapies especially for those with severe disease. The plant lectin Galanthus nivalis binds to mannose structures in the viral envelope. We hypothesized that viral binding should be unaffected by spike protein mutations. Known concentrations of seven clinically relevant SARS-CoV-2 variants were spiked in medium and passed three times over columns containing 1 gm of GNA affinity resin. Percent decrease in viral titer was compared with a control sample. Viral capture efficiency was found to range from 53 to 89% for all variants. Extrapolation indicated that an adult Aethlon Hemopurifier (R) would have more than sufficient binding capacity for viral loads observed in adult patients with severe COVID-19 infection.

Automated summary

The COVID-19 pandemic caused by SARS-CoV-2 virus has lasted for over two years. The spike protein mutations have affected the infectiousness, virulence, and vaccine efficacy. The ongoing development of therapies is necessary, especially for severe cases. The plant lectin Galanthus nivalis can bind to the virus regardless of spike protein mutations. Experimental results showed that Galanthus nivalis had a viral capture efficiency ranging from 53% to 89% for various variants. Extrapolation indicated that Aethlon Hemopurifier (R) could effectively bind to viral loads in adult patients with severe COVID-19 infection.