Human enzyme DPP4 does not enable COVID-19 infection

Research from the Centenary Institute has found that the human enzyme dipeptidyl peptidase (DPP4) does not bind to the spike protein of the SARS-CoV-2 virus and so cannot enable COVID-19 infection in our bodies.

DPP4, which is known to be the key receptor for the MERS-coronavirus (Middle East respiratory syndrome), had been identified as a potential binding target of the SARS-CoV-2 spike protein. The spike protein forms the spikes of the ‘crown’ after which coronaviruses are named. If DPP4 had been able to bind, it would have suggested an alternate port of entry for SARS-CoV-2 into human cells, thus exacerbating COVID-19.

“We already know that SARS-CoV-2 cell entry depends on the interaction between the virus’ spike and the human enzyme ACE2. We needed to find out if DPP4 was also acting as a gateway for COVID-19,” said senior author on the paper, Professor Mark Gorrell, Head of the Liver Enzymes in Metabolism and Inflammation Program at the Centenary Institute.

“Our findings however put to rest the suggestion that DPP4 could be a co-receptor or alternate receptor for SARS-CoV-2 entry. There was no binding detected between the two molecules in our study and so we can be reassured that ACE2 is the sole method for SARS infection.”

The publication, which is in pre-print, is accessible online: A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2.

Further Information on the Centenary Institute’s coronavirus activity can be found here.