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bioRxiv · 10.1101/2021.02.22.432402

Human basigin (CD147) does not directly interact with SARS-CoV-2 spike glycoprotein

Ragotte, R. J.·Pulido, D.·Donnellan, F. R.·Gorini, G.·Davies, H.·Brun, J.·King, L. D.·Skinner, K.·Draper, S. J.
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Abstract

Basigin, or CD147, has been reported as a co-receptor used by SARS-CoV-2 to invade host cells. Basigin also has a well-established role in Plasmodium falciparum malaria infection of human erythrocytes where it is bound by one of the parasites invasion ligands, reticulocyte binding protein homolog 5 (RH5). Here, we sought to validate the claim that the receptor binding domain (RBD) of SARS-CoV-2 spike glycoprotein can form a complex with basigin, using RH5-basigin as a positive control. Using recombinantly expressed proteins, size exclusion chromatography and surface plasmon resonance, we show that neither RBD nor full-length spike glycoprotein bind to recombinant human basigin (either expressed in E. coli or mammalian cells). Given the immense interest in SARS-CoV-2 therapeutic targets, we would caution the inclusion of basigin in this list on the basis of its reported direct interaction with SARS-CoV-2 spike glycoprotein. ImportanceReducing the mortality and morbidity associated with COVID-19 remains a global health priority. Critical to these efforts is the identification of host factors that are essential to viral entry and replication. Basigin, or CD147, was previously identified as a possible therapeutic target based on the observation that it may act as a co-receptor for SARS-COV-2, binding to the receptor binding domain of the spike protein. Here, we show that there is no direct interaction between the RBD and basigin, casting doubt on its role as a co-receptor and plausibility as a therapeutic target.

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Ragotte, R. J., Pulido, D., Donnellan, F. R., Gorini, G., Davies, H., Brun, J., King, L. D., Skinner, K., Draper, S. J.. 2021-02-23. Human basigin (CD147) does not directly interact with SARS-CoV-2 spike glycoprotein. https://doi.org/10.1101/2021.02.22.432402

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