COVID-19 in VR: Spike Protein Mink Mutations

In this video we discuss the amino acid changes in the spike surface glycoprotein that appeared during the recent outbreak in Danish mink and their effect on the antigenicity of the SARS-CoV-2 virus.

Within the infected mink, the SARS-CoV-2 virus mutated giving rise to several amino acid changes in the spike protein. The first was a tyrosine to phenylalanine at amino acid 453 (Y453F). It is a conservative amino acid substitution in the receptor binding domain that directly contacts the host ACE2 receptor at amino acid 34. This ACE2 contact position differs between human and mink (histidine [34H] in humans and tyrosine [34Y] in mink, which suggests that Y453F is an adaptation mutation to mink ACE2. Importantly, 453F increases affinity for human ACE2, which may explain its successful introduction and establishment in humans.

Following the appearance of 453F, additional spike mutations were observed in minks and the humans epidemiologically linked to the infected mink farms. These include the deletion of H69 and V70 in the N-terminal domain of the S1 subunit; I692V – a conservative substitution at position 692 that is located seven amino acids downstream of the furin cleavage site; S1147L – a non-conservative substitution at position 1147 in the S2 subunit; and M1229I – a conservative substitution located within the transmembrane domain.

Research study discussed: Lassaunière et al. (2020). Working paper on SARS-CoV-2 spike mutations arising in Danish mink, their 2 spread to humans and neutralization (preprint). https://files.ssi.dk/Mink-cluster-5-s...

Acknowledgments: We’d like to thank the group of Prof. Giovanni Chillemi of the University of Tuscia, DIBAF department, who provided us with the system we have analyzed.
http://www.unitus.it/it/dipartimento/...

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