Conference Dates

June 12 – 17, 2022


Since its emergence in 2019 the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) continues to a profoundly impact and threaten human health. For the development of novel prophylactic and therapeutic measures a detailed understanding of the virus-host interaction and features that modulate the interaction is of utmost importance. Attachment of the SARS-CoV-2 virus to human host cells predominantly relies on the specific interaction of the viral spike (S) surface glycoprotein with the receptor angiotensin-converting enzyme 2 (ACE-2). Glycans within or surrounding the binding interface have been demonstrated to play an important role in the ACE2:S interaction. The quality of this interaction is multifaceted and affected by several parameters, such as the speed, the number, the strength and duration of bond formation. As mutations within the coding sequences of the interaction partners may affect their binding capacity, they should be thoroughly studied. In this respect, viral evolution and the effect of mutations within the S-protein have received much attention, while human ACE2 polymorphisms naturally occurring throughout the population have so far been largely ignored. Of note, natural ACE2 polymorphisms and viral spike mutants that result in the loss of glycans within the binding interface should receive our particular attention.

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