 Hello, I'm Tino, I'm Melanie, and I'm Christina, and we are from ETH at the University of Turing. And we would like to welcome you to our video abstract on our review, the Bar Tintus Suite, which is published in December issue of protein science. Our work focuses on viruses and specifically how viruses engage cell surface receptors and glycans and proteins, and the study is actually structurally, using crystallography mostly, but also functionally, using very functional assays. And my two talented co-workers Melanie and Christina will now guide you through a little animation that we made that shows you how a virus engages the cell surface. There's technology with glycans and also how antibodies can neutralize the virus and prevent it from binding to the cell surface. So in our study there's some membrane with different types of carbohydrates present on the extracellular side and additional actors are spike virus and antibodies. Carbohydrates, which are present on the cell surface, can serve as viral receptors. They can facilitate attachment and entry of the virus. In this review we focused on viruses with stalk-like attachment proteins. Their glycane receptor binding sites are typically located in exposed regions on viral surfaces. Viruses bind to multiple receptor copies at the same time to overcome the low binding affinity by high avidity. So how do antibodies interfere with virus glycane receptor binding? Antibodies typically bind to exposed regions on viral surfaces with high affinity. Therefore, they often overlap or bind sufficiently close to the receptor binding site to block glycane binding. They achieve neutralization partially because they occlude the glycane binding site and partly due to their shear size, which prevents the virus from reaching the receptor. Thank you for watching our video and we hope you enjoyed reading our review. Bye!