Sugar-binding protein that blocks Sars-CoV-2 infection
An antibody recognizing cancer-specific glycolipids
Cutting glycans off flu hemagglutinin makes it a better vaccine (model)
Interleukin 17 receptor B bound by monoclonal antibody
Monofunctional glycotransferase from S.aureus
Penicillin-Binding Protein 1b from E.coli
NEW WAYS TO FIGHT INFLUENZA VIRUS
Seasonal flu is something everyone can catch.
Yet this common infectious disease is killing half a million people each year around the world. Failure to efficiently kill the virus after infection and failure to develop successful "flu" vaccines are caused by constant variations of its surface proteins. Non-conventional strategies are designed by us: a) truncating the glycan chains in vaccine development to expose more conserved regions; b) using flu-specific glycan-binding agent that arrest the virus before its amplification.
STRUCTURAL BASIS OF CANCER IMMUNOTHERAPY
Cancers are generally not infectious diseases. But do you know that you can defend cancer using the same immune system defending pathogens? What if one day our body can produce anticancer antibodies that kill cancer cells before they'll ever have a chance to develop? What are cancer-specific targets we look for? How can we improve antibody's efficacy? Will cancer vaccine be actually realized? These are major questions to be answered. We believe structural biology will play an indispensable role towards these answers.
You may survive from a chemotherapy after having cancer, but you won't have a chance in infection after bacteria become resistant to all antibiotics. The seemingly simple process of bacterial growth is much more complicated than expected. Antibiotic development is therefore extremely important and involves several stages: inhibitor screening, protein-inhibitor structures and structure-based drug design/improvement.