Researchers at the Icahn School of Medicine at Mount Sinai and collaborators have created the most comprehensive map to date showing how antibodies attach to the SARS-CoV-2 virus, which causes COVID-19, and how viral mutations weaken that attachment. The findings, published in the November 21 online issue of Cell Systems, a Cell Press journal, explain why variants like Omicron can evade immune defenses and suggest new strategies for building longer-lasting antibody therapies and vaccines. The team analyzed more than a thousand three-dimensional structures of antibodies bound to the virus’s spike protein, the main target for immune recognition, and compiled them into a structural atlas of COVID-19 antibodies. By studying these structures together for the first time, the researchers revealed a detailed picture of how the immune system targets the virus and how the virus evolves to evade it.

A fundamental discovery about phosphorylation, a key mechanism that enables nervous system connections to strengthen, may alter the textbook-level understanding of how synapses work. Phosphorylation is a biochemical process considered fundamental for functions within cells, such as metabolism, structural processes and subcellular signaling. It also occurs outside of cells, and scientist found in this study that kinases within the synaptic cleft play an important role in synaptic plasticity. The findings, published Nov. 20 in the journal Science, have direct implications for better understanding the underlying biochemical mechanisms involved in learning, memory and pain, creating broad implications for neuroscience.