Professor Jinwoo Lee of the University of Maryland, College Park

" Exploring the Vital Role of Anionic Lipids in Initiating Membrane Fusion - Corona and Arena Viruses"

Membrane fusion is a crucial step in the entry of coronaviruses and the Lassa virus, driven by the structure and function of their fusion domains. These domains contain a uniquely arranged fusion peptide and fusion loop that work together, playing essential roles in interacting with the host cell membrane. In coronaviruses, the spike (S) protein undergoes structural changes after receptor binding, which exposes the fusion peptide within the S2 subunit. This peptide interacts with the host membrane, promoting membrane destabilization and viral entry. Likewise, the Lassa virus glycoprotein complex (GPC) features a fusion loop in GP2 that becomes active in acidic conditions, embedding into the host membrane to initiate fusion. The specific structures and properties of these viral proteins, along with their ability to bind and disrupt host membranes, are critical to viral infectivity. Understanding these mechanisms offers insight into virus-host interactions and assists in developing antiviral strategies targeting membrane fusion.