structure of reovirus σ1 in complex with its receptor junctional adhesion molecule-a呼肠孤病毒的结构与其受体交界粘附分子u2014σ1复杂.pdfVIP

Structure of Reovirus s1 in Complex with Its Receptor Junctional Adhesion Molecule-A 1 2,3 4 2,3,5 1,5 Eva Kirchner , Kristen M. Guglielmi , Holger M. Strauss , Terence S. Dermody *, Thilo Stehle * 1 Interfaculty Institute for Biochemistry, University of Tuebingen, Tuebingen, Germany, 2 Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee, United States of America, 3 Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University School of Medicine, Nashville, ¨ Tennessee, United States of America, 4 Nanolytics Gesellschaft fur Kolloidanalytik mbH, Potsdam, Germany, 5 Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee, United States of America Abstract Viral attachment to specific host receptors is the first step in viral infection and serves an essential function in the selection of target cells. Mammalian reoviruses are highly useful experimental models for studies of viral pathogenesis and show promise as vectors for oncolytics and vaccines. Reoviruses engage cells by binding to carbohydrates and the immunoglobulin superfamily member, junctional adhesion molecule-A (JAM-A). JAM-A exists at the cell surface as a homodimer formed by extensive contacts between its N-terminal immunoglobulin-like domains. We report the crystal structure of reovirus attachment protein s1 in complex with a