the hexamer structure of the rift valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes六聚体结构的裂谷热病毒核蛋白建议组装机制为核糖核蛋白复合物.pdfVIP

The Hexamer Structure of the Rift Valley Fever Virus Nucleoprotein Suggests a Mechanism for its Assembly into Ribonucleoprotein Complexes 1 2,3 2 4 4 1 Franc¸ois Ferron , Zongli Li , Eric I. Danek , Dahai Luo , Yeehwa Wong , Bruno Coutard , Violaine 1 ´ 5 1 2,3 1,4 Lantez , Remi Charrel , Bruno Canard , Thomas Walz , Julien Lescar * ´ 1 Architecture et Fonction des Macromolecules Biologiques, Marseille, France, 2 Harvard Medical School, Department of Cell Biology, Boston, Massachusetts, United States of America, 3 Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts, United States of America, 4 Nanyang Technological University, School of ´ ´ ´ Biological Sciences, Singapore, 5 Unite des Virus Emergents, Universite Aix-Marseille II et Institut de Recherche pour le Developpement, Marseille, France Abstract Rift Valley fever virus (RVFV), a Phlebovirus with a genome consisting of three single-stranded RNA segments, is spread by infected mosquitoes and causes large viral outbreaks in Africa. RVFV encodes a nucleoprotein (N) that encapsidates the viral RNA. The N protein is the major component of the ribonucleoprotein complex and is also required for genomic RNA ˚ replication and transcription by the viral polymerase. Here we present the 1.