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
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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
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.
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