文章基本信息

标题：Crystal structure of glycoprotein C from Rift Valley fever virus
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作者：Moshe Dessau ; Yorgo Modis
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2013
卷号：110
期号：5
页码：1696-1701
DOI：10.1073/pnas.1217780110
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Rift Valley fever virus (RVFV), like many other Bunyaviridae family members, is an emerging human and animal pathogen. Bunyaviruses have an outer lipid envelope bearing two glycoproteins, GN and GC, required for cell entry. Bunyaviruses deliver their genome into the host-cell cytoplasm by fusing their envelope with an endosomal membrane. The molecular mechanism of this key entry step is unknown. The crystal structure of RVFV GC reveals a class II fusion protein architecture found previously in flaviviruses and alphaviruses. The structure identifies GC as the effector of membrane fusion and provides a direct view of the membrane anchor that initiates fusion. A structure of nonglycosylated GC reveals an extended conformation that may represent a fusion intermediate. Unanticipated similarities between GC and flavivirus envelope proteins reveal an evolutionary link between the two virus families and provide insights into the organization of GC in the outer shell of RVFV.
关键词：icosahedral lattice assembly ; parallel evolution ; pH sensing ; prehairpin