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Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly
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نویسنده
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xu k. ,chan y.-p. ,bradel-tretheway b. ,akyol-ataman z. ,zhu y. ,dutta s. ,yan l. ,feng y. ,wang l.-f. ,skiniotis g. ,lee b. ,zhou z.h. ,broder c.c. ,aguilar h.c. ,nikolov d.b.
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منبع
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plos pathogens - 2015 - دوره : 11 - شماره : 12
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چکیده
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Nipah virus (niv) is a paramyxovirus that infects host cells through the coordinated efforts of two envelope glycoproteins. the g glycoprotein attaches to cell receptors,triggering the fusion (f) glycoprotein to execute membrane fusion. here we report the first crystal structure of the pre-fusion form of the niv-f glycoprotein ectodomain. interestingly this structure also revealed a hexamer-of-trimers encircling a central axis. electron tomography of nipah virus-like particles supported the hexameric pre-fusion model,and biochemical analyses supported the hexamer-of-trimers f assembly in solution. importantly,structure-assisted site-directed mutagenesis of the interfaces between f trimers highlighted the functional relevance of the hexameric assembly. shown here,in both cell-cell fusion and virus-cell fusion systems,our results suggested that this hexamer-of-trimers assembly was important during fusion pore formation. we propose that this assembly would stabilize the pre-fusion f conformation prior to cell attachment and facilitate the coordinated transition to a post-fusion conformation of all six f trimers upon triggering of a single trimer. together,our data reveal a novel and functional pre-fusion architecture of a paramyxoviral fusion glycoprotein. © 2015,public library of science,all rights reserved.
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آدرس
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structural biology program,memorial sloan-kettering cancer center,new york,ny, United States, department of microbiology and immunology,uniformed services university,bethesda,md, United States, paul g. allen school for global animal health,washington state university,pullman,wa, United States, department of microbiology,immunology and molecular genetics,university of california,los angeles,david geffen school of medicine,los angeles,ca, United States, life sciences institute and innovation center for cell biology,zhejiang university,hangzhou,zhejiang, China, life sciences institute,university of michigan,ann arbor,mi, United States, department of microbiology and immunology,uniformed services university,bethesda,md, United States, department of microbiology and immunology,uniformed services university,bethesda,md, United States, csiro animal,food and health sciencesn animal health laboratory,geelong,vic,australia,program in emerging infectious diseases,duke-nus graduate medical school, Singapore, life sciences institute,university of michigan,ann arbor,mi,united states,department of biological chemistry,university of michigan medical school,ann arbor,mi, United States, department of microbiology,icahn school of medicine at mount sinai,new york,ny, United States, department of microbiology,immunology and molecular genetics,university of california,los angeles,david geffen school of medicine,los angeles,ca,united states,california nanosystems institute,university of california,los angeles,david geffen school of medicine,los angeles,ca, United States, department of microbiology and immunology,uniformed services university,bethesda,md, United States, paul g. allen school for global animal health,washington state university,pullman,wa, United States, structural biology program,memorial sloan-kettering cancer center,new york,ny, United States
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Authors
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