Dynamic Envelope of a Fusion Class II Virus: PREFUSION STAGES OF SEMLIKI FOREST VIRUS REVEALED BY ELECTRON CRYOMICROSCOPY
Semliki Forest virus is among the prototypes for Class II virus fusion and targets the endosomal membrane. Fusion protein E1 and its envelope companion E2 are both anchored in the viral membrane and form an external shell with protruding spikes. In acid environments, mimicking the early endosomal mi...
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Veröffentlicht in: | JOURNAL OF BIOLOGICAL CHEMISTRY 2007-03, Vol.282 (9), p.6752-6762 |
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creator | Wu, Shang-Rung Haag, Lars Hammar, Lena Wu, Bomu Garoff, Henrik Xing, Li Murata, Kazuyoshi Cheng, R. Holland |
description | Semliki Forest virus is among the prototypes for Class II virus fusion and targets the endosomal membrane. Fusion protein E1 and its envelope companion E2 are both anchored in the viral membrane and form an external shell with protruding spikes. In acid environments, mimicking the early endosomal milieu, surface epitopes in the virus rearrange along with exposure of the fusion loop. To visualize this transformation into a fusogenic stage, we determined the structure of the virus at gradually lower pH values. The results show that while the fusion loop is available for external interaction and the shell and stalk domains of the spike begin to deteriorate, the E1 and E2 remain in close contact in the spike head. This unexpected observation points to E1 and E2 cooperation beyond the fusion loop exposure stage and implies a more prominent role for E2 in guiding membrane close encounter than has been earlier anticipated. |
doi_str_mv | 10.1074/jbc.M609125200 |
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Holland</creatorcontrib><title>Dynamic Envelope of a Fusion Class II Virus: PREFUSION STAGES OF SEMLIKI FOREST VIRUS REVEALED BY ELECTRON CRYOMICROSCOPY</title><title>JOURNAL OF BIOLOGICAL CHEMISTRY</title><addtitle>J Biol Chem</addtitle><description>Semliki Forest virus is among the prototypes for Class II virus fusion and targets the endosomal membrane. Fusion protein E1 and its envelope companion E2 are both anchored in the viral membrane and form an external shell with protruding spikes. In acid environments, mimicking the early endosomal milieu, surface epitopes in the virus rearrange along with exposure of the fusion loop. To visualize this transformation into a fusogenic stage, we determined the structure of the virus at gradually lower pH values. The results show that while the fusion loop is available for external interaction and the shell and stalk domains of the spike begin to deteriorate, the E1 and E2 remain in close contact in the spike head. This unexpected observation points to E1 and E2 cooperation beyond the fusion loop exposure stage and implies a more prominent role for E2 in guiding membrane close encounter than has been earlier anticipated.</description><subject>Cryoelectron Microscopy</subject><subject>Hydrogen-Ion Concentration</subject><subject>Medicin och hälsovetenskap</subject><subject>Membrane Fusion</subject><subject>Molecular Structure</subject><subject>Phase Transition</subject><subject>Protein Conformation</subject><subject>Semliki Forest virus</subject><subject>Semliki forest virus - chemistry</subject><subject>Semliki forest virus - pathogenicity</subject><subject>Viral Envelope Proteins - chemistry</subject><subject>Viral Envelope Proteins - physiology</subject><subject>Viral Fusion Proteins - chemistry</subject><subject>Viral Fusion Proteins - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>D8T</sourceid><recordid>eNqFkktP4zAQgC3ECsrjyhF84hbWjziOuZXgQERKUNJW9BS5iYMCaVNiwqr_fo1a4ITwZazR99meGQNwgtEFRtz9-zwvLkYeEpgwgtAOGGDkU4cy_LgLBggR7AjC_H1wYMwzsssVeA_sY44FIZwMwPp6vVSLuoBy-a6bdqVhW0EFw97U7RIGjTIGRhGc1l1vLuFDKsNJFiX3MBsPb2QGkxBmchRHdxEMk1RmYziN0kkGUzmVw1hew6sZlLEMxql1gnSWjKIgTbIgeZgdgT-Vaow-3sZDMAnlOLh14uQmCoaxU9kq3hyGC4ZLLURpC1TCwxRxhTzM-RxRSnyOfJf5RUl5iUlB3YJ4uqRK66oiXDNND4GzOdf806t-nq-6eqG6dd6qOt-mXuxO54wTyjzL-z_yq64tv6VP0fbeRZQLq55vVMu99tq85YvaFLpp1FK3vcm5nYf7cc1vIBaW8plvwdMt2M8Xuvx6zOcALXC2ASrV5uqpq00-yQiyXbK_QwjXpf8Bv4qgYg</recordid><startdate>20070302</startdate><enddate>20070302</enddate><creator>Wu, Shang-Rung</creator><creator>Haag, Lars</creator><creator>Hammar, Lena</creator><creator>Wu, Bomu</creator><creator>Garoff, Henrik</creator><creator>Xing, Li</creator><creator>Murata, Kazuyoshi</creator><creator>Cheng, R. 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Holland</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f351t-51c51de99d520a961307a06177b03328708458cd37d12c34c26ed3aeeff27e5e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Cryoelectron Microscopy</topic><topic>Hydrogen-Ion Concentration</topic><topic>Medicin och hälsovetenskap</topic><topic>Membrane Fusion</topic><topic>Molecular Structure</topic><topic>Phase Transition</topic><topic>Protein Conformation</topic><topic>Semliki Forest virus</topic><topic>Semliki forest virus - chemistry</topic><topic>Semliki forest virus - pathogenicity</topic><topic>Viral Envelope Proteins - chemistry</topic><topic>Viral Envelope Proteins - physiology</topic><topic>Viral Fusion Proteins - chemistry</topic><topic>Viral Fusion Proteins - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Shang-Rung</creatorcontrib><creatorcontrib>Haag, Lars</creatorcontrib><creatorcontrib>Hammar, Lena</creatorcontrib><creatorcontrib>Wu, Bomu</creatorcontrib><creatorcontrib>Garoff, Henrik</creatorcontrib><creatorcontrib>Xing, Li</creatorcontrib><creatorcontrib>Murata, Kazuyoshi</creatorcontrib><creatorcontrib>Cheng, R. 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To visualize this transformation into a fusogenic stage, we determined the structure of the virus at gradually lower pH values. The results show that while the fusion loop is available for external interaction and the shell and stalk domains of the spike begin to deteriorate, the E1 and E2 remain in close contact in the spike head. This unexpected observation points to E1 and E2 cooperation beyond the fusion loop exposure stage and implies a more prominent role for E2 in guiding membrane close encounter than has been earlier anticipated.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>17192272</pmid><doi>10.1074/jbc.M609125200</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Cryoelectron Microscopy Hydrogen-Ion Concentration Medicin och hälsovetenskap Membrane Fusion Molecular Structure Phase Transition Protein Conformation Semliki Forest virus Semliki forest virus - chemistry Semliki forest virus - pathogenicity Viral Envelope Proteins - chemistry Viral Envelope Proteins - physiology Viral Fusion Proteins - chemistry Viral Fusion Proteins - physiology |
title | Dynamic Envelope of a Fusion Class II Virus: PREFUSION STAGES OF SEMLIKI FOREST VIRUS REVEALED BY ELECTRON CRYOMICROSCOPY |
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