Intermediate conformations during viral fusion glycoprotein structural transition

被引:42
作者
Baquero, Eduard [1 ]
Albertini, Aurelie A. [1 ]
Vachette, Patrice [2 ]
Lepault, Jean [1 ]
Bressanelli, Stephane [1 ]
Gaudin, Yves [1 ]
机构
[1] CNRS, Lab Virol Mol & Struct, Ctr Rech Gif, UPR 3296, F-91198 Gif Sur Yvette, France
[2] Univ Paris 11, CNRS, UMR 8619, Inst Biochim & Biophys Mol & Cellulaire, F-91405 Orsay, France
关键词
STOMATITIS-VIRUS GLYCOPROTEIN; SEMLIKI-FOREST-VIRUS; MEMBRANE-FUSION; INFLUENZA HEMAGGLUTININ; ENVELOPE GLYCOPROTEIN; CRYSTAL-STRUCTURE; DOMAIN-III; PROTEIN; PH; CAPTURE;
D O I
10.1016/j.coviro.2013.03.006
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Entry of enveloped viruses into cells requires the fusion of viral and cellular membranes, driven by conformational changes in viral glycoproteins. Three different classes of viral fusion proteins have been hitherto identified based on common structural elements. Crystal structures have provided static pictures of pre-fusion and post-fusion conformations of these proteins and have revealed the dramatic reorganization of the molecules, but the transition pathway remains elusive. In this review, we will focus on recent data aiming to characterize intermediate structures during the conformational change. All these data support the existence of a pre-hairpin intermediate, but its oligomeric status is still a matter of debate.
引用
收藏
页码:143 / 150
页数:8
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