Recent mechanistic and structural insights on class III viral fusion glycoproteins

被引:46
作者
Baquero, Eduard [1 ]
Albertini, Aurelie A. V. [1 ]
Gaudin, Yves [1 ]
机构
[1] Univ Paris 11, CNRS, CEA, Inst Integrat Biol Cell I2BC, F-91198 Gif Sur Yvette, France
关键词
STOMATITIS-VIRUS GLYCOPROTEIN; CELL-CELL FUSION; CRYSTAL-STRUCTURE; MEMBRANE-FUSION; BACULOVIRUS GP64; INACTIVE CONFORMATION; LOW-PH; GB; ENTRY; RESIDUES;
D O I
10.1016/j.sbi.2015.07.011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Enveloped viruses enter the cell by fusing their envelope with a cellular membrane. Fusion is catalyzed by conformational changes of viral glycoproteins from pre-fusion to post-fusion states. Structural studies have defined three classes of viral fusion glycoproteins. Class Ill comprises the fusion glycoproteins from rhabdoviruses (G), herpesviruses (gB), and baculoviruses (GP64). Although sharing the same fold, those glycoproteins exhibit striking differences in their modes of activation and interaction with the target membrane. Furthermore, for gB and GP64, only the post-fusion structure is known and the extent of their conformational change is still an unresolved issue. Further structural studies are therefore required to get a detailed insight in the working of those fusion machines.
引用
收藏
页码:52 / 60
页数:9
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