Reference : The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/76170
The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.
English
Gillet, Laurent mailto [Université de Liège - ULg > > Immunologie et vaccinologie >]
Colaco, Susanna [> > > >]
Stevenson, Philip G [> > > >]
2008
PLoS ONE
Public Library of Science
3
7
e2811
Yes (verified by ORBi)
International
1932-6203
San Franscisco
CA
[en] Animals ; Cricetinae ; Dimerization ; Endocytosis ; Endosomes/metabolism ; Glycoproteins/chemistry ; Hydrogen-Ion Concentration ; Membrane Fusion ; Membrane Glycoproteins/metabolism/physiology ; Mice ; Molecular Chaperones/metabolism/physiology ; NIH 3T3 Cells ; Protein Conformation ; Rhadinovirus/metabolism ; Viral Envelope Proteins/metabolism/physiology ; Viral Proteins/chemistry/metabolism/physiology
[en] The glycoprotein H (gH)/gL heterodimer is crucial for herpesvirus membrane fusion. Yet how it functions is not well understood. The Murid Herpesvirus-4 gH, like that of other herpesviruses, adopts its normal virion conformation by associating with gL. However, gH switched back to a gL-independent conformation after virion endocytosis. This switch coincided with a conformation switch in gB and with capsid release. Virions lacking gL constitutively expressed the down-stream form of gH, prematurely switched gB to its down-stream form, and showed premature capsid release with poor infectivity. These data argue that gL plays a key role in regulating a gH and gB functional switch from cell binding to membrane fusion.
http://hdl.handle.net/2268/76170
10.1371/journal.pone.0002811

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