Keywords :
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
Abstract :
[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.
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