The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.
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.
Gillet
Laurent
L
Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom.
Colaco
Susanna
S
Stevenson
Philip G
PG
D000818:Animals; D006224:Cricetinae; D019281:Dimerization; D004705:Endocytosis; D011992:Endosomes / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008561:Membrane Fusion; D008562:Membrane Glycoproteins / Q000378:metabolism / Q000502:physiology*; D051379:Mice; D018832:Molecular Chaperones / Q000378:metabolism / Q000502:physiology*; D041681:NIH 3T3 Cells; D011487:Protein Conformation; D018144:Rhadinovirus / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000378:metabolism / Q000502:physiology*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*
D006023:Glycoproteins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C065527:glycoprotein H, Herpesvirus 4; C103802:glycoprotein L, Human herpesvirus 4