Functions of purified gB, gE:gI, and gH:gL, and their sialyl residues in varicella-zoster virus infection.
Varicella-zoster virus glycoproteins were purified by using monoclonal antibodies and analyzed for their effects on cell-free virus infection. Preinfection treatment of cells with gH:gL reduced the infection efficiency and increased the number of unadsorbed virus. Postinfection treatment of cells with gB increased the infection efficiency, but that with gE:gI reduced it. Treatment of gE:gI and gH:gL with neuraminidase (NA) abolished their inhibitory activity and the plaque formation was enhanced by NA treatment of glycoproteins and cells. Glycoproteins exhibited their diverse activities despite their common role in viral penetration, and sialyl residues were responsible for their function in cell-free virus infection.
Department of Virology, Toyama Medical and Pharmaceutical University, Japan.
K
K
Shiraki
H
H
Sato
J
J
Yamamura
Z H
ZH
Li
T
T
Yokoyama
T
T
Hasegawa
T
T
Okuno
M
M
Kurokawa
S
S
Kageyama
D000818:Animals; D002460:Cell Line; D006168:Guinea Pigs; D014645:Herpesvirus 3, Human / Q000502:physiology*; D006801:Humans; D008562:Membrane Glycoproteins / Q000302:isolation & purification / Q000502:physiology*; D051379:Mice; D019158:N-Acetylneuraminic Acid / Q000502:physiology*; D009439:Neuraminidase / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000302:isolation & purification / Q000502:physiology*; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000302:isolation & purification / Q000502:physiology*
D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C090198:glycoprotein B, varicella-zoster virus; C056913:glycoprotein E, varicella-zoster virus; C094648:glycoprotein gL, varicella-zoster virus; C040496:gp 118 protein, Herpesvirus 3, Human; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid