scholarly journals Herpes simplex virus type 1 glycoprotein L mutants that fail to promote trafficking of glycoprotein H and fail to function in fusion can induce binding of glycoprotein L-dependent anti-glycoprotein H antibodies

2006 ◽  
Vol 87 (4) ◽  
pp. 759-767 ◽  
Author(s):  
Yuri M. Klyachkin ◽  
Krista D. Stoops ◽  
Robert J. Geraghty
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Surface ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Glycoprotein H ◽  
Simplex Virus

The herpes simplex virus type 1 (HSV-1) glycoproteins H (gH) and L (gL) form a heterodimer and efficient expression of gH at the virion or cell surface is dependent upon gL. Five carboxy-terminal deletion mutants of gL were created and their ability to interact with and mediate cell-surface expression of gH, to promote binding of gL-dependent anti-gH antibodies and to contribute to cell fusion was analysed. All of the gL mutants bound gH, but only two mutants, containing the amino-terminal 161 or 168 aa of gL, mediated cell-surface expression of gH, and only gL161 and gL168 functioned in cell fusion. The binding of gL to gH, therefore, was not sufficient to ensure gH cell-surface expression and it was not possible to separate the gH-trafficking role of gL from gL function in fusion. Co-expression of gH with any gL mutant conferred binding of the anti-gH mAbs 53S and LP11. If the acquisition of 53S and LP11 binding to gH reflects a gL-induced conformational change, such a change is not sufficient to mediate trafficking of the gH–gL heterodimer.

scholarly journals Herpes Simplex Virus Type 1 Induces CD83 Degradation in Mature Dendritic Cells with Immediate-Early Kinetics via the Cellular Proteasome

2007 ◽  
Vol 81 (12) ◽  
pp. 6326-6338 ◽  
Author(s):  
Mirko Kummer ◽  
Nadine M. Turza ◽  
Petra Muhl-Zurbes ◽  
Matthias Lechmann ◽  
Chris Boutell ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Surface ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Surface Expression ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Mature dendritic cells (DCs) are the most potent antigen-presenting cells within the human immune system. However, Herpes simplex virus type 1 (HSV-1) is able to interfere with DC biology and to establish latency in infected individuals. In this study, we provide new insights into the mechanism by which HSV-1 disarms DCs by the manipulation of CD83, a functionally important molecule for DC activation. Fluorescence-activated cell sorter (FACS) analyses revealed a rapid downmodulation of CD83 surface expression within 6 to 8 h after HSV-1 infection, in a manner strictly dependent on viral gene expression. Soluble CD83 enzyme-linked immunosorbent assays, together with Western blot analysis, demonstrated that CD83 rapidly disappears from the cell surface after contact with HSV-1 by a mechanism that involves protein degradation rather than shedding of CD83 from the cell surface into the medium. Infection experiments with an ICP0 deletion mutant demonstrated an important role for this viral immediate-early protein during CD83 degradation, since this particular mutant strain leads to strongly reduced CD83 degradation. This hypothesis was further strengthened by cotransfection of plasmids expressing CD83 and ICP0 into 293T cells, which led to significantly reduced accumulation of CD83. In strong contrast, transfection of plasmids expressing CD83 and a mutant ICP0 defective in its RING finger-mediated E3 ubiquitin ligase function did not reduce CD83 expression. Inhibition of the proteasome, the cellular protein degradation machinery, almost completely restored CD83 surface expression during HSV-1 infection, indicating that proteasome-mediated degradation and HSV-1 ICP0 play crucial roles in this novel viral immune escape mechanism.

scholarly journals Analysis of a Membrane Interacting Region of Herpes Simplex Virus Type 1 Glycoprotein H

2008 ◽  
Vol 283 (44) ◽  
pp. 29993-30009 ◽  
Author(s):  
Stefania Galdiero ◽  
Annarita Falanga ◽  
Mariateresa Vitiello ◽  
Luca Raiola ◽  
Roberto Fattorusso ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein H ◽  
Simplex Virus

Replication-Competent Herpes simplex Virus Type 1 Mutant Expressing an Autofluorescent Glycoprotein H Fusion Protein

Intervirology ◽  
2001 ◽  
Vol 44 (4) ◽  
pp. 232-242 ◽  
Author(s):  
E.U. Lorentzen ◽  
B.R. Eing ◽  
W. Hafezi ◽  
R. Manservigi ◽  
J.E. Kühn
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Fusion Protein ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein H ◽  
Simplex Virus

scholarly journals Fusogenic Domains in Herpes Simplex Virus Type 1 Glycoprotein H

2005 ◽  
Vol 280 (31) ◽  
pp. 28632-28643 ◽  
Author(s):  
Stefania Galdiero ◽  
Annarita Falanga ◽  
Mariateresa Vitiello ◽  
Helena Browne ◽  
Carlo Pedone ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein H ◽  
Simplex Virus

Identification of herpes simplex virus type 1 glycoproteins interacting with the cell surface.

1990 ◽  
Vol 64 (6) ◽  
pp. 2491-2497 ◽  
Author(s):  
J E Kühn ◽  
M D Kramer ◽  
W Willenbacher ◽  
U Wieland ◽  
E U Lorentzen ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Surface ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Simplex Virus

Effect of tunicamycin and monensin on the transport to the cell surface and secretion of a viral membrane glycoprotein containing both N- and O-linked sugars

1994 ◽  
Vol 72 (1-2) ◽  
pp. 20-25 ◽  
Author(s):  
Nandini Ghosh-Choudhury ◽  
Martin Butcher ◽  
Ed Reid ◽  
Hara P. Ghosh
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Surface ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Mammalian Cells ◽  
Intracellular Transport ◽  
Simplex Virus ◽  
Cloned Gene

Most membrane glycoproteins contain either N-linked or O-linked oligosaccharides, which play important roles in correct folding, stability, and intracellular transport. Some glycoproteins, however, contain both the N- and O-linked sugars. To study the roles of the two types of glycosylation in intracellular transport we have used as a model the glycoprotein gC-1 of herpes simplex virus type 1 (HSV-1), which contains both N- and O-linked oligosaccharides. Cloned gene of gC-1 was expressed constitutively in mammalian cells to produce the gC-1 glycoprotein containing both types of glycosylation. Only a fraction of the gC-1 glycoprotein was secreted into the medium. Addition of tunicamycin blocked N-glycosylation and the gC-1 protein of reduced size containing only O-linked sugars was formed. This O-glycosylated gC-1 protein was transported to the cell surface and secreted into the medium, indicating that glycoprotein transport to and across the cell surface occurs in the absence of N-glycans. The data suggest either that O-glycans may contribute to this process or that transport can occur in the absence of both N- and O-glycans.Key words: intracellular transport, O-glycosylation, glycoprotein gC-1, herpes simplex virus type 1.

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