The Cell Fusion Protein Gene (UL53) of Herpes Simplex Virus Type 1 — A Pathogenicity Gene

1994 ◽  
pp. 253-260
Author(s):  
Michal Moyal ◽  
Yechiel Becker
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Fusion Protein ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Protein Gene ◽  
Pathogenicity Gene ◽  
Simplex Virus

Nucleotide sequence of a herpes simplex virus type 1 gene that causes cell fusion

Virology ◽  
1985 ◽  
Vol 145 (1) ◽  
pp. 36-48 ◽  
Author(s):  
Chitrita Debroy ◽  
Nels Pederson ◽  
Stanley Person
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Nucleotide Sequence ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
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

Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type 1

Virology ◽  
1983 ◽  
Vol 129 (1) ◽  
pp. 218-224 ◽  
Author(s):  
A.Gwendolyn Noble ◽  
Gloria T-Y. Lee ◽  
Robert Sprague ◽  
Mary Lynn Parish ◽  
Patricia G. Spear
Keyword(s):  
Monoclonal Antibodies ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Simplex Virus ◽  
Inhibit Cell Fusion

scholarly journals Plasma membrane requirements for cell fusion induced by herpes simplex virus type 1 glycoproteins gB, gD, gH and gL

2001 ◽  
Vol 82 (6) ◽  
pp. 1419-1422 ◽  
Author(s):  
Helena Browne ◽  
Birgitte Bruun ◽  
Tony Minson
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Syncytium Formation ◽  
Fusion Event ◽  
In Trans ◽  
Simplex Virus

Herpes simplex virus type 1 (HSV-1) glycoproteins gB, gD and gHL are capable of inducing cell fusion when expressed from plasmid vectors in the absence of any other virus components. Fusion requires the expression of all four glycoproteins on the same membrane, since they are unable to cooperate in trans to induce syncytium formation. In addition, the fusion event is dependent on the expression of a gD receptor on target cell membranes and does not require the presence of cell-surface glycosaminoglycans.

scholarly journals Live Visualization of Herpes Simplex Virus Type 1 Compartment Dynamics

2008 ◽  
Vol 82 (10) ◽  
pp. 4974-4990 ◽  
Author(s):  
Anna Paula de Oliveira ◽  
Daniel L. Glauser ◽  
Andrea S. Laimbacher ◽  
Regina Strasser ◽  
Elisabeth M. Schraner ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Fusion Protein ◽  
Viral Replication ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Fluorescent Protein ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT We have constructed a recombinant herpes simplex virus type 1 (HSV-1) that simultaneously encodes selected structural proteins from all three virion compartments—capsid, tegument, and envelope—fused with autofluorescent proteins. This triple-fluorescent recombinant, rHSV-RYC, was replication competent, albeit with delayed kinetics, incorporated the fusion proteins into all three virion compartments, and was comparable to wild-type HSV-1 at the ultrastructural level. The VP26 capsid fusion protein (monomeric red fluorescent protein [mRFP]-VP26) was first observed throughout the nucleus and later accumulated in viral replication compartments. In the course of infection, mRFP-VP26 formed small foci in the periphery of the replication compartments that expanded and coalesced over time into much larger foci. The envelope glycoprotein H (gH) fusion protein (enhanced yellow fluorescent protein [EYFP]-gH) was first observed accumulating in a vesicular pattern in the cytoplasm and was then incorporated primarily into the nuclear membrane. The VP16 tegument fusion protein (VP16-enhanced cyan fluorescent protein [ECFP]) was first observed in a diffuse nuclear pattern and then accumulated in viral replication compartments. In addition, it also formed small foci in the periphery of the replication compartments which, however, did not colocalize with the small mRFP-VP26 foci. Later, VP16-ECFP was redistributed out of the nucleus into the cytoplasm, where it accumulated in vesicular foci and in perinuclear clusters reminiscent of the Golgi apparatus. Late in infection, mRFP-VP26, EYFP-gH, and VP16-ECFP were found colocalizing in dots at the plasma membrane, possibly representing mature progeny virus. In summary, this study provides new insights into the dynamics of compartmentalization and interaction among capsid, tegument, and envelope proteins. Similar strategies can also be applied to assess other dynamic events in the virus life cycle, such as entry and trafficking.

scholarly journals Structure-Function Analysis of Herpes Simplex Virus Type 1 gD and gH-gL: Clues from gDgH Chimeras

2003 ◽  
Vol 77 (12) ◽  
pp. 6731-6742 ◽  
Author(s):  
Tina M. Cairns ◽  
Richard S. B. Milne ◽  
Manuel Ponce-de-Leon ◽  
Deanna K. Tobin ◽  
Gary H. Cohen ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Surface ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Simplex Virus ◽  
Hsv 1 ◽  
Cell Cell

ABSTRACT In alphaherpesviruses, glycoprotein B (gB), gD, gH, and gL are essential for virus entry. A replication-competent gL-null pseudorabies virus (PrV) (B. G. Klupp and T. C. Mettenleiter, J. Virol. 73:3014-3022, 1999) was shown to express a gDgH hybrid protein that could replace gD, gH, and gL in cell-cell fusion and null virus complementation assays. To study this phenomenon in herpes simplex virus type 1 (HSV-1), we constructed four gDgH chimeras, joining the first 308 gD amino acids to various gH N-terminal truncations. The chimeras were named for the first amino acid of gH at which each was truncated: 22, 259, 388, and 432. All chimeras were immunoprecipitated with both gD and gH antibodies to conformational epitopes. Normally, transport of gH to the cell surface requires gH-gL complex formation. Chimera 22 contains full-length gH fused to gD308. Unlike PrV gDgH, chimera 22 required gL for transport to the surface of transfected Vero cells. Interestingly, although chimera 259 failed to reach the cell surface, chimeras 388 and 432 exhibited gL-independent transport. To examine gD and gH domain function, each chimera was tested in cell-cell fusion and null virus complementation assays. Unlike PrV gDgH, none of the HSV-1 chimeras substituted for gL for fusion. Only chimera 22 was able to replace gH for fusion and could also replace either gH or gD in the complementation assay. Surprisingly, this chimera performed very poorly as a substitute for gD in the fusion assay despite its ability to complement gD-null virus and bind HSV entry receptors (HveA and nectin-1). Chimeras 388 and 432, which contain the same portion of gD as that in chimera 22, substituted for gD for fusion at 25 to 50% of wild-type levels. However, these chimeras functioned poorly in gD-null virus complementation assays. The results highlight the fact that these two functional assays are measuring two related but distinct processes.

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