scholarly journals Analysis of contributions of herpes simplex virus type 1 UL43 protein to induction of cell-cell fusion

2016 ◽  
Vol 15 (6) ◽  
pp. 1137
Author(s):  
Zhaobing Liu ◽  
Junli Huang ◽  
Qing Ding ◽  
Yan Yang ◽  
Hanxiao Sun
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Simplex Virus ◽  
Cell Cell

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.

scholarly journals Mutations in the Amino Terminus of Herpes Simplex Virus Type 1 gL Can Reduce Cell-Cell Fusion without Affecting gH/gL Trafficking

2013 ◽  
Vol 88 (1) ◽  
pp. 739-744 ◽  
Author(s):  
W. Zhou ◽  
F. Chen ◽  
Y. Klyachkin ◽  
Y. Y. Sham ◽  
R. J. Geraghty
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Fusion ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Amino Terminus ◽  
Simplex Virus ◽  
Cell Cell

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

scholarly journals Contribution of Endocytic Motifs in the Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein B to Virus Replication and Cell-Cell Fusion

2007 ◽  
Vol 81 (24) ◽  
pp. 13889-13903 ◽  
Author(s):  
Igor Beitia Ortiz de Zarate ◽  
Lilia Cantero-Aguilar ◽  
Magalie Longo ◽  
Clarisse Berlioz-Torrent ◽  
Flore Rozenberg
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Surface ◽  
Cell Fusion ◽  
Virus Replication ◽  
Herpes Simplex Virus Type ◽  
Wild Type ◽  
Simplex Virus ◽  
Cell Cell

ABSTRACT The use of endocytic pathways by viral glycoproteins is thought to play various functions during viral infection. We previously showed in transfection assays that herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) is transported from the cell surface back to the trans-Golgi network (TGN) and that two motifs of gB cytoplasmic tail, YTQV and LL, function distinctly in this process. To investigate the role of each of these gB trafficking signals in HSV-1 infection, we constructed recombinant viruses in which each motif was rendered nonfunctional by alanine mutagenesis. In infected cells, wild-type gB was internalized from the cell surface and concentrated in the TGN. Disruption of YTQV abolished internalization of gB during infection, whereas disruption of LL induced accumulation of internalized gB in early recycling endosomes and impaired its return to the TGN. The growth of both recombinants was moderately diminished. Moreover, the fusion phenotype of cells infected with the gB recombinants differed from that of cells infected with the wild-type virus. Cells infected with the YTQV-mutated virus displayed reduced cell-cell fusion, whereas giant syncytia were observed in cells infected with the LL-mutated virus. Furthermore, blocking gB internalization or impairing gB recycling to the cell surface, using drugs or a transdominant negative form of Rab11, significantly reduced cell-cell fusion. These results favor a role for endocytosis in virus replication and suggest that gB intracellular trafficking is involved in the regulation of cell-cell fusion.

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
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