scholarly journals Sodium Chloride Enhances Recombinant Adeno-Associated Virus Production in a Serum-Free Suspension Manufacturing Platform Using the Herpes Simplex Virus System

2017 ◽  
Vol 28 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Laura Adamson-Small ◽  
Mark Potter ◽  
Barry J. Byrne ◽  
Nathalie Clément
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Sodium Chloride ◽  
Virus Production ◽  
Adeno Associated Virus ◽  
Serum Free ◽  
Manufacturing Platform ◽  
Simplex Virus ◽  
Virus System ◽  
Serum Free Suspension

Optimization of recombinant adeno-associated virus production using an herpes simplex virus amplicon system

2001 ◽  
Vol 96 (2) ◽  
pp. 97-105 ◽  
Author(s):  
Elisabeth Feudner ◽  
Mahesh de Alwis ◽  
Adrian J. Thrasher ◽  
Robin R. Ali ◽  
Sascha Fauser
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Production ◽  
Adeno Associated Virus ◽  
Simplex Virus

scholarly journals Genetic Analysis of the Herpes Simplex Virus Type 1 UL20 Protein Domains Involved in Cytoplasmic Virion Envelopment and Virus-Induced Cell Fusion

2004 ◽  
Vol 78 (14) ◽  
pp. 7329-7343 ◽  
Author(s):  
Jeffrey M. Melancon ◽  
Timothy P. Foster ◽  
Konstantin G. Kousoulas
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Fusion ◽  
Infectious Virus ◽  
Virus Production ◽  
Virion Morphogenesis ◽  
Production Group ◽  
Simplex Virus ◽  
Mutant Genes

ABSTRACT The herpes simplex virus type 1 UL20 protein (UL20p) is an important determinant for cytoplasmic virion morphogenesis and virus-induced cell fusion. To delineate the functional domains of the UL20 protein, we generated a panel of single and multiple (cluster) alanine substitutions as well as UL20p carboxyl-terminal truncations. The UL20 mutant genes could be broadly categorized into four main groups: Group I UL20 mutant genes complemented for both virus production and virus-induced cell fusion; Group II UL20 mutant genes did not complement for either virus-induced cell fusion or infectious virus production; Group III UL20 mutant genes complemented for virus-induced cell fusion to variable extents but exhibited substantially decreased ability to complement UL20-null infectious virus production; Group IV mutant genes complemented for infectious virus production but had variable effects on virus-induced cell fusion; this group included two mutants that efficiently complemented for gBsyn3, but not for gKsyn1, virus-induced cell fusion. In addition, certain recombinant viruses with mutations in either the amino or carboxyl termini of UL20p produced partially syncytial plaques on Vero cells in the absence of any other virally encoded syncytial mutations. These studies indicated that the amino and carboxyl termini of UL20p contained domains that functioned both in infectious virus production and virus-induced cell fusion. Moreover, the data suggested that the UL20p's role in virus-induced cell fusion can be functionally separated from its role in cytoplasmic virion morphogenesis and that certain UL20p domains that function in gB-syn3 virus-induced cell fusion are distinct from those functioning in gKsyn1 virus-induced cell fusion.

Herpes Simplex Virus Clearance during Purification of a Recombinant Adeno-associated Virus Serotype 1 Vector

2014 ◽  
pp. 150127063140004
Author(s):  
Guo-jie Ye ◽  
Marina M Scotti ◽  
Darby L Thomas ◽  
Lijun Wang ◽  
David R. Knop ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Adeno Associated Virus ◽  
Virus Clearance ◽  
Virus Serotype ◽  
Serotype 1 ◽  
Simplex Virus

scholarly journals 470. Efficient Clearance of Herpes Simplex Virus Using a GMP-Compliant Method for Production of Recombinant Adeno-Associated Virus Vectors

2015 ◽  
Vol 23 ◽  
pp. S186-S187
Author(s):  
Guo-jie Ye ◽  
Chantelle Gaskin ◽  
Charlotte Butts ◽  
Royce Threadgill ◽  
David R. Knop ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Adeno Associated Virus ◽  
Virus Vectors ◽  
Simplex Virus

scholarly journals Herpes Simplex Virus 1 UL37 Protein Tyrosine Residues Conserved among All Alphaherpesviruses Are Required for Interactions with Glycoprotein K, Cytoplasmic Virion Envelopment, and Infectious Virus Production

2016 ◽  
Vol 90 (22) ◽  
pp. 10351-10361 ◽  
Author(s):  
Dmitry V. Chouljenko ◽  
Nithya Jambunathan ◽  
Vladimir N. Chouljenko ◽  
Misagh Naderi ◽  
Michal Brylinski ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infectious Virus ◽  
Virus Production ◽  
Herpes Simplex Virus 1 ◽  
Anterograde Transport ◽  
Tyrosine Residues ◽  
Glycoprotein K ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACTThe herpes simplex virus 1 (HSV-1) UL37 protein functions in virion envelopment attrans-Golgi membranes, as well as in retrograde and anterograde transport of virion capsids. Recently, we reported that UL37 interacts with glycoprotein K (gK) and its interacting partner protein UL20 (N. Jambunathan, D. Chouljenko, P. Desai, A. S. Charles, R. Subramanian, V. N. Chouljenko, and K. G. Kousoulas, J Virol 88:5927–5935, 2014,http://dx.doi.org/10.1128/JVI.00278-14), facilitating cytoplasmic virion envelopment. Alignment of UL37 homologs encoded by alphaherpesviruses revealed the presence of highly conserved residues in the central portion of the UL37 protein. A cadre of nine UL37 site-specific mutations were produced and tested for their ability to inhibit virion envelopment and infectious virus production. Complementation analysis revealed that replacement of tyrosines 474 and 480 with alanine failed to complement the UL37-null virus, while all other mutated UL37 genes complemented the virus efficiently. The recombinant virus DC474-480 constructed with tyrosines 474, 476, 477, and 480 mutated to alanine residues produced a gK-null-like phenotype characterized by the production of very small plaques and accumulation of capsids in the cytoplasm of infected cells. Recombinant viruses having either tyrosine 476 or 477 replaced with alanine produced a wild-type phenotype. Immunoprecipitation assays revealed that replacement of all four tyrosines with alanines substantially reduced the ability of gK to interact with UL37. Alignment of HSV UL37 with the human cytomegalovirus and Epstein-Barr virus UL37 homologs revealed that Y480 was conserved only for alphaherpesviruses. Collectively, these results suggest that the UL37 conserved tyrosine 480 residue plays a crucial role in interactions with gK to facilitate cytoplasmic virion envelopment and infectious virus production.IMPORTANCEThe HSV-1 UL37 protein is conserved among all herpesviruses, functions in both retrograde and anterograde transport of virion capsids, and plays critical roles in cytoplasmic virion envelopment by interacting with gK. We show here that UL37 tyrosine residues conserved among all alphaherpesviruses serve critical roles in cytoplasmic virion envelopment and interactions with gK.

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