Activation and inhibition of expression of the 72,000-da early protein of adenovirus type 5 in mouse cells constitutively expressing an immediate early protein of herpes simplex virus type 1

Virology ◽  
1985 ◽  
Vol 144 (1) ◽  
pp. 35-45 ◽  
Author(s):  
Michel L. Tremblay ◽  
Siu-Pok Yee ◽  
Roy H. Persson ◽  
Silvia Bacchetti ◽  
James R. Smiley ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Adenovirus Type ◽  
Early Protein ◽  
Mouse Cells ◽  
Simplex Virus ◽  
Adenovirus Type 5

scholarly journals The Interplay between Adeno-Associated Virus and Its Helper Viruses

Viruses ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 662 ◽  
Author(s):  
Anita F. Meier ◽  
Cornel Fraefel ◽  
Michael Seyffert
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Adenovirus Type ◽  
Adeno Associated Virus ◽  
Basic Biology ◽  
Simplex Virus ◽  
Adenovirus Type 5

The adeno-associated virus (AAV) is a small, nonpathogenic parvovirus, which depends on helper factors to replicate. Those helper factors can be provided by coinfecting helper viruses such as adenoviruses, herpesviruses, or papillomaviruses. We review the basic biology of AAV and its most-studied helper viruses, adenovirus type 5 (AdV5) and herpes simplex virus type 1 (HSV-1). We further outline the direct and indirect interactions of AAV with those and additional helper viruses.

scholarly journals Differential Cellular Requirements for Activation of Herpes Simplex Virus Type 1 Early (tk) and Late (gC) Promoters by ICP4

2004 ◽  
Vol 78 (12) ◽  
pp. 6162-6170 ◽  
Author(s):  
Susan Zabierowski ◽  
Neal A. DeLuca
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Late Gene ◽  
Early Protein ◽  
Late Genes ◽  
Nuclear Extracts ◽  
Simplex Virus

ABSTRACT The herpes simplex virus type 1 immediate-early protein, ICP4, activates the transcription of viral early and late genes and is essential for viral growth. It has been shown to bind DNA and interact with components of the general transcription machinery to activate or repress viral transcription, depending upon promoter context. Since early and late gene promoters have different architectures and cellular metabolism may be very different at early and late times after infection, the cellular requirements for ICP4-mediated activation of early and late genes may differ. This hypothesis was tested using tk and gC as representative early and late promoters, respectively. Nuclear extracts and phosphocellulose column fractions derived from nuclear extracts were able to reconstitute basal and ICP4-activated transcription of both promoters in vitro. When examining the contribution of the general transcription factors on the ability of ICP4 to activate transcription, the fraction containing the general transcription factor TFIIA was not essential for ICP4 activation of the gC promoter, but it was required for efficient activation of the tk promoter. The addition of recombinant TFIIA restored the ability of ICP4 to efficiently activate the tk promoter, but it had no net effect on activation of the gC promoter. The dispensability of TFIIA for ICP4 activation of the gC promoter required an intact INR element. In addition, microarray and Northern blot analysis indicated that TFIIA abundance may be reduced at late times of infection. This decrease in TFIIA expression during infection and its dispensability for activation of late but not early genes suggest one of possibly many mechanisms for the transition from viral early to late gene expression.

scholarly journals Origin of Expression of the Herpes Simplex Virus Type 1 Protein US1.5

2009 ◽  
Vol 83 (18) ◽  
pp. 9183-9194 ◽  
Author(s):  
J. Jason Bowman ◽  
Priscilla A. Schaffer
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Expression Patterns ◽  
Full Length ◽  
Early Protein ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT ICP22, an immediate-early protein of herpes simplex virus type 1 (HSV-1), is required for viral replication in nonpermissive cell types and for expression of a class of late viral proteins which includes glycoprotein C. An understanding of the mechanism of ICP22 function has been complicated by the coexpression of the full-length protein with an in-frame, C-terminus-specific protein, US1.5. In this report, we confirm that the US1.5 protein is a bona fide translation product since it is detected during infections with three laboratory strains and two low-passage clinical isolates of HSV-1. To clarify the expression patterns of the ICP22 and US1.5 proteins, we examined their synthesis from plasmids in transient expression assays. Because previous studies had identified two different US1.5 translational start sites, we attempted to determine which is correct by studying the effects of a series of deletion, nonsense, and methionine substitutions on US1.5 expression. First, amino acids 90 to 420 encoded by the ICP22 open reading frame (ORF) migrated at the mobility of US1.5 in sodium dodecyl sulfate-polyacrylamide gels. Second, introduction of a stop codon downstream of M90 ablated expression of both ICP22 and US1.5. Finally, mutation of M90 to alanine (M90A) allowed expression of full-length ICP22 while dramatically reducing expression of US1.5. Levels of US1.5 but not ICP22 protein expression were also reduced in cells infected with an M90A mutant virus. Thus, we conclude that expression of IC22 and that of US1.5 can occur independently of each other and that US1.5 translation initiates at M90 of the ICP22 ORF.

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