Herpes simplex virus expressing Epstein-Barr virus nuclear antigen 1

Mary Hummel, Minas Arsenakis, Andrew Marchini, Linda Lee, Bernard Roizman, Elliott Kieff

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


DNA fragments containing an open reading frame known to encode most or all of the EBNAl protein of Epstein-Barr virus (EBV) were fused in the proper transcriptional orientation to the promoter regulatory domain, capping site. and a portion of the 5′ transcribed noncoding sequences of the HSV-1 α4 gene of herpes simplex virus 1 (HSV-1). In these constructs 20, 130, or 385 bp of EBV DNA and 28 bp of HSV-1 DNA separated the α4 cap site from a putative initiator codon of the EBNA1 gene. The chimeric α4-EBNA1 genes were introduced into L cells or recombined into the viral genome using the thymidine kinase selection system. The three chimeric gene constructs resident in the L cell clones expressed a protein indistinguishable from authentic EBNA1 with respect to electrophoretic and immunologic properties indicating that the ATG at the beginning of the EBV open reading frame initiated translation of the bonafide EBNAl protein. The chimeric α4EBNA1 genes resident in L cells were induced by HSV-1 infection and were regulated as α genes. The chimeric α4-EBNA1 gene recombined into the viral genome was also regulated as an α gene. The recombinant viruses were stable and expressed 50- to 100-fold more EBNAl than is ordinarily expressed in human lymphocytes carrying the EBV genome. EBNA1 did not alter the program of HSV-1 protein expression. The utility of the vector is discussed.

Original languageEnglish (US)
Pages (from-to)337-348
Number of pages12
Issue number2
StatePublished - Jan 30 1986
Externally publishedYes

ASJC Scopus subject areas

  • Virology


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