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An antibody made against the herpes simplex virus 1 US 5 gene predicted to encode glycoprotein J was found to react strongly with two proteins, one with an apparentM r of 23,000 and mapping in the S component and one with a herpes simplex virus protein with an apparentM r of 43,000. The antibody also reacted with herpes simplex virus type 2 proteins forming several bands with apparentM r s ranging from 43,000 to 50,000. Mapping studies based on intertypic recombinants, analyses of deletion mutants, and ultimately, reaction of the antibody with a chimeric protein expressed by in-frame fusion of the glutathioneS -transferase gene to an open reading frame antisense to the gene encoding glycoprotein B led to the definitive identification of the new open reading frame, designated UL 27.5. Sequence analyses indicate the conservation of a short amino acid sequence common to US 5 and UL 27.5. The coding sequence of the herpes simplex virus UL 27.5 open reading frame is strongly homologous to the sequence encoding the carboxyl terminus of the herpes simplex virus 2 UL 27.5 sequence. However, both open reading frames could encode proteins predicted to be significantly larger than the mature UL 27.5 proteins accumulating in the infected cells, indicating that these are either processed posttranslationally or synthesized from alternate, nonmethionine-initiating codons. The UL 27.5 gene expression is blocked by phosphonoacetate, indicating that it is a γ2 gene. The product accumulated predominantly in the cytoplasm. UL 27.5 is the third open reading frame found to map totally antisense to another gene and suggests that additional genes mapping antisense to known genes may exist.

U L 27.5 Is a Novel γ 2 Gene Antisense to the Herpes Simplex Virus 1 Gene Encoding Glycoprotein B

U _L 27.5 Is a Novel γ ₂ Gene Antisense to the Herpes Simplex Virus 1 Gene Encoding Glycoprotein B