Characterization of a bovine herpesvirus 4 immediate-early RNA encoding a homolog of the Epstein-Barr virus R transactivator

• Published in: Journal of Virology 1993-02, Vol.67 (2), p.773-784
• Main Author: Van Santen, V.L. (Auburn University, Auburn, AL)
• Format: Article
• Language: English
• Subjects: ADN; Amino Acid Sequence; Animals; ARN; Base Sequence; Biological and medical sciences; BOVIN; Cattle; cDNA; Cells, Cultured; CULTIVO DE CELULAS; CULTURE DE CELLULE; DNA-Binding Proteins - genetics; Epstein-Barr virus; Exons - genetics; EXPRESION GENICA; EXPRESSION DES GENES; Fundamental and applied biological sciences. Psychology; GANADO BOVINO; GENE; Gene Expression Regulation, Viral; GENES; GENETICA; Genetics; GENETIQUE; Herpesviridae - genetics; herpesvirus (bovine) 4; Herpesvirus 4, Human - genetics; HERPESVIRUS BOVIN; HERPESVIRUS BOVINO; HERPETOVIRIDAE; homology; Immediate-Early Proteins; Microbiology; Molecular Sequence Data; nucleotide sequence; open reading frame; Promoter Regions, Genetic - genetics; PROTEINAS; PROTEINE; R transactivator; Regulatory Sequences, Nucleic Acid - genetics; RNA 2; RNA, Messenger - genetics; RNA, Viral - genetics; SECUENCIA NUCLEICA; Sequence Homology, Amino Acid; SEQUENCE NUCLEIQUE; Trans-Activators - genetics; Transcription, Genetic; Transcriptional Activation; Viral Proteins - genetics; Virology
• ISSN: 0022-538X; 1098-5514
• DOI: 10.1128/JVI.67.2.773-784.1993

Immediate-early (IE) RNA 2, the less abundant of two bovine herpesvirus 4 (BHV-4) RNAs detected in Madin-Darby bovine kidney cells infected in the presence of cycloheximide, is a 1.8-kb cytoplasmic polyadenylated RNA transcribed from the 8.3-kb HindIII fragment F. The structure of IE RNA 2 has been determined by S1 nuclease and exonuclease VII mapping, primer extension analysis, and sequencing of a partial cDNA. IE RNA 2 consists of a short, approximately 60-nucleotide 5' exon spliced to a 1.8-kb 3' exon. DNA sequence analysis revealed an open reading frame encoding 551 amino acids with sequence homology to the Epstein-Barr virus (EBV) R transactivator and its homolog in herpesvirus saimiri, HVS.R. IE 2 and HVS.R show higher homology to each other than to the EBV R transactivator. The homology is highest in the approximately 320 amino-terminal amino acids. All three proteins have acidic carboxyl termini but have little amino acid sequence homology in this region. In transient expression cotransfection assays, IE 2 activated expression from the BHV-4 early promoter-regulatory region of the major DNA-binding protein homolog over 100-fold in bovine turbinate cells. IE 1 was not necessary for this transactivation and did not augment it. However, IE 2 did not transactivate EBV or herpesvirus saimiri early promoter-regulatory regions that are transactivated by the EBV R transactivator or HVS.R