Nucleotide and predicted amino acid sequences of Marek's disease virus homologues of herpes simplex virus major tegument proteins

Abstract

The DNA sequence of an 8-4kbp BamHI-EcoRI fragment of Marek's disease virus (MDV) strain GA was determined. Three of the predicted polypeptides are homologous to UL47, UL48 and UL49 encoding the major tegument proteins of herpes simplex virus type 1 (HSV-1), and four are homologous to HSV-1 UL45, UL46, UL49-5 and UL50. These seven genes are found in the long unique region of the MDV genome and are collinear with homologues in HSV-1 and varicella-zoster virus (VZV). Northern blot analysis revealed different transcriptional patterns from those of HSV-1 and VZV. MDV homologues of UL49.5, UL49 and UL47 lack a poly(A) signal immediately downstream of their coding regions. Amino acid conservation between MDV and HSV-1, and between MDV and VZV is as high as that between HSV-1 and VZV. The MDV homologue of UL48 shows 60% similarity to its HSV-1 counterpart. Amino acid sequence comparison reveals that the MDV homologue of UL48 lacks an acidic carboxyl terminus. This homologue, like the VZV homologue of UL48, may be involved in the trans-activation of immediate early genes and may function as an important component of the structural proteins.

Identification and transcriptional analysis of the homologues of the herpes simplex virus type 1 UL41 to UL51 genes in the genome of nononcogenic Marek's disease virus serotype 2.

“…MDV2 UL48 protein has a rather high homology with the HSV-1 UL48 protein, which was reported as a transactivator of immediate-early gene expression after virus infection (Roizman & Sears, 1996). When compared with MDV1 UL48 protein (Yanagida et al, 1993), high homology is found in the acidic domain (residues 1 to 60) and the prolinerich domain (residues 60 to 100) in the N-terminal region of MDV2. However, the MDV2 UL48 protein lacks a region corresponding to the C-terminal activation domain of the HSV-1 UL48 gene product similar to those of VZV, HVT and MDV1 (data not shown).…”

“…The UL49.5 proteins of PRV and BHV-1 are structural components of the viral envelope Liang et al, 1996). The MDV2 UL49.5 gene encodes a 95 amino acid protein with 71 % identity to that of MDV1 (Yanagida et al, 1993), exhibiting characteristics of a membrane protein without a consensus N-glycosylation sequence as described elsewhere (Barnett et al, 1992 ;. The deduced protein of MDV2 UL50 exhibited homology to dUTPase of other alphaherpesviruses.…”

“…A distinct set of apparently 3h-coterminal transcripts was detected by probes VI, VII and VIII. The highly abundant 2n5 kb mRNA detected by probes VI and VII but not Y. Izumiya and others Y. Izumiya and others by probe VIII is possibly a transcript of both the UL48 and UL49 genes, similar to other serotypes of MDV1 (Yanagida et al, 1993) and HVT (Kopa! cek et al, 1997) ; the 2n7 kb transcript reacting with all probes is apparently derived from the UL49.5 gene.…”

“…The MDV2 UL49.5 ORF overlaps the 5h end of the UL50 ORF in a headto-head orientation as shown for VZV (Davison & Scott, 1986), EHV-1 , BHV-1 (Liang et al, 1993), MDV1 (Yanagida et al, 1993) and pseudorabies virus (PRV) . Although several minor ORFs (ORF 208, ORF 91 and ORF 108), conserved within the MDV1 UL45, UL48 and UL49 genes, respectively, were reported by Yanagida et al (1993), no corresponding ORFs were found in the present sequence of the MDV2 genome. Each of the 12 MDV2 ORFs contains a number of potential transcriptional regulatory sites.…”

Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16

“…(A) Schematic representation of VP16 homologs from five herpesviruses and delineation of the VP16-core protein used for crystallography. The VP16 homologs are derived from HSV-1 (strain 17; Campbell et al 1984;Dalrymple et al 1985), VZV (Davison and Scott 1986), GHV-1 (Yanagida et al 1993), EHV-1 (Telford et al 1992), and BHV-1 (Carpenter and Misra 1992). A conserved VP16-core region is shown in dark gray and the carboxy-terminal HSV-1 transcriptional activation domain (AD) is shown in light gray.…”