Molecular cloning and nucleotide sequence of deer papillomavirus

Abstract

The genome of deer papillomavirus (DPV) isolated from American white-tailed deer was cloned into pBR322, and the entire nucleotide sequence of 8,374 base pairs was determined. The overall genetic organization of the DPV genome was similar to that of other papillomaviruses. All significant open reading frames were located on one strand, and the locations of putative promoters and polyadenylation signals were similar to those identified in the closely related bovine papillomavirus type 1 (BPV-1) genome. The DPV genome was approximately colinear with BPV-1 except for a noncoding region separating the early and late regions. The regions of highest nucleotide sequence homology between DPV and BPV-1 were found in the E1 open reading frame coding for BPV-1 DNA replication function and in the L1 open reading frame, which encodes the major capsid protein of BPV-1.

Bovine papillomavirus type 1 E1 replication-defective mutants are altered in their transcriptional regulation

“…Pooled G418-resistant colonies were expanded, and total cellular DNA and RNA were analyzed. Based upon South- ern blot analysis of cellular DNAs cleaved with a no-cut enzyme for the transfected BPV-1 plasmids, the El mutated BPV-1 DNAs were found to be integrated (data not shown) and in low copy number, in agreement with previous studies (8,15,19,21). This result contrasts with the extrachromosomal state and high copy number of wt BPV-1.…”

“…The observations made in this study may provide further evidence for coordinated regulation between viral transcription and viral replication. Previous studies have implicated a role for the E2 transcriptional control circuit in viral DNA plasmid replication by demonstrating that BPV-1 E2 mutants are replication defective (3,4,8,19). A mechanistic link between E2 transcriptional regulation and viral DNA replication was provided by the mapping of an E2-responsive element, E2RE2, to the region containing the P7185 and PL promoters (24).…”

Activation of the platelet-derived growth factor receptor by the bovine papillomavirus E5 transforming protein.

“…Inspection of the amino acid sequences of the BPV E5 protein and PDGF itself revealed that these proteins share a short stretch of similar amino acid sequences (Figure 8). This similarity is also evident in the comparison between PDGF B and the deer papillomavirus E5 protein, which we have recently shown is capable of transforming C127 cells and activating both the precursor and mature forms of the PDGF receptor (Groff and Lancaster, 1985; R.Kulke and D.DiMaio, in preparation). Thus, the fibropapillomavirus ESproteins and PDGF share structural as well as functional similarity, implying that constitutive activation of the receptor 852 BPV E5 protein activates the PDGF receptor may result from a direct physical interaction between the E5 protein and the PDGF receptor.…”

Structural and mutational analysis of E2 trans-activating proteins of papillomaviruses reveals three distinct functional domains.

“…But at the amino acid level, the homology between the putative proteins of papillomaviruses is too low to allow such a conclusion: -30 % within the E6 ORFs and -55 % for the most conserved ORF, El. The homology between the E2 ORFs of unrelated papillomaviruses such as HPV 11 Our amino acid sequence analysis of the E2 proteins is based on the first 10 papillomavirus genomes sequences determined: two fibropapillomaviruses, BPV1I (Chen et al, 1982) and the deer papillomavirus DPV (Groff et al, 1985) which are closely related, three cutaneous viruses, CRPV (Gini et al, 1985a), HPVlI, the agent of deep plantar warts (Danos et al, 1982) and HPV8, a virus associated with a rare cutaneous disease (Epidermodysplasia verruciformis) (Fuchs et al, 1986), and five human genital viruses, three 2824 of them (HPV 16, HPV18 and HPV33) being strongly implicated in the aetiology of genital cancers (Seedorf et al, 1985;Cole and Streeck, 1986;Cole and Danos, 1987); whereas HPVI11 and HPV6 are rarely found in invasive tumours (Dartmann et al, 1986;Schwarz et al, 1983). As shown in Figure 1, only 9 % of the amino acids are conserved within the 10 proteins.…”