DNA sequence and expression of the B95-8 Epstein—Barr virus genome

Baer, Richard; Bankier, Alan T.; Biggin, Mark D.; Deininger, Prescott L.; Farrell, Patrick J.; Gibson, Toby J.; Hatfull, Graham F.; Hudson, Graham S.; Satchwell, Sandra C.; Séguin, Carl; Tuffnell, P.; Barrell, Bart

doi:10.1038/310207a0

Cited by 1,951 publications

(1,204 citation statements)

References 60 publications

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“…The cloning of genes or cDNAs for UDGs from bacteria [40], yeast [41], the fish Xiphophorus [42], mouse [43] and human cells [43,44] and several herpes viruses [45][46][47][48][49][50][51][52] has demonstrated a striking similarity between these enzymes, ranging from 40.3 % (yeast) to 90 % (mouse) amino acid identity relative to human UDG. The similarity is confined to several discrete boxes.…”

Section: Udgs Belong To a Highly Conserved Ancient Familymentioning

confidence: 99%

DNA glycosylases in the base excision repair of DNA

Krokan

Standal

Slupphaug

1997

Biochemical Journal

766

566

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A wide range of cytotoxic and mutagenic DNA bases are removed by different DNA glycosylases, which initiate the base excision repair pathway. DNA glycosylases cleave the Nglycosylic bond between the target base and deoxyribose, thus releasing a free base and leaving an apurinic\apyrimidinic (AP) site. In addition, several DNA glycosylases are bifunctional, since they also display a lyase activity that cleaves the phosphodiester backbone 3h to the AP site generated by the glycosylase activity. Structural data and sequence comparisons have identified common features among many of the DNA glycosylases. Their active sites have a structure that can only bind extrahelical target bases, as observed in the crystal structure of human uracil-DNA glycosylase in a complex with double-stranded DNA. Nucleotide flipping is apparently actively facilitated by the enzyme. With bacteriophage T4 endonuclease V, a pyrimidine-

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Section: Udgs Belong To a Highly Conserved Ancient Familymentioning

confidence: 99%

DNA glycosylases in the base excision repair of DNA

Krokan

Standal

Slupphaug

1997

Biochemical Journal

766

566

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“…On the other hand a 40 Kb DNA fragment (named p31) including the BamH1 D to BamH1 A regions of EBV genome, has been found able to immortalize epithelial cells from African green monkey kidney (Gri n and Karran, 1984) and marmoset or human fetal kidney (Karran et al, 1990). Among about 20 ORFs (Open Reading Frames) localized in this 40 kb fragment (Baer et al, 1984), BARF0 and BARF1 were reported to be expressed in biopsies from NPC patients (Hitt et al, 1989;Sbih-Lammali et al, 1996), suggesting that either or both ORFs might be involved in epithelial cell immortalization process. We have previously shown that BARF1 ORF expression induced tumorigenic transformation in either the rodent ®broblast line Balb/c 3T3 (Wei and Ooka, 1989) or in the human EBV-negative B cell line Louckes (Wei et al, 1994): after injection of BARF1-transfected cells into new-born rats, we observed the development of agressive tumors from the murine ®broblasts, while the Louckes line induced small tumors which disappeared after 3 weeks post-injection.…”

Section: Introductionmentioning

confidence: 99%

Establishment of a monkey kidney epithelial cell line with the BARF1 open reading frame from Epstein-Barr Virus

Decaussin

et al. 1997

Oncogene

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“…Homology scores with human collagenase (54) and with the metalloproteinase of Serratia (60) were considerably lower. Interestingly, optimized alignment of fibrolase and BRRFl protein (Baer et al, 1984) shows that the viral protein retains the essential components of the zinc-binding site, including the consensus signature. The significance, if any, of this identity remains to be established, although it raises some intriguing questions concerning symbiotic relationships between viruses and snakes.…”

Section: A Randolph Et Afmentioning

confidence: 99%

Amino acid sequence of fibrolase, a direct‐acting fibrinolytic enzyme from agkistrodon contortrix contortrix venom

Randolph¹,

Chamberlain²,

Chu³

et al. 1992

Protein Science

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The complete amino acid sequence of fibrolase, a fibrinolytic enzyme from southern copperhead (Agkistrodon contortrix contortrix) venom, has been determined. This is the first report of the sequence of a direct-acting, nonhemorrhagic fibrinolytic enzyme found in snake venom. The majority of the sequence was established by automated Edman degradation of overlapping peptides generated by a variety of selective cleavage procedures. The amino-terminus is blocked by a cyclized glutamine (pyroglutamic acid) residue, and the sequence of this region of the molecule was determined by mass spectrometry. Fibrolase is composed of 203 residues in a single polypeptide chain with a molecular weight of 22,891, as determined by the sequence. Its sequence is homologous to the sequence of the hemorrhagic toxin Ht-d of Crotalus atrox venom and with the sequences of two metalloproteinases from Trimeresurusflavoviridis venom. Microheterogeneity in the sequence was found at both the amino-terminus and at residues 189 and 192. All six cysteine residues in fibrolase are involved in disulfide bonds. A disulfide bond between cysteine-118 and cysteine-198 has been established and bonds between cysteines-158/165 and between cysteines-160/192 are inferred from the homology to Ht-d. Secondary structure prediction reveals a very low percentage of a-helix (4"70), but much greater 0-structure (39.5%). Analysis of the sequence reveals the absence of asparagine-linked glycosylation sites defined by the consensus sequence: asparagine-X-serine/threonine. Keywords: amino acid sequence; secondary structure; snake venom fibrolase Fibrinolytic activity has been found in the venom of snakes from the families Crotalidae, Viperidae, and Elapidae, with venom from members of the Crotalidae having the highest levels of fibrinolytic activity (for a recent review, see Markland, 1988). Fibrolase is a direct-acting fibrinolytic enzyme from southern copperhead (Agkistrodon contortrix contortrix) venom that does not require bloodborne cofactors for activity (Guan et al., 1991). As previously described (Markland, 1983;Markland et al., 1988; Reprint requests to: Anne Randolph, Chiron Research Laboratories, Retzios & Markland, 1988), the enzyme is a nonhemorrhagic, zinc metalloproteinase which cleaves primarily the a-chain of human fibrinogen and fibrin. Specific cleavage sites have been determined for several venom metalloproteinases using natural or synthetic substrates (Tu et al., 1981;Hagihara et al., 1985;Fox et al., 1986;Mori et al., 1987).

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DNA sequence and expression of the B95-8 Epstein—Barr virus genome

Cited by 1,951 publications

References 60 publications

DNA glycosylases in the base excision repair of DNA

DNA glycosylases in the base excision repair of DNA

Establishment of a monkey kidney epithelial cell line with the BARF1 open reading frame from Epstein-Barr Virus

Amino acid sequence of fibrolase, a direct‐acting fibrinolytic enzyme from agkistrodon contortrix contortrix venom

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