Dataset Information

Junonia coenia Densovirus (JcDNV) Genome Structure.

ABSTRACT: The sequence of Junonia coenia densovirus was the first densovirus genome sequence published, but the first published sequence contained incomplete inverted terminal repeats and ambiguous nucleotides or indels leading to an incorrect map of the open reading frames. Our sequencing of clones of the complete genome demonstrated that this virus is closely related to other viruses in the Densovirus genus.

SUBMITTER: Pham HT

PROVIDER: S-EPMC3738899 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Junonia coenia Densovirus (JcDNV) Genome Structure.

Pham Hanh T HT Huynh Oanh T H OT Jousset Françoise-Xavière FX Bergoin Max M Tijssen Peter P

Genome announcements 20130808 4

The sequence of Junonia coenia densovirus was the first densovirus genome sequence published, but the first published sequence contained incomplete inverted terminal repeats and ambiguous nucleotides or indels leading to an incorrect map of the open reading frames. Our sequencing of clones of the complete genome demonstrated that this virus is closely related to other viruses in the Densovirus genus. ...[more]

PMID: 23929483

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Project description:Junonia coenia densovirus (JcDNV) is an autonomous parvovirus that infects the larvae of the common buckeye butterfly, Junonia coenia. Unlike vertebrate parvoviruses, the genes encoding the structural protein and nonstructural (NS) proteins of JcDNV are in opposite orientations; thus, each strand contains a sense and antisense open reading frame (ORF). The promoter at map position 93 controls expression of NS ORFs 2, 3, and 4, which encode three NS proteins, NS-1, NS-2, and NS-3. These proteins are likely to be involved in viral DNA replication, among other functions. In contrast to the nonstructural proteins of the vertebrate parvoviruses, the NS proteins of the Densovirinae have not been characterized. Here, we describe biochemical properties of the NS-1 protein of JcDNV. The NS-1 ORF was cloned in frame with the Escherichia coli malE gene, which encodes the bacterial maltose binding protein (MBP). Using electrophoretic mobility shift and DNase I protection assays, we identified the region of the JcDNV terminal sequence that is recognized specifically by the MBP-NS-1 fusion protein. The site consists of (GAC)4 and is located on the A-A' region of the terminal palindrome. In addition, the MBP-NS-1 fusion protein catalyzes the cleavage of single-stranded DNA (ssDNA) substrates derived from the JcDNV putative origin of replication, primarily at two sites in the motif 5'-G*TAT*TG-3'. One cleavage site is between the thymidine dinucleotide at positions 92 and 93 and the other site corresponds to thymidine at nucleotide 95; both sites are on the complementary strand of the sequence assigned GenBank accession number A12984. Cleavage of ssDNA is dependent on the presence of a divalent metal cofactor but does not require nucleoside triphosphate hydrolysis. Parvovirus NS proteins contain the phylogenically conserved Walker A- and B-site ATPase motifs. These sites in JcDNV NS-1 diverge from the consensus, yet despite these atypical motifs our analyses support that MBP-NS-1 has ATP-dependent helicase activity. These results indicate that JcDNV NS-1 possesses activities common to the superfamily of rolling-circle replication initiator proteins in general and the parvovirus replication proteins in particular, and they provide a basis for comparative analyses of the structure and function relationships among the parvovirus NS-1 equivalents.

Dataset Information

Junonia coenia Densovirus (JcDNV) Genome Structure.

Publications

Junonia coenia Densovirus (JcDNV) Genome Structure.

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