The Three-Dimensional Structure of Canine Parvovirus and Its Functional Implications

Tsao, Jun; Chapman, Michael; Agbandje, Mavis; Keller, Walter; Smith, Kathy; Wu, Hao; Luo, Ming; Smith, Thomas J.; Rossmann, Michael G.; Compans, Richard W.; Parrish, Colin R.

doi:10.1142/9789814513357_0026

Cited by 8 publications

(12 citation statements)

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“…The second region had an average height of 3.5 but was not easily interpreted in terms of a standard nucleotide structure. Icosahedrally ordered genome structure has been previously observed in canine parvovirus (36) and minute virus of mice (35) but not in invertebrate densoviruses (Table 1). …”

Section: Resultsmentioning

confidence: 88%

“…Residues lining the channel are mostly hydrophobic and guide the externalization of a conserved glycine-rich sequence near the amino ends of the VPs (35)(36)(37). The loops connecting the ␤-strands of the jelly roll fold are usually exceptionally large in parvoviruses compared with the loops in picornaviruses (28,38) and form the exterior of the virus and intersubunit contacts (Fig.…”

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confidence: 99%

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The Structure and Host Entry of an Invertebrate Parvovirus

Meng

Zhang

Plevka

et al. 2013

J Virol

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bThe 3.5-Å resolution X-ray crystal structure of mature cricket parvovirus (Acheta domesticus densovirus [AdDNV]) has been determined. Structural comparisons show that vertebrate and invertebrate parvoviruses have evolved independently, although there are common structural features among all parvovirus capsid proteins. It was shown that raising the temperature of the AdDNV particles caused a loss of their genomes. The structure of these emptied particles was determined by cryo-electron microscopy to 5.5-Å resolution, and the capsid structure was found to be the same as that for the full, mature virus except for the absence of the three ordered nucleotides observed in the crystal structure. The viral protein 1 (VP1) amino termini could be externalized without significant damage to the capsid. In vitro, this externalization of the VP1 amino termini is accompanied by the release of the viral genome. Parvoviruses are small (ϳ250-to 300-Å-diameter), singlestranded DNA (ssDNA), icosahedral (Tϭ1), nonenveloped viruses whose genomes are approximately 5 kb long (1). The Parvoviridae family has been subdivided into viruses that infect vertebrates (Parvovirinae) and those that infect invertebrates (Densovirinae) (2). Parvoviruses replicate in dividing cells such as in tissues from insect larvae and fetuses. Densoviruses are highly pathogenic, and those that use insect hosts usually kill 90% of the larvae within a few days (2). Densoviruses pose a threat to commercial invertebrates such as shrimp (3), silkworms (4), and crickets (5, 6). Some highly pathogenic densoviruses are potential selective pesticides for vectors that transmit mosquito-borne diseases (7). Parvovirinae generally have three types of proteins (VP1, VP2, and VP3) in their capsids (8), whereas Densovirinae generally have four types of proteins (VP1 to VP4) in their capsids (2). In densoviruses there are 200 additional amino acids in VP1 at the N terminus. These different proteins result from different initiation sites for translation of the capsid gene and from posttranslational modification of their N termini (8). Generally, each of the 60 subunits within a capsid has the same amino acid sequence and is structurally the same, except that the different proteins start at different amino acids. The VP2s of some densoviruses are unique among VP2s of parvoviruses since they are not completely contained within corresponding VP1s (Fig. 1A).Parvoviruses enter cells by dynamin-dependent receptor-mediated endocytosis and escape the endosome by the phospholipase (PLA2) activity within the amino-terminal domain of VP1 (9-13). Although there is often less than 5% amino acid identity among the structural proteins of parvoviruses, the sequence of the PLA2 N-terminal domain of VP1 has more than 30% amino acid identity ( Fig. 1A and B). The PLA2 domain is not exposed in assembled, full parvoviruses such as minute virus of mice (MVM) (13) and human parvovirus B19 (14), and it therefore has to be exposed during endocytosis (9,11,(13)(14)(15). However, the mechanism by which ...

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Section: Resultsmentioning

confidence: 88%

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confidence: 99%

The Structure and Host Entry of an Invertebrate Parvovirus

Meng

Zhang

Plevka

et al. 2013

J Virol

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“…The amino acid residue 440 is important because it is located at the top of the 3-fold spike (GH loop) of the VP2 protein on the surface of the capsid, the main antigenic site of the virus [49,50]. This residue was undergoing positive selection for the past few years and had evolved independently in different populations, which explained its world-wide mutation in unrelated CPV-2 populations [51].…”

Section: Discussionmentioning

confidence: 99%

Full-length VP2 gene analysis of canine parvovirus reveals emergence of newer variants in India

Nookala¹,

Mukhopadhyay²,

Sivaprakasam³

et al. 2016

Acta Microbiologica et Immunologica Hungarica

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The canine parvovirus (CPV) infection is a highly contagious and serious enteric disease of dogs with high fatality rate. The present study was taken up to characterize the full-length viral polypeptide 2 (VP2) gene of CPV of Indian origin along with the commercially available vaccines. The faecal samples from parvovirus suspected dogs were collected from various states of India for screening by PCR assay and 66.29% of samples were found positive. Six CPV-2a, three CPV-2b, and one CPV-2c types were identified by sequence analysis. Several unique and existing mutations have been noticed in CPV types analyzed indicating emergence of newer variants of CPV in India. The phylogenetic analysis revealed that all the field CPV types were grouped in different subclades within two main clades, but away from the commercial vaccine strains. CPV-2b and CPV-2c types with unique mutations were found to be establishing in India apart from the prevailing CPV-2a type. Mutations and the positive selection of the mutants were found to be the major mechanism of emergence and evolution of parvovirus. Therefore, the incorporation of local strain in the vaccine formulation may be considered for effective control of CPV infections in India.

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“…The structures for several members of the mammalian Parvoviridae have been determined using X-ray crystallography and/or cryoelectron microscopy and image reconstruction (cryoreconstruction), including those of MVM, canine parvovirus (CPV), feline panleukopenia virus (FPV), and porcine parvovirus (PPV) (28)(29)(30)(31)(32)(33)(34)(35)(36). In most of these structures, only ϳ520 to 550 residues (depending on the virus) of VP2 (or VP3 in virions) in the overlapping polypeptide region is observed.…”

Section: H -1 Parvovirus (H-1pvmentioning

confidence: 99%

Structural Characterization of H-1 Parvovirus: Comparison of Infectious Virions to Empty Capsids

Halder

Nam

Govindasamy

et al. 2013

J Virol

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bThe structure of single-stranded DNA (ssDNA) packaging H-1 parvovirus (H-1PV), which is being developed as an antitumor gene delivery vector, has been determined for wild-type (wt) virions and noninfectious (empty) capsids to 2.7-and 3.2-Å resolution, respectively, using X-ray crystallography. The capsid viral protein (VP) structure consists of an ␣-helix and an eightstranded anti-parallel ␤-barrel with large loop regions between the strands. The ␤-barrel and loops form the capsid core and surface, respectively. In the wt structure, 600 nucleotides are ordered in an interior DNA binding pocket of the capsid. This accounts for ϳ12% of the H-1PV genome. The wt structure is identical to the empty capsid structure, except for side chain conformation variations at the nucleotide binding pocket. Comparison of the H-1PV nucleotides to those observed in canine parvovirus and minute virus of mice, two members of the genus Parvovirus, showed both similarity in structure and analogous interactions. This observation suggests a functional role, such as in capsid stability and/or ssDNA genome recognition for encapsulation. The VP structure differs from those of other parvoviruses in surface loop regions that control receptor binding, tissue tropism, pathogenicity, and antibody recognition, including VP sequences reported to determine tumor cell tropism for oncotropic rodent parvoviruses. These structures of H-1PV provide insight into structural features that dictate capsid stabilization following genome packaging and three-dimensional information applicable for rational design of tumor-targeted recombinant gene delivery vectors. H -1 parvovirus (H-1PV) is a member of the rodent subgroup of the Parvovirus genus of the single-stranded DNA (ssDNA) Parvoviridae (1). H-1PV was first isolated from rats transplanted with HEP-1, a human liver adenocarcinoma cell line (2), and also from aborted human fetuses (3). Recombinant vectors based on H-1PV and a number of other rodent parvoviruses, including minute virus of mice (MVM) and LuIII, are promising candidates for antitumor delivery vectors, particularly for cytoreductive and immunogene therapy approaches (reviewed in references 4 and 5). The inherent oncotropism of these autonomous parvoviruses is based on their dependence on cellular proliferation factors expressed during the S phase and the differentiated state of the host cell (6, 7). The rodent parvoviruses display oncopreferential cytotoxic activity in vitro and also possess an oncosuppressive potential, inhibiting the formation of spontaneous and chemical or virus-induced tumors in vitro and in vivo (8-13). These viruses can also persistently infect their natural hosts, do not integrate their genome into cellular chromosomes, and are not associated with human disease (reviewed in reference 4).Recombinant rodent parvovirus vectors targeted for tumor therapy utilize a double-edged strategy that takes advantage of their inherent oncotropism and selective cytotoxicity plus their ability to deliver therapeutic genes that code for ...

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The Three-Dimensional Structure of Canine Parvovirus and Its Functional Implications

Cited by 8 publications

References 0 publications

The Structure and Host Entry of an Invertebrate Parvovirus

The Structure and Host Entry of an Invertebrate Parvovirus

Full-length VP2 gene analysis of canine parvovirus reveals emergence of newer variants in India

Structural Characterization of H-1 Parvovirus: Comparison of Infectious Virions to Empty Capsids

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