Expression of Muscovy Duck Parvovirus Capsid Proteins (VP2 and VP3) in a Baculovirus Expression System and Demonstration of Immunity Induced by the Recombinant Proteins

Gall-Reculé, Ghislaine Le; Jestin, Véronique; Chagnaud, P.; Blanchard, Ph.; Jestin, André

doi:10.1099/0022-1317-77-9-2159

Cited by 49 publications

(34 citation statements)

References 13 publications

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“…VP3, a proteolytic cleavage product of VP2, has been observed only in DNAcontaining particles (1,13,51,67). Empty, recombinant viruslike particles (VLPs), self-assembled from MVMp VP2, are morphologically and immunologically similar to native, empty MVMp particles (11,23,35,56), as demonstrated previously for other parvoviral VLPs (29,38,39,57).…”

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confidence: 88%

Minute Virus of Mice, a Parvovirus, in Complex with the Fab Fragment of a Neutralizing Monoclonal Antibody

Kaufmann

López-Bueno

Mateu

et al. 2007

J Virol

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confidence: 88%

Minute Virus of Mice, a Parvovirus, in Complex with the Fab Fragment of a Neutralizing Monoclonal Antibody

Kaufmann

López-Bueno

Mateu

et al. 2007

J Virol

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“…The sequence of the whole VP1 gene was determined in the case of goose parvovirus strain SHM 319 (Brown et al, 1995) and Muscovy duck parvovirus strain 89384 (Le Gall-Reculé et al, 1996). To our knowledge, phylogenetic study in order to analyse the relationship of different goose and duck parvovirus strains was done only on Taiwanese isolates based on the sequence of a 539 bp long polymerase chain reaction (PCR) product that corresponds to a part of VP3 gene (Chang et al, 2000).…”

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confidence: 99%

Phylogenetic analysis of Hungarian goose parvovirus isolates and vaccine strains

et al. 2004

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Polymerase chain reaction and sequencing were used to analyse goose parvovirus field isolates and vaccine strains. Two fragments of the genome were amplified. Fragment "A" represents a region of VP3 gene, while fragment "B" represents a region upstream of the VP3 gene, encompassing part of the VP1 gene. In the region of fragment "A" the deduced amino acid sequence of the strains was identical, therefore differentiation among strains could be done only at the nucleotide level, which resulted in the formation of three groups: Hungarian, West-European and Asian strains. In the region of fragment "B", separation of groups could be done by both nucleotide and deduced amino acid sequence level. The nucleotide sequences resulted in the same groups as for fragment "A" but with a different clustering pattern among the Hungarian strains. Within the "Hungarian" group most of the recent field isolates fell into one cluster, very closely related or identical to each other, indicating a very slow evolutionary change. The attenuated strains and field isolates from 1979/80 formed a separate cluster. When vaccine strains and field isolates were compared, two specific amino acid differences were found that can be considered as possible markers for vaccinal strains. Sequence analysis of fragment "B" seems to be a suitable method for differentiation of attenuated vaccine strains from virulent strains.

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“…A pore at the center of the ␤-cylinder at each pentameric vertex runs between the outer surface of the virion and the interior of the virus. It has been demonstrated for several parvoviruses that VLPs are similar in morphogenicity and antigenicity to native virions (13,15,17,28,44). However, differences in the neutralizing response against B19 VP2 VLPs and VLPs containing VP2 and VP1 indicated that VP1 modifies VP2 epitopes (17, 41).…”

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Visualization of the Externalized VP2 N Termini of Infectious Human Parvovirus B19

Kaufmann

Chipman

Kostyuchenko

et al. 2008

J Virol

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The structures of infectious human parvovirus B19 and empty wild-type particles were determined by cryoelectron microscopy (cryoEM) to 7.5-Å and 11.3-Å resolution, respectively, assuming icosahedral symmetry. Both of these, DNA filled and empty, wild-type particles contain a few copies of the minor capsid protein VP1. Comparison of wild-type B19 with the crystal structure and cryoEM reconstruction of recombinant B19 particles consisting of only the major capsid protein VP2 showed structural differences in the vicinity of the icosahedral fivefold axes. Although the unique N-terminal region of VP1 could not be visualized in the icosahedrally averaged maps, the N terminus of VP2 was shown to be exposed on the viral surface adjacent to the fivefold ␤-cylinder. The conserved glycine-rich region is positioned between two neighboring, fivefold-symmetrically related VP subunits and not in the fivefold channel as observed for other parvoviruses.Human parvovirus B19 (B19) belongs to the genus Erythrovirus within the Parvoviridae family (33, 54) and is highly tropic for erythroid progenitor cells. It is a human pathogen that causes the mild childhood disease erythema infectiosum (4) and has also been associated with a variety of other clinical symptoms, such as arthropathies, hepatitis (34), failure of red cell production (8), hydrops fetalis (18), fetal loss (14), and myocarditis (35).The single-stranded DNA genome of B19 is encapsidated in a nonenveloped protein shell that has an external diameter of about 260 Å (2). The 60 Tϭ1 icosahedrally related protein subunits of the wild-type B19 virus capsid are comprised of two structural proteins, viral protein 1 (VP1; 83 kDa) and VP2 (58 kDa), that are produced from a single open reading frame by transcriptional regulation. The major structural component of the protein shell is VP2, accounting for about 95% of the total capsid protein (36). VP2 alone is sufficient to form icosahedral virus-like particles (VLPs) with characteristic parvoviral surface features, including protrusions adjacent to the threefold axes, depressions at the icosahedral twofold axes, and canyonlike depressions surrounding the ␤-cylindrical structure at the fivefold vertices. A pore at the center of the ␤-cylinder at each pentameric vertex runs between the outer surface of the virion and the interior of the virus. It has been demonstrated for several parvoviruses that VLPs are similar in morphogenicity and antigenicity to native virions (13,15,17,28,44). However, differences in the neutralizing response against B19 VP2 VLPs and VLPs containing VP2 and VP1 indicated that VP1 modifies VP2 epitopes (17, 41).The structural protein VP1 differs from VP2 only in an N-terminal extension of 227 amino acids called the unique region (VP1u). A phospholipase A2-like activity that has been linked to VP1u is required during parvoviral infection (49,53,56,60). In contrast to other mammalian parvoviruses and despite its relatively low concentration in the virion, B19 VP1u represents a dominant antigenic target for neutral...

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Expression of Muscovy Duck Parvovirus Capsid Proteins (VP2 and VP3) in a Baculovirus Expression System and Demonstration of Immunity Induced by the Recombinant Proteins

Cited by 49 publications

References 13 publications

Minute Virus of Mice, a Parvovirus, in Complex with the Fab Fragment of a Neutralizing Monoclonal Antibody

Minute Virus of Mice, a Parvovirus, in Complex with the Fab Fragment of a Neutralizing Monoclonal Antibody

Phylogenetic analysis of Hungarian goose parvovirus isolates and vaccine strains

Visualization of the Externalized VP2 N Termini of Infectious Human Parvovirus B19

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