Infectious process of the parvovirus H-1: correlation of protein content, particle density, and viral infectivity

Paradiso, Peter R.

doi:10.1128/jvi.39.3.800-807.1981

Cited by 64 publications

(30 citation statements)

References 14 publications

(22 reference statements)

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“…The spatial orientation of the amino terminus of VP2 in recombinant capsids expressed in the baculovirus system (12,33) is still to be investigated. Also, there is evidence that for VP2 to be infective, about 20 amino acids have to be cleaved away from the amino terminus of VP2, resulting in the capsid protein VP3 (7,8,17). The effect of neutralizing antibodies which bind to the amino terminus of VP2 of CPV could very well be hindrance of a proteolytic cleavage that unmasks a viral domain essential for infection.…”

Section: Discussionmentioning

confidence: 99%

B-cell epitopes of canine parvovirus: distribution on the primary structure and exposure on the viral surface

Langeveld

Casal

Vela

et al. 1993

J Virol

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Ten antigenic sites on canine parvovirus (CPV) were mapped with a complete set of overlapping nonapeptides of the capsid proteins VP1 and VP2: five of these sites were recognized by sera from CPV-infected dogs, three were recognized by a rabbit anti-CPV antiserum, and two were recognized by murine monoclonal anti-CPV antibodies. A region covering the first 21 amino-terminal amino acid residues of VP2 was recognized by three sera from infected dogs, one neutralizing rabbit antiserum, and one neutralizing murine monoclonal antibody. Immunoabsorption experiments with full virions indicated that at least 6 of the 10 antigenic sites are located on the surface. Of these six, three sites occur in the amino terminus of VP2. When superimposed on the three-dimensional structure of canine parvovirus (J.

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Section: Discussionmentioning

confidence: 99%

B-cell epitopes of canine parvovirus: distribution on the primary structure and exposure on the viral surface

Langeveld

Casal

Vela

et al. 1993

J Virol

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“…The virus was prepared according to the procedure of Paradiso (1981) and modified as in Luo, Tsao, Rossmann, Basak & Compans (1988) and Tsao et al (1991). Solution scattering patterns were collected by methods similar to those used by Schmidt, Johnson & Phillips (1983), except that the sample concentration was about 10 mg m1-1 rather than 150 mg m1-1 because of the difficulty of propagating sufficient virus in mammalian cell lines.…”

Section: Experimental Methodsmentioning

confidence: 99%

Ab initiophase determination for spherical viruses: parameter determination for spherical-shell models

Chapman¹,

Tsao²,

Rossmann³

1992

Acta Cryst Sect A

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The structure determination of canine parvovirus depended on the extension of phases calculated initially from a spherical-shell model [Tsao, Chapman, Wu, Agbandje, Keller & Rossmann (1992). Acta Cryst. B48, 75-88]. Such ab initio phasing holds the promise of obviating initial experimental phasing by isomorphous or molecular replacement, thereby expediting the structure determinations of spherical virus capsids. In this paper, it is shown how parameters such as radii, DNA density and particle positions may be determined and refined from diffraction data with sufficient precision to start phase extension from 20 A resolution for a virus of approximately 122 A radius.

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“…CPV was propagated in canine fibroma cell line A72 (6) and grown (for 72 h at 37°C in 5% CO 2 ) in Dulbecco's mod-ified Eagle's medium supplemented with 10% fetal calf serum (Gibco, Paisley, United Kingdom). CPV was purified according a modification of the procedure of Paradiso (28,29). The ratio of infectious to empty viral particles was estimated to be 40:60 from the sedimentation profile of hemagglutinating CPV in CsCl gradients (1).…”

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confidence: 99%

Intracellular Route of Canine Parvovirus Entry

Vihinen‐Ranta

Kalela

Mäkinen

et al. 1998

J Virol

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The present study was designed to investigate the endocytic pathway involved in canine parvovirus (CPV) infection. Reduced temperature (18°C) or the microtubule-depolymerizing drug nocodazole was found to inhibit productive infection of canine A72 cells by CPV and caused CPV to be retained in cytoplasmic vesicles as indicated by immunofluorescence microscopy. Consistent with previously published results, these data indicate that CPV enters a host cell via an endocytic route and further suggest that microtubule-dependent delivery of CPV to late endosomes is required for productive infection. Cytoplasmic microinjection of CPV particles was used to circumvent the endocytosis and membrane fusion steps in the entry process. Microinjection experiments showed that CPV particles which were injected directly into the cytoplasm, thus avoiding the endocytic pathway, were unable to initiate progeny virus production. CPV treated at pH 5.0 prior to microinjection was unable to initiate virus production, showing that factors of the endocytic route other than low pH are necessary for the initiation of infection by CPV.

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Infectious process of the parvovirus H-1: correlation of protein content, particle density, and viral infectivity

Cited by 64 publications

References 14 publications

B-cell epitopes of canine parvovirus: distribution on the primary structure and exposure on the viral surface

B-cell epitopes of canine parvovirus: distribution on the primary structure and exposure on the viral surface

Ab initiophase determination for spherical viruses: parameter determination for spherical-shell models

Intracellular Route of Canine Parvovirus Entry

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