Search results for "Canine parvovirus"

Parvovirus capsid disorders cholesterol-rich membranes.

2008

In this study canine parvovirus, CPV, was found to induce disorder in DPPC:cholesterol membranes in acidic conditions. This acidicity-induced fluidizing effect is suggested to originate from the N-terminus of the viral capsid protein VP1. In accordance with the model membrane studies, a fluidizing effect was seen also in the endosomal membranes during CPV infection implying an important functional role of the fluidization in the endocytic entry of the virus.

Sphingomyelin induces structural alteration in canine parvovirus capsid.

2007

One of the essential steps in canine parvovirus (CPV) infection, the release from endosomal vesicles, is dominated by interactions between the virus capsid and the endosomal membranes. In this study, the effect of sphingomyelin and phosphatidyl serine on canine parvovirus capsid and on the phospholipase A(2) (PLA(2)) activity of CPV VP1 unique N-terminus was analyzed. Accordingly, a significant (P< or =0.05) shift of tryptophan fluorescence emission peak was detected at pH 5.5 in the presence of sphingomyelin, whereas at pH 7.4 a similar but minor shift was observed. This effect may relate to the exposure of VP1 N-terminus in acidic pH as well as to interactions between sphingomyelin and CP…

Late steps of parvoviral infection induce changes in cell morphology.

2008

Previously, virus-induced non-filopodial extensions have not been encountered in connection with viral infections. Here, we report emergence of long extensions protruding from Norden laboratory feline kidney (NLFK) and A72 (canine fibroma) cells infected with canine parvovirus for 72 h. These extensions significantly differ in length and number from those appearing in control cells. The most striking feature in the extensions is the length, reaching up to 130 microm, almost twice the average length of a healthy NLFK cell. In A72 cells, the extensions were even longer, up to 200 microm. The results presented here also suggest that the events leading to the growth of these extensions start ea…

Diagnosi di enteriti infettive di origine virale nel cane

2013

Canine Viral Enteritis are widespread in farms and kennels. Responsible viruses are Parvovirus (CPV), Coronavirus (CCoV), Rotavirus (CRV) and Distemper Virus (CDV). Aim of this study was to assess their prevalence in Sicily and to characterize the strains isolated during 2009-2012. For this purpose, samples (stools, rectal swabs, intestine, liver, spleen, heart, lung, brain) collected from dogs were analyzed by PCR, RT-PCR and Real Time RT-PCR. Positive samples were processed for virus isolation on cell lines. Viruses isolated were analyzed by RFLP and sequencing for molecular characterization. Results show an high prevalence of CPV infection in dogs, followed by CCoV, CRV and CDV. CPV prev…

Intracellular route of canine parvovirus entry.

1998

ABSTRACT 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 membr…

G2/M checkpoint regulation and apoptosis facilitate the nuclear egress of parvoviral capsids

2022

The nuclear export factor CRM1-mediated pathway is known to be important for the nuclear egress of progeny parvovirus capsids in the host cells with virus-mediated cell cycle arrest at G2/M. However, it is still unclear whether this is the only pathway by which capsids exit the nucleus. Our studies show that the nuclear egress of DNA-containing full canine parvovirus. capsids was reduced but not fully inhibited when CRM1-mediated nuclear export was prevented by leptomycin B. This suggests that canine parvovirus capsids might use additional routes for nuclear escape. This hypothesis was further supported by our findings that nuclear envelope (NE) permeability was increased at the late stages…

Promoter-Targeted Histone Acetylation of Chromatinized Parvoviral Genome Is Essential for the Progress of Infection

2015

ABSTRACT The association of host histones with parvoviral DNA is poorly understood. We analyzed the chromatinization and histone acetylation of canine parvovirus DNA during infection by confocal imaging and in situ proximity ligation assay combined with chromatin immunoprecipitation and high-throughput sequencing. We found that during late infection, parvovirus replication bodies were rich in histones bearing modifications characteristic of transcriptionally active chromatin, i.e., histone H3 lysine 27 acetylation (H3K27ac). H3K27ac, in particular, was located in close proximity to the viral DNA-binding protein NS1. Importantly, our results show for the first time that in the chromatinized …

Endosomal escape of canine parvovirus is assisted by membrane fluidization

2007

Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells

2004

AbstractA mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protei…

Assembly of fluorescent chimeric virus-like particles of canine parvovirus in insect cells

2004

Canine parvovirus (CPV) is a small non-enveloped ssDNA virus composed of the viral proteins VP1, VP2, and VP3 with a T=1 icosahedral symmetry. VP2 is nested in VP1 and the two proteins are produced by differential splicing of a primary transcript of the right ORF of the viral genome. The VP2 protein can be further proteolytically cleaved to form VP3. Previous studies have shown that VP1 and VP3 are unnecessary for capsid formation and consequently, that VP2 alone is sufficient for assembly. We have hypothesized that insertion of the enhanced green fluorescent protein (EGFP) at the N-terminus of VP2 could be carried out without altering assembly. To investigate the possibility to develop flu…