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PubMed1973

Thermal inactivation of Newcastle disease virus. I. Coupled inactivation rates of hemagglutinating and neuraminidase activities.

The thermal stability of Newcastle disease virus has been characterized in terms of the rate constants for inactivation of hemagglutinating activity (HA), neuraminidase activity (NA), and infectivity. Inactivation of HA results in the concomitant loss of NA. Infectivity, however, is much more thermolabile. Disintegration of the virus particle is not responsible for the identical rate constants for inactivation of HA and NA, nor is their parallel inactivation uncoupled in envelope fragments produced by pretreating the virus with phospholipase-C. The data indicate that a common envelope factor(s) can influence the thermal stability of both activities.

Animals↗
PubMed1969

Morphogenesis of Newcastle disease virus in chorioallantoic membrane.

Chick embryo chorioallantoic membrane, infected with the Blacksburg strain of Newcastle disease virus, was examined with an electron microscope to investigate the sequence of viral-induced host cell alterations. These were evident mostly in the endodermal epithelial cells lining the allantoic sac and were divided arbitrarily into three stages. Stage 1 was characterized by commencement of cell hypertrophy and hyperplasia and presence of fewer cytoplasmic inclusion bodies normally found in the cells; in stage 2, juxtanuclear nucleocapsid-glycogen aggregates appeared, and there were increased numbers of microvilli; stage 3 was characterized by increased cytoplasmic density and evidence of viral assembly and release. The morphological features of viral assembly and the virion are also described.

Animals↗
PubMedDate not supplied

Scanning electron microscopy of tracheal epithelium of chickens infected with velogenic viscerotropic Newcastle disease virus.

Ultrastructural changes in the tracheal epithelium of chickens infected intranasally with velogenic viscerotropic Newcastle disease virus were examined by scanning electron microscopy. Hypertrophy of the mucus-secreting, or goblet, cells was the first sign of change, followed by disoriented and deformed cilia, hemorrhage, and hyperplasia of goblet cells accompanied by an increase in mucus. By day 7 postinfection, there was a marked decrease in the number of ciliated cells. Submucosal glands and some collagen fibers were exposed to the surface, an indication of loss of the epithelial cells. Macrophages and cell debris were abundant, and hyperplasia of the basal cells was evident in the later stages of infection, probably in an attempt to regenerate the lost epithelium. However, all chickens died 10 days postinfection, before any further work could be done.

Animals↗
PubMed2004

Retrospective characterization of Newcastle Disease Virus Antrim '73 in relation to other epidemics, past and present.

In November 1973 Newcastle disease suddenly appeared in Northern Ireland, where the viscerotropic disease had not been seen in 3 1/2 years and the two Irelands had been regarded as largely disease free for 30 years. It was successfully controlled with only 36 confirmed affected layer flocks, plus 10 more slaughtered as 'dangerous contacts'. Contemporary investigations failed to reveal the source of the Irish epidemic. Using archival virus samples from most of the affected flocks, RT PCR was conducted with primers selected for all six NDV genes. Phylogenetic analyses of three genes, HN, M and F, confirmed vaccine as the cause of one of the outbreaks. The other six samples were identical and closely related to previous outbreaks in the United States and western Europe initiated by infected imported Latin American parrots. The probable cause of the epidemic followed from the importation from The Netherlands of bulk feed grains contaminated with infected pigeon faeces.

HN Protein↗
PubMed1984

Enhancement of Newcastle disease virus-induced fusion of mouse L cells by sodium vanadate.

Sodium vanadate enhanced Newcastle disease virus (NDV)-induced cell fusion in L cells, and there was a direct correlation between the degree of cell fusion and the dose of vanadate added. When anti-F protein of NDV monospecific antiserum was added to the culture fluid of L cells infected with NDV, the enhancement of cell fusion was suppressed. In contrast, neither anti-HN nor anti-M protein monospecific antiserum inhibited the enhancement. Incubation at low temperature (4 C) and addition of sodium azide to the culture fluid suppressed the enhancement. The suppression by azide was seen only when the drug was added within 5 min after the beginning of incubation of NDV-infected L cells with vanadate. On the other hand, incubation at low temperature inhibited the enhancement at any time during incubation with vanadate. Cytochalasin D also inhibited the enhancement if it was added at any time during incubation with vanadate.

Animals↗
PubMed1992

Effects of the components of Newcastle disease virus on the structural order of lipid assemblies.

The membrane M-protein of Newcastle disease virus is localized directly beneath the lipid bilayer. Although this protein is the major constituent of the virus, its structural relationship to the lipid or to the other viral component hemagglutinin-neuraminidase, the so called HN-glycoprotein, is still unknown. The effects of either M-protein alone or both M-protein and HN-glycoprotein on the lipid assemblies in reconstituted liposomes were determined by differential polarized phase fluorometry, steady-state fluorescence anisotropy and emission lifetime measurements. It is demonstrated that the degree of rotation of fluorophores in reconstituted liposomes is restricted by the molecular packing of lipids in the bilayer and this in turn can be correlated with the structural order of the lipids in the membrane. The experimental results show that the structural order parameters calculated from the fluorescence measurements are strongly influenced by the presence of both M-protein and HN-glycoprotein in the lipid assemblies.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1979

Molecular species of interferon induced in mouse L cells by Newcastle disease virus and polyriboinosinic-polyribocytidylic acid.

Interferons were stimulated in mouse L cells by Newcastle disease virus (NDV) or by polyriboinosinic-polyribocytidylic acid poly(rI).poly(rC). These were fractionated by sequential affinity chromatography on bovine plasma albumin (BPA)-Sepharose and on omega-carboxypentyl (CH)-Sepharose. Based on their interaction with CH-Sepharose, interferon induced by NDV was resolved into three major bands of activity (L/NDV-1,2,3) and poly(rI).poly(rC)-interferon into two (L/rI:rC-1,2). These interferon components were purified to a specific activity of 3 X 10(7) to 4 X 10(7) units/mg protein by antibody affinity chromatography and examined by electrophoresis in SDS-polyacrylamide gels. A total of five molecular species was thus identified for NDV-induced interferon and three for poly(rI).poly(rC) induced interferon, as summarized in Table 1. We conclude from our observations that mouse interferons can be produced by L cells in multiple forms with specific physiochemical properties and in proportions determined by the type of agent employed for induction.

Animals↗
PubMed1973

Precursor protein for Newcastle disease virus.

The course of viral protein synthesis during infection of chicken embryo fibroblasts with Newcastle disease virus (NDV) L. Kansas has been followed by using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Of the three major virion polypeptide molecular weight classes, I (78,400 daltons), II (53,500 daltons), and III (37,600 daltons), only II, having the same electrophoretic mobility as nucleocapsid polypeptide, appears to be the cleavage product of a precursor polypeptide PII (64,800 daltons) detected in NDV-infected cells after brief labeling with radioactive amino acids. Nucleocapsids were isolated from NDV-infected cells which had been pulse-labeled with radioactive amino acids or pulse-labeled and further incubated with unlabeled amino acids. Gel electrophoretic analysis of proteins derived from nucleocapsids showed that an increase in the period of incubation with unlabeled amino acids resulted in an increase in the amount of radioactivity in nucleocapsid protein. Polypeptide PII was not detected as a transient component of the isolated nucleocapsid fraction. These results are consistent with two interpretations. The product of PII cleavage is (i) nucleocapsid polypeptide, or (ii) a nonvirion or minor envelope polypeptide having the same electrophoretic mobility as nucleocapsid polypeptide.

Animals↗
PubMed1986

Topological and operational delineation of antigenic sites on the HN glycoprotein of Newcastle disease virus and their structural requirements.

Monoclonal antibodies to the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus have identified four antigenic sites on the glycoprotein, which are topologically and operationally discriminated from one another. To define the metabolisms and cellular compartments required for formation of the individual antigenic sites, a panel of monoclonal antibodies were examined for their reactivity with the nascent and variously processed forms of the antigen molecules in combination with the use of inhibitors of glycosylation (tunicamycin and N-methyl-1-deoxynojirimycin) and glycoprotein transport (carbonyl cyanide m-chlorophenylhydrazone and monensin). Reactivity was also examined with the antigen molecules deglycosylated by endoglycosidase F and with the antigen molecules reduced by 2-mercaptoethanol. The results taken together suggest that posttranslational organization of the glycoprotein is important for all four of the antigenic sites. At the same time, there appeared to be marked site-specific requirements with respect to glycosylation and disulfide bond formation. However, all of these metabolic requirements were found to be provided within the rough endoplasmic reticulum, and no further processing of the antigen molecules appeared to be necessary for the formation of any of the antigenic sites.

Amino Acid Sequence↗
PubMedDate not supplied

Newcastle disease virus passage in MDBK cells as an aid in detection of a virulent subpopulation.

Newcastle disease virus strains (NDV) La Sota, Texas GB (GB), and mixtures of the two strains were serially passaged in embryonated chicken eggs or the MDBK cell line, a more restrictive culture system than eggs for NDV. The two culture systems were compared by evaluating culture harvests for pathogenicity in inoculated chickens; the harvests were identified by hemagglutination-inhibition tests against monoclonal antibodies that can differentiate La Sota and GB cultures. Both viruses, inoculated alone or as mixtures, were propagated by passage in chicken eggs. La Sota strain failed to propagate by continuous passage in MDBK cells, and only GB was identified in culture harvests propagated in MDBK cells that had been inoculated with GB or mixtures of GB and La Sota. The results indicate that the MDBK cell line is a more selective substrate than chicken eggs and suggest that passage in MDBK cells may aid in selecting for more virulent subpopulations of NDV in a mixed culture. Other reference NDV strains, pigeon NDV isolates, and recent lentogenic NDV isolates from chickens were also passaged in MDBK cells; all strains except those that are classified as lentogens like La Sota could be serially propagated in MDBK cells.

Animals↗
PubMed2005

Tumor-targeted gene transfer in vivo via recombinant Newcastle disease virus modified by a bispecific fusion protein.

Previously we have demonstrated that a recombinant Newcastle disease virus (NDV) carrying the transgene EGFP can be retargeted to IL-2 receptor positive tumor cells by a bispecific fusion protein alphaHN-IL-2 in vitro. The purpose of the present study was to investigate the specificity and efficiency of gene delivery to tumor cells in vivo via this modified RNA virus. Prior ex vivo infection of murine lymphoma cells by the modified virus resulted in selective EGFP expression in IL-2R+ target tumor cells in vivo. Direct fluorescence microscopy and immunohistology showed viral replication in target positive tumor tissue resulting in much more EGFP expression than in target negative tumor tissue, 24 h after intratumoral injection of the alphaHN-IL-2 modified NDV. A quantitative real-time RT-PCR for EGFP mRNA. confirmed the selective gene expression in IL-2R+ tumor cells. Biodistribution studies showed that EGFP transgene delivery was reduced by 35-100% in liver, spleen, kidney, lung and thymus by the modified virus, while 98% of the transgene was delivered to IL-2R+ tumors. In conclusion, the modification of NDV by the bispecific protein does not compromise severely the efficiency of gene delivery into IL-2R-positive tumors, but greatly reduces viral gene expression in IL-2R-negative tumors and in normal tissues.

Animals↗
PubMed1998

Variability of antigenic epitopes of the fusion protein of Newcastle disease virus.

Using a panel of 10 monoclonal antibodies (Mab) against fusion (F) protein of Newcastle disease virus (NDV), strain Australia-Victoria, three non-overlapping antigenic sites (F1, F2 and F3) and one site partially overlapping with the sites F1 and F2 (F1.2) have been identified. The sites F2 and F3 are clusters that each include four antigenic epitopes. The antigenic stability of the above epitopes was estimated by comparison of the binding capacity of the corresponding Mabs towards 63 NDV strains isolated in different years and places from various avian species. The results demonstrated high variability of the site F1.2 and of all the four epitopes of the site F2. At the same time, the only epitope of the site F1 can be defined as highly conservative: the corresponding Mab gave positive binding with 60 from 63 NDV strains, one from the four epitopes pertaining to site F3 was the most conservative--the corresponding Mab reacted with all the 63 strains used in the studies, while the other three Mabs showed rather low stability--the corresponding Mabs reacted with 34-39 NDV strains. Thus, as opposed to the published data asserting antigenic stability of the F protein contrary to the high variability of the haemagglutinin-neuraminidase (HN) protein, our results have revealed a number of variable epitopes on the F protein. This demonstrates an evolutionary changeability of the F protein, which is of importance from the theoretical (viral antigenic evolution) as well as practical point of view.

Antibodies, Monoclonal↗
PubMed2004

Nucleotide and predicted amino acid sequence analysis of the fusion protein and hemagglutinin-neuraminidase protein genes among Newcastle disease virus isolates. Phylogenetic relationships among the Paramyxovirinae based on attachment glycoprotein sequences.

Highly virulent Newcastle disease virus (NDV) isolates are List A pathogens for commercial poultry, and reports of their isolation among member nations must be made to the Office of International Epizootes (OIE). The virus is classified as a member of the order Mononegavirales in the family Paramyxoviridae of the subfamily Paramyxovirinae. Two interactive surface glycoproteins, the fusion (F) and hemagglutinin-neuraminidase (HN) proteins, play essential roles in NDV attachment and fusion of cells during infection. Antibodies to the F or HN proteins are capable of virus neutralization; however, no full-length sequences are available for these genes from recently obtained virulent isolates. Therefore, nucleotide and predicted amino acid sequences of the F and HN protein genes from 16 NDV isolates representing highly virulent viruses from worldwide sources were obtained for comparison to older virulent isolates and vaccine strains. The F protein amino acid sequence was relatively conserved among isolates maintaining potential glycosylation sites and C residues for disulfide bonds. A dibasic amino acid motif was present at the cleavage site among more virulent isolates, while the low virulence viruses did not have this sequence. However, a Eurasian collared dove virus had a K114Q substitution at the F cleavage site unique among NDV isolates. The HN protein among NDV isolates maintained predicted catalytic and active site residues necessary for neuraminidase activity and hemagglutination. Length of the HN for the Eurasian collared dove isolate and a previously reported heat resistant virulent isolate were longer relative to other more recent virulent isolates. Phylogenetically NDV isolates separated into four groups with more recent virulent isolates forming a diverse branch, while all the avian paramyxoviruses formed their own clade distinct from other members of the Paramyxoviridae.

Amino Acid Sequence↗
PubMed2003

Role of the cytoplasmic domain of the Newcastle disease virus fusion protein in association with lipid rafts.

To explore the association of the Newcastle disease virus (NDV) fusion (F) protein with cholesterol-rich membrane domains, its localization in detergent-resistant membranes (DRMs) in transfected cells was characterized. After solubilization of cells expressing the F protein with 1% Triton X-100 at 4 degrees C, ca. 40% of total, cell-associated F protein fractionated with classical DRMs with densities of 1.07 to l.14 as defined by flotation into sucrose density gradients. Association of the F protein with this cell fraction was unaffected by the cleavage of F(0) to F(1) and F(2) or by coexpression of the NDV attachment protein, the hemagglutinin-neuraminidase protein (HN). Furthermore, elimination by mutation, of potential palmitate addition sites in and near the F-protein transmembrane domain had no effect on F-protein association with DRMs. Rather, specific deletions of the cytoplasmic domain of the F protein eliminated association with classical DRMs. Comparisons of deletions that affected fusion activity of the protein and deletions that affected DRM association suggested that there is no direct link between the cell-cell fusion activity of the F protein and DRM association. Furthermore, depletion of cholesterol from cells expressing F and HN protein, while eliminating DRM association, had no effect on the ability of these cells to fuse with avian red blood cells. These results suggest that specific localization of the F protein in cholesterol-rich membrane domains is not required for cell-to-cell fusion. Paramyxovirus F-protein cytoplasmic domains have been implicated in virus assembly. The results presented here raise the possibility that the cytoplasmic domain is important in virus assembly at least in part because it directs the protein to cholesterol-rich membrane domains.

Amino Acid Sequence↗