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PubMedDate not supplied

Pathogenicity and cross-protection of pigeon paramyxovirus-1 and Newcastle disease virus in young chickens.

Avian paramyxovirus-1 (PMV-1) isolates from Delaware racing pigeons were compared with Newcastle disease virus (NDV) in pathogenicity and cross-protection studies in young chickens. The pathogenicity of pigeon PMV-1 isolates was more closely related to mesogenic (Roakin) NDV than to lentogenic (La Sota) or velogenic (Texas GB) NDV strains. Pigeon PMV-1 produced 100% mortality in 1-day-old NDV-susceptible chickens following intratracheal and intracerebral inoculation. Laboratory tests often used in conjunction with chicken pathogenicity procedures for patho-typing NDV gave conflicting results. Pigeon PMV-1 isolates produced large clear plaques (up to 3.5 mm) in chicken-embryo-fibroblast cultures. Chicken embryo mean death times were considerably greater for pigeon PMV-1 (88 and 109 hr) than for Roakin (66 hr) and Texas GB (48 hr). B1 strain NDV and pigeon PMV-1 produced complete cross-protection in challenge studies in chickens. Extensive cross-reaction between pigeon PMV-1 and NDV occurred in hemagglutination-inhibition tests using polyclonal antisera. However, pigeon PMV-1 and NDV were readily distinguishable using a NDV monoclonal antibody, 2F12.

Animals↗
PubMed2003

[The effect of newcastle disease virus on the biological behavior of tumor cells].

AIM: To investigate the anti-tumor effect of newcastle disease virus (NDV). METHODS: Plaque formation test was used to investigate the effect of NDV on chicken embryofibroblasts(CEF). Cell suppression test, agarose gel electrophoresis, cytoskeleton staining, fluorescence staining, TUNEL staining, and sialic acid content determination were used to observe the influence of NDV on several human tumor cells. RESULTS: The Plaque formation was observed in chicken embryo fibroblasts.NDV could lead to the apparent cytopathy of BHK, Hela and Hep-2 tumor cells, but has no apparent effect on Wish cells. The strong suppressive effect of NDV on the growth of these tumor cells was found without dose dependence. The optimal dose of NDV could induce the death of tumor cells which was mainly apoptosis, as showed by the classical DNA ladder in DNA gel electrophoresis. NDV also resulted in the changes of cytoskeleton and decreased the level of sialic acid contents on tumor cells. CONCLUSION: NDV may be a potential anti-tumor agent.

Animals↗
PubMedDate not supplied

Heat inactivation of the neuraminidase and haemagglutinin estimated in the agglutination-separation reactions using red blood cells sensitized with Newcastle disease virus.

The agglutination-separation (AS) reactions estimate the effects of heat on the release of altered Newcastle disease virus (NDV) and HN glycoprotein spikes from red blood cells (RBC) sensitized with NDV (SRBC), the inactivations of the neuraminidase (NA), then the haemagglutinin (HA) in a direct assay. Heating SRBC for 1.5 min at 56 degrees C inactivated the NA by 50%; after 4.5 min no separation occurred indicating 100% inactivation of the NA. Heating a suspension of NDV for 78 min inactivated the NA 50% as assayed by cleavage of fetuin. Comparatively, the AS test was up to 52-fold (78 min/1.5 min = 52) more efficient in detecting NA inactivation than was the basic reference test where cleavage of fetuin was assayed. The HA was 50% inactivated after 18 min of heating and 100% inactivated after 36 min as no agglutination was seen. Free HA on SRBC was agglutinated by and thus was titrated with the sialic acid on NRBC. The large area of RBC increased the efficiency of the AS test when compared with tests using suspensions of NDV. At 51-60 degrees C all NA and HA inactivations were sequential, and invariably the NA was more heat labile than the HA. The release of altered NDV and HN spikes was inhibited with mild heat although the separation of SRBC and NRBC continued. Biological purifications showed that the heat stability of the HA and the lability of the NA were genetically stable.

Animals↗
PubMed1987

Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus.

The nucleotide sequence of the mRNA encoding the fusion (F0) protein of a virulent strain of Newcastle disease virus was determined. A single open reading frame in the sequence encodes a protein of 553 amino acids with a calculated molecular weight of 59058. The amino acid sequence predicted several structural features involving the fusion-inducing hydrophobic stretch (residues 117-142) and the cleavage-activation site (residues 112-116) to generate the disulfide-linked F1 and F2 subunits. The cleavage-activation site as well as a part of the fusion-inducing sequence were compared among a series of virulent and avirulent strains by the chain-termination method using a synthetic oligonucleotide primer. It was found that without exception, the cleavage-activation site of virulent strains consisted of two dibasic residues with an intervening glutamine, Arg-Arg-Gln-Arg-Arg, whereas the corresponding region of avirulent strains was made of a sequence with single basic residues scattered among uncharged residues, Gly-LysArg-Gln-GlySer-Arg. On the basis of these observations and the previous results showing a strict correlation between the pathogenicity and the cleavability of the fusion protein of NDV (Y. Nagai, H-D. Klenk, and R. Rott, Virology, 72, 494-508, 1976), we propose the importance of the dibasic residues for efficient proteolytic activation of the fusion protein and for the pantropic property of NDV. Some strains were found to have Leu-Ile-Gly as the N-terminus of F1, whereas others contained Phe-Ile-Gly, indicating that Phe-X-Gly is not always conserved at F1 N-terminus of paramyxovirus.

Amino Acid Sequence↗
PubMed2002

Newcastle disease virus HN protein alters the conformation of the F protein at cell surfaces.

Conformational changes in the Newcastle disease virus (NDV) fusion (F) protein during activation of fusion and the role of HN protein in these changes were characterized with a polyclonal antibody. This antibody was raised against a peptide with the sequence of the amino-terminal half of the F protein HR1 domain. This antibody immunoprecipitated both F(0) and F(1) forms of the fusion protein from infected and transfected cell extracts solubilized with detergent, and precipitation was unaffected by expression of the HN protein. In marked contrast, this antibody detected significant conformational differences in the F protein at cell surfaces, differences that depended upon HN protein expression. The antibody minimally detected the F protein, either cleaved or uncleaved, in the absence of HN protein expression. However, when coexpressed with HN protein, an uncleaved mutant F protein bound the anti-HR1 antibody, and this binding depended upon the coexpression of specifically the NDV HN protein. When the cleaved wild-type F protein was coexpressed with HN protein, the F protein bound anti-HR1 antibody poorly although significantly more than F protein expressed alone. Anti-HR1 antibody inhibited the fusion of R18 (octadecyl rhodamine B chloride)-labeled red blood cells to syncytia expressing HN and wild-type F proteins. This inhibition showed that fusion-competent F proteins present on surfaces of syncytia were capable of binding anti-HR1. Furthermore, only antibody which was added prior to red blood cell binding could inhibit fusion. These results suggest that the conformation of uncleaved cell surface F protein is affected by HN protein expression. Furthermore, the cleaved F protein, when coexpressed with HN protein and in a prefusion conformation, can bind anti-HR1 antibody, and the anti-HR1-accessible conformation exists prior to HN protein attachment to receptors on red blood cells.

Amino Acid Sequence↗
PubMed1989

Effect of amino acid substitutions on glycosylation of the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus strain Beaudette C.

The nucleotide sequences of two monoclonal antibody-resistant mutant viruses predict changes from the wild-type in the number of potential glycosylation (Asn-X-Thr/Ser) in the mutant haemagglutinin-neuraminidase (HN) glycoproteins of the Beaudette C strain of Newcastle disease virus. The HN glycoproteins of these mutants, F5 and Z18, migrate either slower (F5) or faster (Z18) than that of the wild-type in SDS-PAGE. HN proteins synthesized in chick embryo fibroblasts following infection by either mutant or wild-type virus in the presence of tunicamycin (an inhibitor of glycosylation), comigrate on SDS-PAGE. These results confirm that the HN protein of the mutant virus, F5, has gained a glycosylation site at Asn(323)-Ser-Ser and that the conserved potential glycosylation site at Asn(481)-His-Thr is indeed glycosylated in the HN protein of the wild-type Beaudette C strain of Newcastle disease virus but is lost in that of the mutant virus, Z18.

Amino Acid Sequence↗
PubMedDate not supplied

[Discovery of natural foci of Newcastle disease virus in the USSR].

In examination of colonial birds in the Volga delta in the Astrakhan region (188 bioassays from 229 birds) and in the Komandorskie Islands of the Kamchatka region (244 bioassays from 208 birds) in 1974, 15 strains of Newcastle disease virus (NDV) were isolated (8 strains from 7 birds and 7 strains from 12 birds, respectively). The strains were isolated from Egretta alba and Ardea cinerea, and Phalacracorax carbo in the Astrakhan region and from Lunda cirrhata and Uria aalge in the Komandorskie Islands. The isolates were obtained from tracheal and cloacal washings and from pools of viscera. These data are the first evidence of the existence of Newcastle disease virus foci in the USSR.

Animals↗
PubMed1990

Newcastle disease virus fusion protein expressed in a fowlpox virus recombinant confers protection in chickens.

A cDNA copy of the RNA encoding the fusion (F) protein of Newcastle disease virus (NDV) strain Texas, a velogenic strain of NDV, was obtained and the sequence was determined. The 1,792-base-pair sequence encodes a protein of 553 amino acids which has essential features previously established for the F protein of virulent NDV strains. These include the presence of three strongly hydrophobic regions and pairs of dibasic amino acids in the pentapeptide Arg-Arg-Gln-Arg-Arg preceding the putative cleavage site. When inserted into a fowlpox virus vector, a glycosylated protein was expressed and presented on the surface of infected chicken embryo fibroblast cells. The F protein expressed by the recombinant fowlpox virus was cleaved into two polypeptides. When inoculated into susceptible birds by a variety of routes, an immunological response was induced. Ocular or oral administration of the recombinant fowlpox virus gave partial protection, whereas both intramuscular and wing-web routes of inoculation gave complete protection after a single inoculation.

Amino Acid Sequence↗
PubMed1986

Nucleotide sequence of the gene encoding the fusion glycoprotein of Newcastle disease virus.

The nucleotide sequence of the gene encoding the fusion (F) glycoprotein of the Beaudette C strain of Newcastle disease virus (NDV) has been determined from cDNA clones obtained from virion RNA. The gene is 1792 nucleotides long, including mRNA start and polyadenylation signals typical of paramyxoviruses. The single open reading frame encodes a polypeptide of 553 amino acids, with a predicted molecular weight of 59042. The F polypeptide has three regions of high hydrophobicity: an N-terminal signal peptide, the N terminus of F1 (known from protein sequencing) and a C-terminal membrane-spanning region by which the F glycoprotein is anchored to the membrane. The cleavage site of F0 is located in a highly basic region of the F polypeptide. Five potential asparagine-linked glycosylation sites are present in the amino acid sequence, of which one is in F2 and the others in F1. Comparison of the NDV F amino acid sequence to those from other paramyxoviruses reveals homology to Sendai virus, simian virus 5 and human respiratory syncytial virus. There is also limited homology between the N terminus of F1 of NDV and the N termini of HA2 of influenza viruses. Post-translational modifications of the NDV F polypeptide are discussed in the light of information provided by the amino acid sequence.

Amino Acid Sequence↗
PubMed1972

Temperature-sensitive mutants isolated from L cells persistently infected with Newcastle disease virus.

Virus mutants (NDV(pi)) isolated from L cells persistently infected with the Herts strain of Newcastle disease virus have been previously reported by this laboratory to differ from the wild-type virus (NDV(o)) in several physical and biological properties. It has now been determined that, in addition to these differences, the NDV(pi) mutants are also spontaneously selected temperature-sensitive mutants. The temperature sensitivity of 10 NDV(pi) clones was confirmed by temperature inhibition, plaquing efficiency, and single-cycle yield experiments. The cut-off temperature, at which more than 90% of virus replication is inhibited was between 41 and 42 C. All 10 NDV(pi) clones were also found to be defective in virus-specific ribonucleic acid (RNA) synthesis in infected chick embryo cells at 42 C and are tentatively classified as RNA(-). The possible relationships of the temperature sensitivity, the other NDV(pi) properties, and the maintenance of the persistently infected state are discussed.

Animals↗
PubMed1985

Infection of mice with Newcastle disease virus inhibits the T suppressor afferent cell circuit which regulates contact sensitivity to picryl chloride.

The interaction between Newcastle disease virus (NDV) and the suppressor cell circuit which regulates the induction phase of contact sensitivity reaction to picryl chloride (Pcl) was investigated. NDV infection impairs the activity of the T suppressor afferent cells (Ts-aff) which inhibit DNA synthesis in the draining lymph nodes of mice specifically sensitized with Pcl and the development of contact sensitivity. The inhibitory effect of NDV was evident when the virus was administered up to 2 days before or at the same time as the injection of picrylsulfonic acid; this effect required infectious virus, as NDV inactivated by ultraviolet irradiation failed to inhibit Ts-aff activity. Taken together with the previous finding that the T suppressor efferent cell is unaffected by NDV, the present results support the view that contact sensitivity reaction to picryl chloride is regulated by two distinct T-suppressor-cell circuits.

Animals↗
PubMed1985

Conformational changes in Newcastle disease virus fusion glycoprotein during intracellular transport.

The migration on polyacrylamide gels of nascent (pulse-labeled) and more processed (pulse-labeled and then chased) forms of nonreduced Newcastle disease virus fusion glycoprotein were compared. Results are presented which demonstrate that pulse-labeled fusion protein, which has an apparent molecular weight of 66,000 under reducing conditions (Collins et al., J. Virol. 28: 324-336), migrated with an apparent molecular weight of 57,000 under nonreducing conditions. This form of the Newcastle disease virus fusion protein has not been previously detected. This result suggests that the nascent fusion protein has extensive intramolecular disulfide bonds which, if intact, significantly alter the migration of the protein on gels. Furthermore, upon a nonradioactive chase, the migration of the fusion protein in polyacrylamide gels changed from the 57,000-molecular-weight species to the previously characterized nonreduced form of the fusion protein (molecular weight, 64,000). Evidence is presented that this change in migration on polyacrylamide gels is due to a conformational change in the molecule which is likely due to the disruption of some intramolecular disulfide bonds: Cleveland peptide analysis of the pulse-labeled nonreduced fusion protein (molecular weight, 57,000) yielded a pattern of polypeptides quite different from that obtained from the more processed form of the fusion protein (molecular weight, 64,000). However, the pattern of polypeptides obtained from the nonreduced 64,000-molecular-weight species was quite similar to that obtained from the fully reduced nascent protein (molecular weight, 66,000). This conformational change occurred before cleavage of the molecule. To determine the cell compartment in which the conformational change occurs, use was made of inhibitors which block glycoprotein migration at specific points. Monensin allowed the appearance of the 64,000-molecular-weight form of the fusion protein, whereas carboxyl cyanide m-chlorophenylhydrazine blocked the appearance of the 64,000-molecular-weight form of the fusion protein. Thus, the fusion protein undergoes a conformational change as it moves between the rough endoplasmic reticulum and the medial Golgi membranes.

Animals↗
PubMed2003

Identification of a mutation in editing of defective Newcastle disease virus recombinants that modulates P-gene mRNA editing and restores virus replication and pathogenicity in chicken embryos.

Editing of P-gene mRNA of Newcastle disease virus (NDV) enables the formation of two additional proteins (V and W) by inserting one or two nontemplated G residues at a conserved editing site (5'-AAAAAGGG). The V protein of NDV plays an important role in virus replication and is also a virulence factor presumably due to its ability to counteract the antiviral effects of interferon. A recombinant virus possessing a nucleotide substitution within the A-stretch (5'-AAgAAGGG) produced 20-fold-less V protein and, in consequence, was impaired in replication capacity and completely attenuated in pathogenicity for chicken embryos. However, in a total of seven serial passages, restoration of replication and pathogenic capacity in 9- to 11-day-old chicken embryos was noticed. Determining the sequence around the editing site of the virus at passage 7 revealed a C-to-U mutation at the second nucleotide immediately upstream of the 5'-A(5) stretch (5'-GuUAAgAAGGG). The V mRNA increased from an undetectable level at passage 5 to ca. 1 and 5% at passages 6 and 7, respectively. In addition, similar defects in another mutant possessing a different substitution mutation (5'-AAAcAGGG) were restored in an identical manner within a total of seven serial passages. Introduction of the above C-to-U mutation into the parent virus (5'-GuUAAAAAGGG) altered the frequency of P, V, and W mRNAs from 68, 28, and 4% to 15, 44, and 41%, respectively, demonstrating that the U at this position is a key determinant in modulating P-gene mRNA editing. The results indicate that this second-site mutation is required to compensate for the drop in edited mRNAs and consequently to restore the replication capacity, as well as the pathogenic potential, of editing-defective NDV recombinants.

Amino Acid Sequence↗
PubMed1993

[Detection of antibodies against Newcastle disease virus in wild birds].

262 samples from wild birds of 26 species were examined for antibodies against the Newcastle Disease virus (NDV). By using the haemagglutination inhibition test (HI) 22 serum samples showing positive antibody titers could be detected. The epidemiology and the significance of ND for wild birds and waterfowl in farms is discussed.

Animals↗
PubMed1987

Detection of polycistronic transcripts in Newcastle disease virus infected cells and identification of their sequence content.

The synthesis of six to seven polycistronic transcripts of Newcastle disease virus (NDV) in BHK cells was detected by Northern hybridization using cDNA clones generated by reverse transcription of five NDV mRNAs. Within the molecular weight range resolved by the gel electrophoresis system employed, four of the transcripts were suggested to be distronic, containing sequences of two genes, NP-P, P-M, M-F0 and F0-HN, respectively. In addition, tricistronic molecules of M-F0-HN and possibly of NP-P-M as well as P-M-F0 appeared to develop, although they were very low in amount. These data suggest a gene order of NP-P-M-F0-HN on the NDV genome. The polycistronic as well as monocistronic transcripts were generated with an almost constant proportion in amount throughout the virus replication. Further, at least several of them were also generated under the conditions where only the primary transcription was allowed by inhibiting de novo protein synthesis. Therefore, it appears likely that there is no distinct temporal control in NDV genome expression.

Amino Acid Sequence↗