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PubMed2001

Cloning, expression, and crystallization of the fusion protein of Newcastle disease virus.

We have recently reported the X-ray crystal structure of a fragment of the fusion protein (F) of Newcastle disease virus (NDV). This work describes the methodology involved in the production and crystallization of that protein in recombinant form. The full-length cDNA of NDV-F was cloned and the ectodomain expressed in both CHO-K1 and Lec-3.2.8.1 cells. The recombinant protein, secreted as a single-chain polypeptide F0', was purified using a c-myc antibody affinity column followed by gel filtration chromatography. Electron microscopic imaging showed the F0' product to consist of unaggregated club-shaped particles. Trypsin treatment of F0' could be used to produce disulfide-linked F2 and F1' chains. However, imaging revealed extensive rosette-like aggregation of the trypsin-treated material, indicative of a conformational change. Only the non-trypsin-treated product was thus suitable for crystallization and two crystal forms were obtained, diffracting to ca. 3.5 and 4.0 A, respectively. Both crystal forms were used in the structure determination.

Amino Acid Sequence↗
PubMed1996

Role of cotranslational disulfide bond formation in the folding of the hemagglutinin-neuraminidase protein of Newcastle disease virus.

The role of cotranslational disulfide bond formation in the folding pathway of the hemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus was explored. Electrophoresis of pulse-labeled HN protein in the presence or absence of reducing agent showed that, characteristic of many glycoproteins, the nascent HN protein contains intramolecular disulfide bonds. As reported by Braakman et al. (EMBO J. 11, 1717-1722, 1992), incubation of cells in dithiothreitol (DTT) blocked the formation of these bonds. Removal of DTT after a pulse-label allowed for the subsequent formation of intramolecular disulfide bonds and folding of the molecule as assayed by the appearance of conformationally sensitive antigenic sites and by the formation of disulfide-linked dimers. However, the t1/2 for the formation of a conformationally sensitive antigenic site after synthesis in the presence of DTT was over twice that of the control. Furthermore, the order of appearance of the antigenic sites was different from the control, suggesting that inhibition of cotranslational disulfide bond formation altered the folding pathway of the protein. Similar results were obtained in a cell-free system containing membranes. The HN protein forced to form intramolecular disulfide bonds posttranslationally had no detectable neuraminidase or cell attachment activity, suggesting that the protein had an abnormal conformation.

Animals↗
PubMed1974

Antigenic relationships among Newcastle disease virus mutants obtained from laboratory strains and from recent California isolates.

The antigenic relationship between pairs of plaque mutants of Newcastle disease virus (NDV) derived from laboratory strains and from isolates from the 1971-72 California epizootic were examined by kinetic neutralization test. Comparing four sets of mutants from laboratory strains by both kinetic neutralization and hemagglutination inhibition tests, a similarity was found in the antigenic relationship expressed as an r value with both tests. However, kinetic neutralization was the more precise as well as sensitive assay. Antigenic diversity was greatest between pairs of mutants from different strains, but distinctions could also be made between mutants from the same strains such as Herts-L and Herts-S with an r value of 36%. Examination of mutants from the California epizootic isolated from separate locations and at different times showed antigenic divergence which was greatest between two red-plaque mutants with an r value of 39%. Antigenic distinctions were found between a red- and clear-plaque mutant obtained from isolates taken from brain and tracheal swabs of one infected chicken. In addition to antigenic divergence found between pairs of some mutants, two of the clear-plaque mutants reacted more avidly with antibody than did the corresponding red-plaque partner. Thus, both differences in antigenicity and avidity can be found among these NDV mutants. The antigenic variation found among these mutants is similar to that found within a serotype. This would imply that at the present NDV is a single serological type.

Animals↗
PubMed1984

Mutation in the matrix protein of Newcastle disease virus can result in decreased fusion glycoprotein incorporation into particles and decreased infectivity.

Virus particles produced in eggs by the group D ts mutants of Newcastle disease virus at permissive temperature display low infectious and hemolytic activities (M.E. Peeples and M. A. Bratt , J. Virol. 42:440-446, 1982). These lower activities correlate with a decreased incorporation of F1+2 (fusion glycoprotein) into virus particles, compared with that for wild type. The incorporation of F1+2 into virus particles of the group D mutants is also lower than that for wild type when grown in chicken embryo cells in culture at either permissive or nonpermissive temperature. The infectivity of virions from these mutants correlates with the amounts of F1+2 in the virus particles, below a certain concentration, indicating that the quantity of F1+2 in virus particles is a determining factor in the infectivity of those particles. In addition, one of these mutants, D1, produces an M (matrix protein) which migrates at a faster rate in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Three of four revertants of D1 have coreverted to wild-type M electrophoretic mobility, associating M with the ts lesion and the other observed phenotypes. In each of these revertants, as well as in three revertants each from D2 and D3, there has been coreversion from the low specific infectious and hemolytic activities to greater, and often wild-type, activities. There is also a coreversion for F1+2 incorporation into virions. All of the revertants incorporate F1+2 into virions more efficiently than their mutant parents. The coreversions associate those phenotypes with the ts lesion and, in the case of D1, with the M lesion as well.

Animals↗
PubMed2006

Use of FTA filter paper for the molecular detection of Newcastle disease virus.

The feasibility of using Flinders Technology Associates filter papers (FTA cards) to collect allantoic fluid and chicken tissue samples for Newcastle disease virus (NDV) molecular detection was evaluated. Trizol RNA extraction and one-step reverse transcriptase-polymerase chain reaction (RT-PCR) were used. FTA cards allowed NDV identification from allantoic fluid with a titre of 10(5.8) median embryo lethal doses/ml. The inactivated virus remained stable on the cards for 15 days. NDV was detected from FTA imprints of the trachea, lung, caecal tonsil and cloacal faeces of experimentally infected birds. RT-PCR detection from FTA cards was confirmed by homologous frozen-tissue RT-PCR and virus isolation. Direct nucleotide sequence of the amplified F gene allowed prediction of NDV virulence. No virus isolation was possible from the FTA inactivated samples, indicating viral inactivation upon contact. The FTA cards are suitable for collecting and transporting NDV-positive samples, providing a reliable source of RNA for molecular characterization and a hazard-free sample.

Animals↗
PubMed2000

Newcastle disease virus phosphoprotein gene analysis and transcriptional editing in avian cells.

Nucleotide sequence was determined for the phosphoprotein (P) gene from 23 Newcastle disease virus (NDV) isolates representing all defined pathotypes with different chronological and geographic origins. Sequence variation, with synonymous substitutions dominating, occurred throughout the P gene. An exception was a conserved central region containing the transcriptional editing site. Four G nucleotide additions were detected in NDV P gene mRNA potentially creating alternative open reading frames. However, only one in-frame stop codon exists with a single G addition among all isolates that would allow for a potential V protein. A second potential stop codon does not exist in the P gene consensus sequence among all isolates with more than one G nucleotide addition at the editing site. This precludes a possible W protein in these isolates. A second potential alternative in-frame start site exists among all isolates that could encode a predicted X protein for NDV. Comparison of the P gene editing sites among the Paramyxovirinae and predicted P gene usage demonstrates that NDV more closely resembles the respiroviruses and morbilliviruses. Phylogenetic analysis of P gene sequences among NDV isolates demonstrates there are two clades of these viruses. One group includes viruses isolated in the US prior to 1970, while a second cluster includes virulent viruses circulating worldwide.

Amino Acid Sequence↗
PubMed2005

Genome sequence of the thermostable Newcastle disease virus (strain I-2) reveals a possible phenotypic locus.

The complete genome sequence of the Australian I-2 heat-tolerant Newcastle disease virus (NDV) vaccine (master seed stocks) was determined and compared to the sequence of the parent virus from which it had been derived after exposure of the parent stock at 56 degrees C for 30 min. Nucleotide changes were observed at a number of positions with synonymous mutations being greater than those observed for non-synonymous mutations. Sequence data for the HN gene of a parental culture of V4 and two heat-tolerant variants of V4 were obtained. These were compared with the data for the I-2 viruses and with published sequences for parental V4 and for a number of ND vaccine strains. Sequence analyses did not reveal the ARG(303) deletion in the HN protein, previously claimed to be responsible for the thermostable phenotype. No consistent changes were detected that would indicate involvement of the HN protein in heat resistance. The majority of alterations were observed in the L protein of the virus and it is proposed that these alterations were responsible for the heat-tolerant phenotype of the I-2 NDV vaccine.

Amino Acid Sequence↗
PubMed1991

Neutralization map of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus: domains recognized by monoclonal antibodies that prevent receptor recognition.

Monoclonal antibodies (MAbs) to the hemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus delineate seven overlapping antigenic sites which form a continuum on the surface of the molecule. Antibodies to five of these sites neutralize viral infectivity principally by preventing attachment of the virion to cellular receptors. Through the identification of single amino acid substitutions in variants which escape neutralization by MAbs to these five antigenic sites, a neutralization map of HN was constructed, identifying several residues that contribute to the epitopes recognized by MAbs which block the attachment function of the molecule. These epitopes are defined, at least in part, by three domains on HN: residues 193 to 201; 345 to 353 (which include the only linear epitope we have identified in HN); and a C-terminal domain composed of residues 494, 513 to 521, and 569. To identify HN residues directly involved in receptor recognition, each of the variants was tested for its ability to agglutinate periodate-modified chicken erythrocytes. One variant with a single amino acid substitution at residue 193 was 2.5- to 3-fold more resistant to periodate treatment of erythrocytes than the wild-type virus, suggesting that this residue influences the binding of virus to a sialic acid-containing receptor(s) on the cell surface.

Animals↗
PubMed1977

Alterations of actin-containing structures in BHK21 cells infected with Newcastle disease virus and vesicular stomatitis virus.

The distribution pattern of actin-containing structures in BHK21 cells and the changes which they undergo upon infection with Newcastle disease virus (NDV) and vesicular stomatitis virus (VSV) were studied by means of immunofluorescence. Double labelling with antibodies conjugated with fluorescein (for actin) and rhodamine (for virus antigens) has shown that the progressive cytopathic effects after virus infection are accompanied by extensive alterations of the structures demonstrable by antiactin antibodies. In NDV-infected BHK21 cells the number of actin filaments increases, some zones which contain virus antigens apparently being in close association with the actin structures. By contrast, infection with VSV results in a strong reduction of actin-containing fibres. The results indicate that in the genesis of morphologically detectable alterations of a cell after virus infection--the 'cytopathic changes'--alterations of those structural elements are involved which are also probably responsible for maintenance of cell shape and motility.

Actins↗
PubMed1988

Role of macrophages in bypassing the inhibitory activity of Newcastle disease virus on the T-suppressor-cell circuit which regulates contact sensitivity to picryl chloride.

The interaction between the paramyxovirus of Newcastle disease virus (NDV) and the T-suppressor-cell circuit which regulates the expression phase of contact sensitivity reaction to picryl chloride was investigated. NDV infection impairs the T-acceptor-cell (Tacc) activity, as demonstrated by the failure of Tacc from mice infected with NDV both on Day 0 and on Day 3 to release the nonspecific inhibitor of the passive transfer of contact sensitivity. Tacc from NDV-infected mice fail to bind appreciable amounts of exogenous T suppressor factor, so indicating that the virus eliminates this T-cell population. However, macrophages from mice infected with NDV are able to release a nonspecific inhibitor of the passive transfer of contact sensitivity, indicating that the inhibition of Tacc activity in mice infected with NDV is bypassed by macrophages, so that the T-suppressor circuit is functionally active in NDV-infected mice. The mechanism of the selective inhibition of the Tacc activity by NDV is discussed.

Animals↗
PubMed1985

Studies on the development of pelleted Newcastle disease virus (NDV) vaccine.

White leghorn chickens (7-10 weeks old) were orally infused with varied doses of lentogenic and mesogenic strains of Newcastle disease virus. The antibody response of the chickens was monitored by haemagglutination inhibition tests weekly for 4 weeks postinfusion. A high dose of virus (10(9) EID50) was necessary to induce a serological response typical of chickens that resist challenge. Sera from chickens infused with low doses (10(5) EID50) of the virus only showed marginal haemagglutination inhibiting activity. Trypsin levels as high as 0.35 mg ml-1 were detected from duodenal secretions and are assumed to be responsible in part for viral inactivation. Fasting (no food and water) the chickens beyond 12 h did not appear to increase antibody response to low titre virus.

Animals↗
PubMed1980

Proteolytic activation of the haemagglutinin-neuraminidase of Newcastle disease virus involves loss of a glycopeptide.

The uncleaved (HN0) and the cleaved (HN) forms of the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus (NDV), strain Ulster, were analysed by polyacrylamide gel electrophoresis under reducing and non-reducing conditions. When HN0 is converted into HN, a glycopeptide with an apparent mol. wt. of about 8000, which is not found in the mature spike, is removed.

Glycopeptides↗
PubMed2007

Listeria monocytogenes mutants carrying Newcastle disease virus F gene fused to its actA and plcB: in vitro expression and immunogenicity in chickens.

Recombinant Listeria monocytogenes mutants carrying Newcastle disease virus (NDV) fusion protein gene F were constructed by homologous recombination. NDV F or its truncated fragment Fa was used as the model heterologous gene to be integrated into actA or plcB downstream of their signal sequences. Correct orientation of the inserted genes was verified by polymerase chain reaction amplification of F or Fa. The inserted F and Fa were expressed in the two recombinants Lm-DeltaactA-F and Lm-DeltaplcB-Fa as shown by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and western blot. Both recombinants exhibited reduced virulence to embryonated eggs and mice by about 1.5-2.5 logs as compared with the parent wild strain 10403S. They were also less invasive than strain 10403S (P<0.05). Chickens receiving the recombinant strains orally or intraperitoneally were partially protected from virulent NDV challenge possibly due to enhancement of non-specific immunity because the antibody titers against the homologous virus strain or the recombinant truncated fusion protein were marginal. Further research is needed in other animal models to see if the low antibody response results from insufficient expression of the heterologous genes as a result of failure of L. monocytogenes or its recombinants to persist or replicate in chickens.

Animals↗
PubMed2006

Third genome size category of avian paramyxovirus serotype 1 (Newcastle disease virus) and evolutionary implications.

The goal of the study was to establish if there was a relationship between molecular patterns and virus evolution. Therefore the complete genome sequence of two distinct apathogenic Newcastle disease virus (NDV) strains was determined and a third genome size category, containing 15,198 nucleotides, was recognized. Phylogenetic analysis revealed that two major separations resulting in three genome size categories occurred during the history of NDV. An ancient division in the primordial reservoir (wild waterbird species) led to two basal sister clades, class I and II, with genome sizes 15,198 (due to a 12 nucleotide insert in the phosphoprotein gene) and 15,186 nucleotides, respectively. Ancestors of only class II viruses colonized chicken populations and subsequently converted to virulent forms. These took place more than once and resulted in an early lineage [including genotypes I-IV and H33(W)] with genome size of 15,186 nucleotides. A second division occurred in the 20th century in the secondary (chicken) host. This gave rise to the branching-off of a clade (including recent genotypes V-VIII consisting of only pathogenic viruses) with the concomitant insertion of six nucleotides into the 5' non-coding region of the nucleoprotein gene thereby increasing the genome size to 15,192 nucleotides.

Animals↗
PubMed1984

Recovery of host cell protein synthesis during infection with a temperature-sensitive mutant of Newcastle disease virus.

When chick embryo fibroblasts infected with high multiplicities of a non-revertible temperature-sensitive (ts) mutant (ts53) of Newcastle disease virus (NDV) at the permissive temperature (34 degrees C) and incubated to allow the appearance of virus-induced proteins were shifted up to and incubated at the non-permissive temperature (42 degrees C), analysis of [3H]leucine-labelled proteins by SDS-PAGE revealed a marked increase in cellular protein synthesis and a decline in viral synthesis, with an eventual return to an apparently uninfected state. Mutant ts53 apparently ceased to suppress cellular protein synthesis, and translation of viral proteins was markedly inhibited. This was not observed in ts+-infected cells, or in ts53-infected cells maintained at the permissive temperature. Recovery from the infected state was inhibited by actinomycin D at any stage, but was not prevented by cycloheximide present immediately before and during temperature shift-up. Mutant ts53 was shown to be RNA- at 42 degrees C, although viral mRNAs synthesized at 34 degrees C are shown to be present throughout host recovery but in an inactive state.

Animals↗
PubMed2006

Deduced amino acid sequences surrounding the fusion glycoprotein cleavage site and of the carboxyl-terminus of haemagglutinin-neuraminidase protein of the avirulent thermostable vaccine strain I-2 of Newcastle disease virus.

A single-tube RT-PCR technique generated a 387 bp or 300 bp cDNA amplicon covering the F(0) cleavage site or the carboxyl (C)-terminus of the HN gene, respectively, of Newcastle disease virus (NDV) strain I-2. Sequence analysis was used to deduce the amino acid sequences of the cleavage site of F protein and the C-terminus of HN protein, which were then compared with sequences for other NDV strains. The cleavage site of NDV strain I-2 had a sequence motif of (112) RKQGRLIG(119), consistent with an avirulent phenotype. Nucleotide sequencing and deduction of amino acids at the C-terminus of HN revealed that strain I-2 had a 7-amino-acid extension (VEILKDGVREARSSR. This differs from the virulent viruses that caused outbreaks of Newcastle disease in Australia in the 1930s and 1990s, which have HN extensions of 0 and 9 amino acids, respectively. Amino acid sequence analyses of the F and HN genes of strain I-2 confirmed its avirulent nature and its Australian origin.

Amino Acid Motifs↗