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PubMed2004

Virosome and ISCOM vaccines against Newcastle disease: preparation, characterization and immunogenicity.

The purpose of this study was to prepare and characterize virosomes and ISCOMs containing envelope proteins of Newcastle disease virus (NDV) and to evaluate their immunogenicity in target animals (chickens). Virosomes were prepared by solubilization of virus with either Triton X-100 or octyl glucoside (OG) followed by detergent removal. Biochemical analysis revealed that these virosomes contained both the haemagglutinin-neuraminidase protein (HN) and the fusion protein (F), with preserved biological activity. Acidic environment triggered the fusion between virosomes and chicken erythrocyte ghosts. Formation of ISCOMs was achieved by solubilizing phospholipids, cholesterol, envelope protein antigen and Quil A in Triton X-100. The ISCOM particles were formed by removal of the detergent. In each formulation the relative HN content correlated with the capability to agglutinate red blood cells. The immunogenicity of these lipid-based subunit vaccines was determined in chickens after subcutaneous immunization. The relative HN content of the subunit vaccines correlated with the haemagglutination-inhibition (HI) antibody titres. Virosomes prepared with Triton X-100 and ISCOMs offered high clinical protection (> 80%) upon challenge with virulent NDV. Virosomes prepared with OG yielded lower clinical protection despite high HI antibody titres. Virosomes with reduced antigen density showed poor immunogenicity and protection. In conclusion, ND virosomes and ISCOMs were found to be immunogenic and provided good protection.

Animals↗
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↗
PubMed1994

Modulation of the activities of HN protein of Newcastle disease virus by nonconserved cysteine residues.

Comparisons of the sequences of the hemagglutinin-neuraminidase (HN) protein from thirteen different strains of Newcastle disease virus (NDV) show that while 12 cysteine residues are conserved in all strains, two cysteine residues are variably present (Sakaguchi et al. (1989) Virology 169, 260-272). One of these residues, at amino acid 6, is in the cytoplasmic domain. The other cysteine is at amino acid 123 in the ectodomain and is responsible for disulfide-linked HN dimers detected in some NDV strains (McGinnes and Morrison (1994) Virology 200, 470-483). To explore the role of these nonconserved residues in the structure and function of the protein, cysteine residues at amino acid 6 and 123 in the HN protein of the AV strain of NDV were mutated individually and in combination by site specific mutagenesis to serine and tryptophan, respectively. Proteins with mutations in either residue (C6S or C123W) or in both residues (C6S,123W) were transported to the cell surface. However, all three mutants had reduced attachment, neuraminidase, and fusion promotion activities. All three mutant proteins also showed an alteration in an antigenic site specific for oligomers of HN protein while all other antigenic sites were present at wild type levels. These results suggest that the nonconserved cysteine residues in the HN sequence may modulate the biological activities of the protein by affecting the oligomeric structure of the protein.

Animals↗
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↗
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↗
PubMed1988

The P protein and the nonstructural 38K and 29K proteins of Newcastle disease virus are derived from the same open reading frame.

The nucleotide sequence of cloned cDNA copies of the mRNA encoding the Newcastle disease virus (NDV), strain AV, phosphoprotein (P) was determined. The sequence of 1443 nucleotides contains one long open reading frame which could encode a protein with a molecular weight of 42,126, and two smaller open reading frames which could encode proteins with molecular weights of 11,178 and 13,935. Full-length cDNA clones were constructed in an SP6 vector, mRNA was transcribed in a cell-free system using the SP6 polymerase, and the mRNA was translated in a wheat germ cell-free extract. The P mRNA directed the synthesis of, primarily, four products. One, with a molecular weight of 53,000 Da, comigrated with authentic P protein made in infected cells and was precipitable with antisera with specificity for the NDV P protein. The other products of the cell-free reaction had molecular weights of 38,000, 29,000 and 12,000. The 29,000- and the 38,000-Da polypeptides were also precipitable with anti-P protein antibody. Using truncated cDNA clones, evidence is presented that the 38,000- and 29,000-Da proteins are derived from initiation at AUG triplets in the same reading frame as the P protein. Infected cells also contain these polypeptides which may be analogous to C proteins of other paramyxoviruses. Thus the NDV P protein mRNA is different than most other paramyxovirus P protein mRNAs which are translated in two different reading frames to yield the P and C proteins.

Amino Acid Sequence↗
PubMed1999

Comparison of substrate specificities against the fusion glycoprotein of virulent Newcastle disease virus between a chick embryo fibroblast processing protease and mammalian subtilisin-like proteases.

The fusion (F) protein precursor of virulent Newcastle disease virus (NDV) strains has two pairs of basic amino acids at the cleavage site, and its intracellular cleavage activation occurs in a variety of cells; therefore, the viruses cause systemic infections in poultry. To explore the protease responsible for the cleavage in the natural host, we examined detailed substrate specificity of the enzyme in chick embryo fibroblasts (CEF) using a panel of the F protein mutants at the cleavage site expressed by vaccinia virus vectors, and compared the specificity with those of mammalian subtilisin-like proteases such as furin, PC6 and PACE4 which are candidates for F protein processing enzymes. It was demonstrated in CEF cells that Arg residues at the -4, -2 and -1 positions upstream of the cleavage site were essential, and that at the -5 position was required for maximal cleavage. Phe at the +1 position was also important for efficient cleavage. On the other hand, furin and PC6 expressed by vaccinia virus vectors showed cleavage specificities against the F protein mutants consistent with that shown by the processing enzyme of CEF cells, but PACE4 hardly cleaved the F proteins including the wild type. These results indicate that the proteolytic processing enzymes of poultry for virulent NDV F proteins could be furin and/or PC6 but not PACE4. The significance of individual contribution of the three amino acids at the -5, -2 and +1 positions to cleavability was discussed in relation to the evolution of virulent and avirulent NDV strains.

Animals↗
PubMed1982

RNA synthesis by Newcastle disease virus temperature-sensitive mutants in two RNA-negative complementation groups.

The temperature-sensitive RNA-negative mutants of Newcastle disease virus comprise two complementation groups, group A (seven members) and group E (one member). The RNA-synthesizing activities of four representative members of group A and the single member of group E were compared with the activity of the wild type. These mutants were defective to varying extents in primary transcription at the nonpermissive temperature, ranging from mutant A1, which had no activity, to mutant E1, which lost only 50% of its activity. All of the mutants were also defective in a postprimary transcriptive process since after preincubation at the permissive temperature in the presence of cycloheximide, there was no subsequent RNA synthesis at the nonpermissive temperature upon removal of the cycloheximide. Similarly, in experiments in which cycloheximide was not used, shifts from the permissive temperature to the nonpermissive temperature before 3 h postinfection did not result in RNA synthesis. However, later shifts to the nonpermissive temperature did allow RNA synthesis. With the exception of mutant A1, all of the mutants maintained this RNA-synthetic ability for at least 3 h, suggesting that RNA synthesis from progeny genomes was not the major postprimary transcriptive defect in these mutants. In contrast, the RNA-synthetic ability of mutant A1 rapidly decayed at the nonpermissive temperature, suggesting that the A gene product is involved in RNA synthesis from progeny genomes. The postprimary transcriptive defect(s) of the other mutants may be in the processing or stability of a protein, in the processing of mRNA, or in replication. Plaque-forming revertants (ts+) of all of the mutants coreverted for RNA synthesis. This finding strengthens the relationship between temperature sensitivity for plaquing and both the primary and postprimary RNA-negative phenotypes.

Cycloheximide↗
PubMed1994

Local pathological reactions induced in pigs and cats by adjuvant ISA-70 containing inactivated Newcastle disease virus antigen.

Gross and microscopic changes at the injection site in pigs and cats were investigated for 8 weeks after an intramuscular injection of oil adjuvant ISA-70 emulsion, containing inactivated Newcastle disease virus antigen. In pigs, an egg-sized and discolored lesion with pinpoint to miliary-sized nodules was observed at 2 to 8 weeks post injection (PI). In cats, there was partial thickening of the subcutaneous tissue at 2 to 8 weeks PI. Histopathologic changes in pigs were fundamentally similar to those in cats, however, the local tissue reactions in pigs were severer and more protracted than those in cats. The lesions in pigs were characterized by formation of large-sized cysts and well-developed encapsulation of the cysts with epithelioid cells.

Adjuvants, Immunologic↗
PubMed1995

The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus.

To explore the role of N-linked carbohydrate in the activities of the hemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus (NDV), the six glycosylation addition sites (G1-G6) in the HN sequence of the AV strain of NDV were mutated. Migration of mutant protein on polyacrylamide gels as well as endoglycosidase H digestion of mutant protein showed that four of the addition sites (G1, G2, G3, and G4 at amino acids 119, 341, 433, and 481, respectively) are used while two (G5 and G6 at amino acids 508 and 538, respectively) are not used. Proteins expressed from single and all possible combinations of double and triple mutant DNAs as well as the unglycosylated molecule were characterized for the presence of specific antigenic sites, formation of disulfide-linked dimers, stability, transport to the cell surface, and biological activity. Results showed that glycosylation at positions G1 and G2 play little detectable role in the folding, stability, or transport of the molecule either singly or in combination with other mutations. Mutation of these sequons, however, significantly increased the cell attachment and fusion promotion activities of the protein, particularly in combination. Mutation of the glycosylation site at G4 either singly or in combination with other site-eliminating mutants inhibited the formation of the mature protein, while a mutation eliminating the addition site at G3 had a slight effect on the efficiency of folding, particularly in combination with mutation of the site G4. When normalized to surface expression, elimination of carbohydrate addition sites at G3 and G4 singly or in combination with other mutations depressed in particular the neuraminidase activity of the protein but not the fusion promotion activity. Thus two oligosaccharides do not have a detectable role in maturation but do modulate the biological activities of the protein. The other two oligosaccharides influence both folding and activity of the protein.

Animals↗
PubMed2005

Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational change.

It has been shown that the L289A-mutated Newcastle disease virus (NDV) fusion (F) protein gains the ability to promote fusion of Cos-7 cells independent of the viral hemagglutinin-neuraminidase (HN) protein and exhibits a 50% enhancement in HN-dependent fusion over wild-type (wt) F protein. Here, we show that HN-independent fusion by L289A-F is not exhibited in BHK cells or in several other cell lines. However, similar to the results in Cos-7 cells, the mutated protein plus HN does promote 50 to 70% more fusion above wt levels in all of the cell lines tested. L289A-F protein exhibits the same specificity as the wt F protein for the homologous HN protein, as well as NDV-human parainfluenza virus 3 HN chimeras. The mutated F protein promotes fusion more effectively than the wt when it is coexpressed with either the chimeras or HN proteins deficient in receptor recognition activity. In addition, its fusogenic activity is significantly more resistant to removal of sialic acid on target cells. These findings are consistent with the demonstration that L289A-F interacts more efficiently with wt and mutated HN proteins than does wt F by a cell surface coimmunoprecipitation assay. Taken together, these findings indicate that L289A-F promotes fusion by a mechanism analogous to that of the wt protein with respect to the HN-F interaction but is less dependent on the attachment activity of HN. The phenotype of the mutated F protein correlates with a conformational change in the protein detectable by two different monoclonal antibodies. This conformational change may reflect a destabilization of F structure induced by the L289A substitution, which may in turn indicate a lower energy requirement for fusion activation.

Animals↗
PubMed2005

[Safety and efficacy of attenuated Salmonella typhimurium harbouring DNA vaccine against Newcastle disease virus].

A pair of primers were designed and synthesized according to the previously published sequence of fusion protein (F) gene of Newcastle disease virus (NDV) and used to amplify F gene by reverse-transcription polymerase chain reaction (RT-PCR) from the genomic RNA of a NDV strain JS5 isolated from goose. The PCR product was identified by sequencing. Then recombinant eukaryotic expression vector pVAX1-F was constructed through inserting F gene into MCS of pVAX1. The recombinant plasmid pVAX1-F was transfected in COS-7 cells, and identified for the transient expression of F gene by indirect immunofluorescent assay. Finally, the recombinant plasmid was transformed into attenuated Salmonella typhimurium SL7207, and the recombinant was screened and designated as SL7207 (pVAX1-F). It was verified that SL7207 (pVAX1-F) as the oral NDV DNA vaccine was safe for chickens after oral immunization at dosage of 10(10) CFU or below. 1-day-old commercial ISA brown chickens were immunized orally with SL7207 (pVAX1-F) at two different dosages (10(9) CFU and 10(8) CFU) on day 1, 14 and 28. On day 7 after the last immunization, no significant difference was observed in the body weight between these two groups (p > 0.05), and also no significant difference between those two groups and negative control group (p > 0.05). Since there were maternal antibodies, high ELISA titers of serum antibodies against NDV were detected in the chickens of all groups on day 14. However, the levels of serum antibodies were decreased in the chickens of all groups on day 28, but the anti-NDV antibody response detected in the sera of chickens immunized with SL7207 (pVAX1-F) at the dosage of 10(9) CFU were increased and significantly higher than the response induced by immunization with SL7207 (pVAX1) on day 35 (p < 0.05). Intestinal mucosal immune response was observed in chickens immunized with SL7207 (pVAX1-F) at the dosage of 10(9) CFU or 10(8) CFU. The high ELISA titers of antibodies against NDV in small intestinal mucosal samples from immunized chickens were on day 28 and 35. After challenged intranasally with virulent NDV strain F48E8, the chickens immunized with SL7207 (pVAX1-F) at the dosage of 10(9) CFU could be protected with the protective rate of 77.27%, significantly higher than those with SL7207 (pVAX1) (p < 0.05). In summary, the DNA vaccine delivered by attenuated Salmonella typhimurium was safe and has good immunogenicity for chickens. A novel mucosal DNA vaccine was developed and could be useful for controlling the infection and epidemic of ND in the poultry.

Animals↗