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PubMed1995

Modulation of the neuraminidase activity of HN protein from Newcastle disease virus by substrate binding and conformational change: kinetic and thermal denaturation studies.

A statistical study of the enzyme kinetics of the soluble fraction of Haemagglutinin-Neuraminidase (HN) protein from Newcastle Disease virus reveals that a high substrate concentrations its neuraminidase activity follows substrate-inhibition kinetics, in which the binding of a second molecule of substrate to the protein inhibits its enzymatic activity. Results show that the enzymatic activity is modulated by the second substrate to a different extent when the protein is in different environments. Taken together with results obtained by thermal denaturation studies of HN under varying conditions the data show that conformational changes leading to a loss of rigidity of HN are concomitant with the loss of catalytic activity. Also, electrophoretic and sucrose gradient analyses show that the soluble domain of HN behaves as a monomer.

Kinetics↗
PubMed2004

The P gene of Newcastle disease virus does not encode an accessory X protein.

Many paramyxoviruses encode non-essential accessory proteins that are involved in the regulation of virus replication and inhibition of cellular antiviral responses. It has been suggested that the P gene mRNA of Newcastle disease virus (NDV) encodes an accessory protein - the so-called X protein - by translation initiation at a conserved in-frame AUG codon at position 120. Using a monoclonal antibody that specifically detected the P and X proteins, it was shown that an accessory X protein was not expressed in NDV-infected cells. Recombinant NDV strains in which the AUG was changed into a GCC (Ala) or GUC (Val) codon were viable but showed a reduction in virulence, probably because the amino acid change affected the function of the P and/or V protein.

Codon↗
PubMed1996

Pathogenicity and phylogenetic evaluation of the variant Newcastle disease viruses termed "pigeon PMV-1 viruses" based on the nucleotide sequence of the fusion protein gene.

The nucleotide sequences of the entire F genes of two isolates of the pigeon PMV-1 (PPMV-1) variant of Newcastle disease virus (NDV) were determined using RTPCR. The deduced amino acid sequences of the F0 protein showed four differences between isolate 760/83 which had been passaged 4 times in chickens and gave an intravenous pathogenicity index in chickens (IVPI) of 2.01 and isolate 1168/84 which had received six passages in chickens and had an IVPI of 0.00. The F genes of virus from two passage levels of isolate 1447/84, 0 with IVPI value 0.00 and six with IVPI value 0.58, were partially sequenced to cover the areas of variation between 760/83 and 1168/84. The two passage levels of 1447/84 showed identical sequences in these areas which in turn were identical of those of 760/83. It was concluded that the recorded differences in intravenous pathogenicity were unlikely to be associated with differences in the primary structure of the F0 protein. Phylogenetic comparisons of the F gene sequences of the two PPMV-1 viruses with those published for other NDV strains and isolates showed that the PPMV-1 viruses formed a new fourth lineage but were closely related to strain Warwick with which they presumably shared a common origin.

Amino Acid Sequence↗
PubMed1990

A host range mutant of Newcastle disease virus with an altered cleavage site for proteolytic activation of the F protein.

The primary structure of the F protein of a host range mutant of the Ulster strain of Newcastle Disease virus (NDV) has been determined by nucleotide sequence analysis and compared to that of the wild type and other NDV strains. The cleavage site of the mutant had the sequence Gly-Lys-Gln-Arg-Arg as compared to two isolated basic amino acids [Gly-Lys(Arg)-Gln-Gly-Arg] with the apathogenic strains and two pairs of basic amino acids [Arg-Arg-Gln-Lys(Arg)-Arg] with the pathogenic strains. The data indicate that the cleavability of the F protein of NDV increases with the number of arginine and lysine residues at the cleavage site and that the susceptibility of the pathogenic strains to ubiquitous host proteases depends on both pairs of basic amino acids.

Amino Acid Sequence↗
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↗
PubMed1993

The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation.

Using Cos-7 cells and an SV40-based vector, quantitative assays for fusion directed by the Newcastle disease virus hemagglutinin-neuraminidase (HN) and fusion glycoproteins were developed. Data from these assays showed that after cotransfection of the HN protein and the fusion protein DNAs, there was a progressive increase in syncytia size over background levels while transfection with HN protein or F protein DNA alone resulted in no changes over background. Using immunofluorescence, the efficiency of syncytia formation directed by the glycoproteins was assessed. Virtually all cells expressing the fusion protein alone or the HN protein alone existed as single nucleated cells. However, all cells coexpressing the two genes existed in syncytia with 4 to 50 nuclei. Using these assays, the fusion promotion activity of two deletion mutants of the HN protein was quantitated. One mutation deleted amino acids 4 through 26, effectively removing the cytoplasmic domain of the protein. This mutant protein was found at the cell surface, although in very reduced amounts. The mutant protein could bind red blood cells and could promote fusion, although the syncytia formed were smaller (4 to 9 nuclei) than those promoted by the wild-type protein. A second mutation deleted nine amino acids (91-99) located 37 amino acids from the transmembrane region in the ectodomain. This mutant was detected at the cell surface at 33% the level of wild type and it retained near normal ability to bind red blood cells. However, this mutation completely eliminated the fusion promotion activity of the HN protein. This mutation effectively separates the attachment function of the HN protein from fusion promotion.

Animals↗
PubMedDate not supplied

Viscerotropic velogenic Newcastle disease in turkeys: isolation of Newcastle disease virus from tracheal and cecal tonsil organ cultures.

Tracheal and cecal-tonsil organ cultures were made from vaccinated turkeys that had survived challenge of immunity with viscerotropic velogenic strain of Newcastle disease virus (NDV). Culture fluids were tested to show that latent infections did exist in the vaccinated and challenged turkeys, thus indicating a possible carrier state. NDV was recovered from 6 of 159 turkeys examined. Preliminary tests indicate that 4 isolants are velogenic and 2 are lentogenic.

Administration, Oral↗
PubMed1984

Selective breeding for high and low antibody responses to inactivated Newcastle disease virus in Japanese quails.

Two lines of Japanese quail were divergently selected for high and low antibody responses after being twice injected at 4 and 6 weeks of age with inactivated Newcastle disease virus antigen. After seven generations of selection, the serum antibody level in the high line was 24% greater than the level in the unselected control lines, whereas the low line antibody level was approximately 37% less than that in the control line. The estimated heritability (H2S + D) was approximately .12 +/- .50. The realized h2, calculated from coefficient of regression formula on seven generations (G3 to G9 ), was .07.

Animals↗
PubMedDate not supplied

Detection of a macrophage-specific antigen and the production of interferon gamma in chickens infected with Newcastle disease virus.

Formalin-fixed, paraffin-embedded spleen and intestinal tissues were harvested at 2 days postinfection from 4-wk-old white rock chickens infected with five different strains of Newcastle disease virus (NDV). These tissues were examined for the presence of macrophage antigen expression, virus replication, and interferon gamma (IFN gamma) production. The five strains represented all three NDV pathotypes. Viral replication and IFN gamma, as determined by riboprobe in situ hybridization, were detected only in those chickens infected with velogenic viscerotropic NDV (VVNDV) strains. Macrophage antigen expression, an indicator of macrophage activation, was determined by immunohistochemistry with a macrophage-specific antibody, CVI-ChNL-68.1. Presence of macrophage antigen was most prominent in VVNDV-infected chickens. The distribution of this antigen within tissues was far more diffuse than the staining for viral mRNA. The presence of IFN gamma mRNA was detected in the spleen and intestinal lymphoid tissue of VVNDV-infected chickens. There was also increased macrophage antigen expression in the mesogen-infected birds, but it was less dramatic than in tissues from VVNDV-infected chickens. One of two lentogen-infected birds had evidence of increased macrophage antigen expression only in the spleen.

Animals↗
PubMed1990

Monoclonal antibodies to three structural proteins of Newcastle disease virus: biological characterization with particular reference to the conformational change of envelope glycoproteins associated with proteolytic cleavage.

Monoclonal antibodies (MAbs) to the haemagglutinin-neuraminidase (HN), fusion (F) and matrix (M) proteins of Newcastle disease virus were prepared and characterized. At least three non-overlapping or partially overlapping antigenic sites were delineated on the HN, three on the F and three on the M proteins by competitive binding assays. Antigenic sites on the HN and F proteins roughly represented functional domains defined by serological tests. Two antigenic sites on the F protein were involved in virus neutralizing and haemolysis-inhibiting activity. These antigenic determinants were readily affected by treatment with certain surfactants and acetone. Proteolytic cleavage of the HN and F proteins was associated with conformational change, revealed by altered reactivity with MAbs and by altered topological arrangements of some epitopes. None of the anti-M MAbs inhibited any biological activities of the virus.

Animals↗
PubMed1980

Enhanced production of virus-inhibiting factor (interferon) in human diploid cells by ultraviolet irradiation and temperature shift-down after stimulation with Newcastle disease virus.

The production of the virus-inhibiting factor or interferon (IF) was highest in cells incubated at 37 C after inoculation with Newcastle disease (ND) virus and decreased as the incubation temperature was lowered. Shift-down of incubation temperature to 32 C or 34 C after incubation at 37 C for 4--7 hr enhanced IF production in cell cultures stimulated with ND virus, as compared with cultures incubated continuously at 37 C. Shift-down to 32 C after incubation at 37 C for 6 hr was optimal for this enhancement of IF yield. Enhanced IF production was also observed in cell cultures irradiated by ultraviolet light 4--7 hr after stimulation with ND virus.

Cell Line↗
PubMedDate not supplied

Evaluation of different methods of inactivation of Newcastle disease virus and avian influenza virus in egg fluids and serum.

Viruses conveyed in shipments of eggs, viral diagnostic reagents, or avian serum samples are a potential hazard for susceptible poultry. Different methods of treatment of those materials to eliminate the hazard of virulent and avirulent strains of Newcastle disease virus (NDV) or avian influenza virus (AIV) were evaluated. The NDV strains tested were more thermostable than the AIV strains. The results suggest that standard pasteurization methods would not reliably inactivate the concentrations of NDV used. beta-Propiolactone (BPL) (greater than or equal to 0.025%) inactivated NDV or AIV in allantoic fluid, but higher concentrations were needed to inactivate virus diluted in serum. Hemagglutination (HA) of NDV and AIV and hemolysis (HL) activity of NDV were reduced or eliminated by 0.4% BPL. Formalin (greater than or equal to 0.04%) inactivated either virus but adversely affected HA and HL activity. NDV or AIV was inactivated by binary ethylenimine (BEI) (0.01 M) with no adverse effect on HA or HL. Heat (56 C) or BEI (0.01 M) had no apparent effect on hemagglutination-inhibition (HI) titers of NDV and AIV antisera, the effect of formalin (0.1%) was variable, and BPL (greater than or equal to 0.25%) depressed the HI titers of both antisera. The optimum method should achieve virus inactivation without harming the treated material.

Animals↗
PubMed2006

Recombinant haemagglutinin neuraminidase antigen-based single serum dilution ELISA for rapid serological profiling of Newcastle disease virus.

A recombinant haemagglutinin neuraminidase (HN) antigen-based single serum dilution enzyme linked immuno-sorbent assay (ELISA) was developed to measure the specific antibody in sera of chickens against Newcastle disease virus. A linear relationship was found between the predicted antibody titres at a single working dilution of 1:1000 and the corresponding observed serum titres as determined by the standard serial dilution method. Regression analysis was used to determine a standard curve from which an equation was derived that allowed the demonstration of this correlation. The equation was then used to convert the corrected absorbance readings of the single working dilution directly into the predicted ELISA antibody titres. The assay proved to be sensitive, specific and accurate as compared to the standard haemagglutination inhibition (HI) test.

Animals↗
PubMed1985

Differential effect of poly rI.rC and Newcastle disease virus on the expression of interferon and cellular genes in mouse cells.

The expression of type I murine interferon (MuIFN) genes and several other cellular genes was examined in poly rI.rC induced and Newcastle disease virus (NDV) infected mouse cells. Northern analysis of RNA from induced L cells revealed that the MuIFN-alpha s are expressed efficiently in NDV infected cells but only at low levels in poly rI.rC induced cells. MuIFN-beta 1, however, is expressed equally well in cells treated with poly rI.rC or infected with NDV. As shown by the use of a probe specific for poly rI.rC, interferon induction correlates with the cellular uptake of poly rI.rC into the cells. The relative levels of alpha and beta 1 mRNAs in the cells reached a maximum at 10 hr after the induction which indicates coordinate expression of alpha and beta 1 interferon genes. The effect of viral infection on the expression of two murine genes coinduced with interferon (pMIF20/11 and pMIF3/10) and several cellular genes was also examined. While pMIF20/11 is an inducible gene, the pMIF3/10 gene is expressed constitutively in mouse L cells. Viral infection, but not poly rI.rC treatment, enhanced the expression of the pMIF3/10 gene, as well as two other cellular genes; H-2 and c-myc, however, the expression of beta-actin gene was unaltered. These data indicate that enhancement of gene expression in virus infected cells in not limited to the interferon system.

Actins↗
PubMed1988

Characterization of the sites of proteolytic activation of Newcastle disease virus membrane glycoprotein precursors.

The F1- and F2-polypeptide components of the fusion proteins and the hemagglutinin/neuraminidase proteins of the avirulent Queensland (V4) and virulent Australia-Victoria (AuV) strains of Newcastle disease virus have been isolated and subjected to extensive primary structural analysis including amino-terminal sequence analysis and fast atom bombardment-mass spectrometry mapping. Nucleotide sequence analysis was performed on the gene which encodes the V4 hemagglutinin/neuraminidase protein. Signal peptidase cleavage was found to have occurred at the Ser31-Leu32 peptide bond of the primary translation products of the fusion protein genes. Activation cleavage of the V4 fusion protein precursor generated a sequence of -Gly-Lys-Gln-Gly84 at the carboxyl terminus of the F2-polypeptide and an amino-terminal sequence of the F1-polypeptide commencing with 86Leu-Ile-Gly-. The V4 hemagglutinin/neuraminidase protein gene was found to encode a primary translation product 45 amino acids longer at the carboxyl terminus than obtainable from the corresponding gene of the AuV strain (McGinnes, L. W., and Morrison, T. G. (1986) Virus Res. 5, 343-356). However, post-translational proteolytic processing, exclusive to the primary translation product of the V4 hemagglutinin/neuraminidase protein gene, was found to have removed the last 42 residues of this carboxyl-terminal appendage.

Amino Acid Sequence↗
PubMed1988

Differential detergent treatment allows immunofluorescent localization of the Newcastle disease virus matrix protein within the nucleus of infected cells.

Paramyxoviruses are cytoplasmic viruses and presumably do not require any nuclear function for their replication. However, recent studies using monoclonal antibodies directed against the Newcastle disease virus matrix (M) protein have found a large portion of the M protein apparently associated with the nucleus of infected cells. Whether the M protein is associated with the cytoplasmic surface of the nucleus or whether the M protein is actually located within the nucleus has not been clearly determined. To examine this question, conditions for selectively permeabilizing the cytoplasmic membrane were sought. After treating fixed cells with a low concentration (0.02%) of the nonionic detergent Triton X-100, the cytoplasmic antigen vimentin was stained with a monoclonal antibody, but nuclear antigens were not. Apparently, 0.02% Triton permeabilizes the plasma membrane while leaving the nuclear membrane intact. Under these conditions, monoclonal antibodies directed against the NDV phosphoprotein and hemagglutinin/neuraminidase glycoprotein stained infected cells, but a monoclonal antibody to the M protein did not. The inability of the anti-M monoclonal antibody to stain the nucleus, even though the outer nuclear membrane is accessible under these conditions, indicates that the M protein is not associated with the outer membrane of the nucleus. The nuclei of infected cells treated with a higher concentration (0.05%) of Triton X-100 were stained both with antibodies to nuclear antigens and with the anti-M monoclonal antibody.

Animals↗