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At least 1,153 records · Page 64Linked to original sources
PubMed1984

Effect of N-acetyl-muramyl-L-alanyl-D-isoglutamine on interferon production in mice by Newcastle disease virus.

The activity (carbon clearance) of the reticuloendothelial system (RES) of mice inoculated intraperitoneally with N-acetyl-muramyl-L-alanyl-D-isoglutamine (muramyl dipeptide, MDP) was greatly stimulated 1 day, but not 7 days after MDP treatment. No enhancement of resistance to ectromelia virus infection and influenza virus infection in mice treated with MDP was observed. In mice splenectomized 1 week after MDP pretreatment, normal levels of circulating interferon were produced in response to Newcastle disease virus (NDV), whereas in the mice treated with MDP after splenectomy, circulating interferon levels were reduced to the same level as produced in the MDP-untreated and splenectomized mice. Interferon production in response to NDV was augmented in non-adherent peritoneal and spleen cell cultures derived from MDP-pretreated mice, whereas it was reduced in peritoneal and splenic macrophage cultures. These results suggest that the non-adherent spleen cells activated with MDP were disseminated from the spleen to other organs, that the lack of enhancement of interferon production in mice pretreated with MDP might be due to reduced interferon production in macrophages, and that the activation of the RES of the whole body by MDP did not correlate with the enhancement of interferon production in spleen cells or with the reduction of interferon production in macrophages.

Acetylmuramyl-Alanyl-Isoglutamine↗
PubMed1990

Comparison of the positions and efficiency of cleavage activation of fusion protein precursors of virulent and avirulent strains of Newcastle disease virus: insights into the specificities of activating proteases.

The F1- and F2-polypeptide components of in ovo activated fusion proteins of one virulent (AV or Australia-Victoria) strain, one low-virulence (EG or Eaves-Grimes) strain, and two avirulent (V4 or Queensland and WA2116) strains of Newcastle disease virus (NDV) were isolated and subjected to structural analysis. This included complementary application of amino acid analysis, fast atom bombardment-mass spectrometry, and N-terminal sequence analysis to fragments isolated from AspN protease digests of the F2-polypeptides using HPLC. As a result, the complete sequences of the F2-polypeptides were determined, including documentation of glycosylation of asparagine 54. The sequence of the cleavage-activation site of the WA2116 F0-protein was found to be distinctly different from this site in any other NDV F0-protein. Cleavage activation at the C termini of the F2-polypeptide regions was found to have occurred to approximately equivalent extents at arginines 82 and 85 of the AV and EG strains, but was restricted largely to arginine 85 of the V4 strain and completely to arginine 85 of the WA2116 strain. In each case cleavage activation was apparently succeeded by trimming of the basic residues from the newly formed C termini. Immunochemical analysis with antipeptide antisera showed that the extent of cleavage was influenced by amino acids adjacent to these arginines. These data provide insight into the substrate specificities of the enzymes involved in cleavage activation of the fusion protein precursors.

Amino Acid Sequence↗
PubMed1989

Modification of tumor cells by a low dose of Newcastle disease virus. II. Augmented tumor-specific T cell response as a result of CD4+ and CD8+ immune T cell cooperation.

Augmented tumor-specific T cell responses were observed against the high metastatic murine lymphoma variant ESb when using as immunogen ESb tumor cells that had been modified by infection with a low dose of Newcastle disease virus (NDV). Such virus-modified inactivated tumor cells (ESb-NDV) were potent tumor vaccines when applied postoperatively for active specific immunotherapy of ESb metastases. We demonstrate here that immune spleen cells from mice immunized with ESb-NDV contain enhanced immune capacity in both the CD4+, CD8- and the CD4-, CD8+ T cell compartments to mount a secondary-tumor-specific cytotoxic T cell response in comparison with immune cells from mice immunized with ESb. ESb-NDV immune CD4+, CD8- helper T cells also produced more interleukin 2 after antigen stimulation than the corresponding ESb immune cells. There was no participation of either CD4+ or CD8+ virus-specific cells in the augmented response. The specificity of the T cells for the tumor-associated antigen remained unchanged. Thus, there is the paradox that the virus-mediated augmentation of the tumor-specific T cell response in this system involves increased T helper activity but does not involve the recognition of viral epitopes as potential new helper determinants.

Animals↗
PubMedDate not supplied

Sudden death of a bearded vulture (Gypaetus barbatus) possibly caused by Newcastle disease virus.

An adult female bearded vulture (Gypaetus barbatus) in the Tel Aviv University Research Zoo was found dead without previous clinical signs. The predominant pathologic changes were considerable bloody content in the intestines and enlargement of the liver, which had a rubbery consistency with color changes. Microscopic lesions consisted of multifocal histiocytic infiltration in the liver. Newcastle disease virus (NDV) was isolated from a cloacal swab and from the lungs and liver. Intracerebral pathogenicity index of the virus, as estimated in 1-day-old chicks, was repeated three times and had an average value of 1.68, indicating a velogenic strain. Numerous Clostridium septicum bacteria were found on the intestinal surface, but bioassays in which they were orally administered into chickens and mice revealed that, even though they were heavily multiplied in the intestines, they were nonpathogenic. It seems that NDV, documented for the first time in a bearded vulture in Israel, was the likely cause of sudden death.

Animals↗
PubMed1999

Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein.

For most paramyxoviruses, syncytium formation requires the expression of both surface glycoproteins (HN and F) in the same cell, and evidence suggests that fusion involves a specific interaction between the HN and F proteins (X. Hu et al., J. Virol. 66:1528-1534, 1992). The stalk region of the Newcastle disease virus (NDV) HN protein has been implicated in both fusion promotion and virus specificity of that activity. The NDV F protein contains two heptad repeat motifs which have been shown by site-directed mutagenesis to be critical for fusion (R. Buckland et al., J. Gen. Virol. 73:1703-1707, 1992; T. Sergel-Germano et al., J. Virol. 68:7654-7658, 1994; J. Reitter et al., J. Virol. 69:5995-6004, 1995). Heptad repeat motifs mediate protein-protein interactions by enabling the formation of coiled coils. Upon analysis of the stalk region of the NDV HN protein, we identified two heptad repeats. Secondary structure analysis of these repeats suggested the potential for these regions to form alpha helices. To investigate the importance of this sequence motif for fusion promotion, we mutated the hydrophobic a-position amino acids of each heptad repeat to alanine or methionine. In addition, hydrophobic amino acids in other positions were also changed to alanine. Every mutant protein retained levels of attachment activity that was greater than or equal to the wild-type protein activity and bound to conformation-specific monoclonal as well as polyclonal antisera. Neuraminidase activity was variably affected. Every mutation, however, showed a dramatic decrease in fusion promotion activity. The phenotypes of these mutant proteins indicate that individual amino acids within the heptad repeat region of the stalk domain of the HN protein are important for the fusion promotion activity of the protein. These data are consistent with the idea that the HN protein associates with the F protein via specific interactions between the heptad repeat regions of both proteins.

Alanine↗
PubMed2001

Serological status for Chlamydophila psittaci, Newcastle disease virus, avian polyoma virus, and Pacheco disease virus in scarlet macaws (Ara macao) kept in captivity in Costa Rica.

From 1998 to 1999, a total of 128 blood samples were collected from scarlet macaws (Ara macao), kept in captivity in 11 different aviaries located in six provinces of Costa Rica. The sera were examined for antibodies directed against Chlamydophila psittaci, Newcastle disease virus (NDV), avian polyoma virus (APV), and Pacheco disease virus (PDV). Testing by enzyme-linked immunosorbent assay (ELISA), showed 16 (12.39%) of the samples (n = 129) exhibited antibodies directed against C. psittaci. Employing haemagglutination inhibition tests for NDV antibodies, all of the samples were found to be negative. The prevalence of antibodies specific for APV was tested with a blocking ELISA and serum neutralization tests (SNT) and 12 of 128 samples (9.37%) were found to be positive with both tests. In SNT, two out of 128 samples (1.56%) were positive for PDV. This is the first description of the serological status in scarlet macaws in captivity in Costa Rica. The study demonstrates the absence of NDV antibodies in the birds investigated on one hand, but also indicates a health hazard for numerous avian species due to the risk of infections with C. psittaci, APV or PDV.

Animals↗
PubMed1995

Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein.

The paramyxovirus fusion proteins have a highly conserved leucine zipper motif immediately upstream from the transmembrane domain of the F1 subunit (R. Buckland and F. Wild, Nature [London] 338:547, 1989). To determine the role of the conserved leucines in the oligomeric structure and biological activity of the Newcastle disease virus (NDV) fusion protein, the heptadic leucines at amino acids 481, 488, and 495 were changed individually and in combination to an alanine residue. While single amino acid changes had little effect on fusion, substitution of two or three leucine residues abolished the fusogenic activity of the protein, although cell surface expression of the mutants was higher than that of the wild-type protein. Substitution of all three leucine residues with alanine did not alter the size of the fusion protein oligomer as determined by sedimentation in sucrose gradients. Furthermore, deletion of the C-terminal 91 amino acids, including the leucine zipper motif and transmembrane domain, resulted in secretion of an oligomeric polypeptide. These results indicate that the conserved leucines are not necessary for oligomer formation but are required for the fusogenic ability of the protein. When the polar face of the potential alpha helix was altered by nonconservative changes of serine to alanine (position 473), glutamic acid to lysine or alanine (position 482), asparagine to lysine (position 485), or aspartic acid to alanine (position 489), the fusogenic ability of the protein was not significantly disrupted. In addition, a double mutant (E482A,D489A) which removed negative charges along one side of the helix had negligible effects on fusion activity.

Amino Acid Sequence↗
PubMed1995

Detection of Newcastle disease virus in poultry vaccines using the polymerase chain reaction and direct sequencing of amplified cDNA.

In order to develop an in vitro method for the control of poultry vaccines for identity and the absence of extraneous agents, reverse transcription-polymerase chain reaction (RT-PCR) was applied for the detection of Newcastle disease virus (NDV). NDV vaccines were employed for the establishment of the method, using two primer pairs spanning the cleavage site of the F0 fusion protein coding sequence. Amplification of a specific cDNA segment was possible from live and inactivated, oil-adjuvanted NDV vaccines without prior treatment. The cDNA was characterized by restriction endonuclease digestion as well as by direct nucleotide sequencing. The RT-PCR was able to detect between 5 x 10(2) EID50 (in live vaccine preparations) and 10(5) EID50 or 0.056 haemagglutinating units of NDV (in inactivated vaccine preparations). In addition, live vaccine preparations were inactivated with beta-propiolactone (beta-PL). Amplified cDNA was obtained after treatment with 0.1% beta-PL, whereas at a concentration of 1% or 10% no specific bands were visible in the agarose gel. These results demonstrate the applicability of the method for the control of poultry vaccines for identity and for the absence of extraneous agents, and additionally allow a rapid characterization of the respective NDV strain.

Animals↗
PubMed1975

Protein metabolism during the steady state of Newcastle disease virus infection. I. Kinetics of amino acid and protein accumulation.

Pulse-chase experiments and studies on the effects of varying pulse lenghts on radioactive amino acid and protein accumulation have been carried out to evaluate several possible mechanisms for the inhibition in cellular protein accumulation during infection of chicken embryo cells by Newcastle disease virus. The inhibition is probably at the level of synthesis of cellular protein since no evidence for either increased degradation of protein or alterations in cellular permeability to protein was found in infected cultures. The magnitude of the reduction in the rate of cellular protein accumulation and consequently total protein accumulation depend upon the length of the radioisotopic labeling period. In contrast, the rate of viral protein accumulation is independent of the length of the labeling period. A double-label difference analysis of polyacrylamide gels was used in all of the kinetics studies to distinguish between viral and cellular protein accumulation. An unstable fraction which could be labeled with radioactive amino acids was detected in both infected and uninfected cultures. This material migrated mainly in the 50,000- to 60,000-dalton region of polyacrylamide gels, exhibited saturation kinetics during accumulation studies, and turned over rapidly during a chase. The relative amount of this fraction was not affected by infection. Gel analysis of the radioactive protein recovered from the medium from both infected and uninfected cultures revealed a major component with an apparent molecular weight of 33,000. None of the major viral polypeptides could be detected in the medium after a 30-min chase following a brief labeling period.

Amino Acids↗
PubMed1997

Early induction of proinflammatory cytokine and type I interferon mRNAs following Newcastle disease virus, poly [rI:rC], or low-dose LPS challenge of the mouse.

Numerous cytokines induce symptoms characteristic of the flu syndrome common to acute viral infections. To better characterize the cytokine mRNA profile associated with the early phase of this syndrome, we examined the induction of cytokine mRNAs in spleens of mice 1, 2, and 4 h following intraperitoneal inoculation of Newcastle disease virus (NDV). The reverse transcriptase-polymerase chain reaction was used to detect mRNAs for mouse proinflammatory cytokines [interleukin (IL)-1 alpha, IL-1 beta, IL-6, tumor necrosis factor-alpha (TNF-alpha), macrophage colony-stimulating factor (M-CSF), and interferon (IFN)-gamma] and type I IFNs (IFN-alpha 4 and IFN-beta). We observed a rapid (within 2 h) induction of most of these cytokine mRNAs in the mouse spleen following challenge with live NDV or the viral stimulant poly[rI:rC]. IL-1 beta, M-CSF, and IFN-gamma mRNAs were also induced by heat-inactivated NDV, suggesting the possibility of endotoxin contamination of the virus (confirmed by Limulus lysate assay). Examination of cytokine induction by comparable doses of lipopolysaccharide indicated that endotoxin contamination could account for the cytokine mRNA-inducing activity of the heat-inactivated virus. These studies point to a critical control (heat-inactivated virus) for viral cytokine studies. In addition, they indicate that certain cytokine mRNAs (IL-1 alpha, IL-6, M-CSF, IFN-gamma, IFN-alpha, and IFN-beta) are rapidly induced in the spleen when live virus is inoculated intraperitoneally, independently of contaminating endotoxin.

Animals↗
PubMed1998

Characterization of pathotype-specific epitopes of newcastle disease virus fusion glycoproteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and post-source decay sequencing.

Matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) was used to characterize the F2 polypeptide of the fusion (F) protein of an avirulent isolate (VRI 82-6409) of Newcastle disease virus (NDV) that was previously identified by immunochemical screening as having a variant cleavage activation sequence in its fusion protein precursor (F0). The major glycoform of the intact F2 polypeptide of the VRI 82-6409 isolate was 89 Da smaller than the F2 polypeptide of the avirulent V4 isolate of the Queensland strain of NDV. Analysis of AspN protease digests of the F2 polypeptides by MALDI/TOF-MS, with and without high-performance liquid chromatographic (HPLC) separation, showed this mass difference to be due to a combination of differences in the extents of glycosylation and an amino acid difference in the AspN peptides derived from the C-termini of the F2 polypeptides. Accuracies achieved in analysis of the AspN peptides allowed the identification of this amino acid difference as glutamic acid in the VRI 82-6409 isolate compared with glycine in the V4 isolate. Analysis of fragments formed by post-source decay (PSD) of ions of the C-terminal AspN peptides localized the difference to the C-terminal residues of the respective F2 polypeptides. The present study demonstrated that MALDI/TOF-MS is a highly effective technique for the characterization of NDV variants identified by immunochemical screening of pathotype-specific epitopes at the C-termini of their F2 polypeptides.

Amino Acid Sequence↗