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PubMed1982

Topological location and biological significance of phospholipids in the membrane of Newcastle disease virus. Hydrolysis of phospholipids in intact virion with pure phospholipases A2, C, and D.

The composition, topological distribution and biological significance of phospholipids in the membrane of Newcastle disease virus (NDV) grown in embryonated chicken eggs were investigated. Phosphatidylethanolamine and sphingomyelin were the predominant phospholipids in NDV membrane. The location of phospholipids in the lipid bilayer of the membrane was studied by assessing their reactivities with highly purified phospholipase A2 (Agkistrodon halys blomhoffi) and phospholipase D (Streptomyces chromofuscus), and the biological role of membrane phospholipids was also investigated by using pure phospholipases A2, C (Bacillus cereus) and D. Choline-containing phospholipids were found predominantly in the outer layer of the membrane. The inner layer was composed mainly of aminoglycerophospholipids, though a fair amount of them also appeared to be located in the outer half of the bilayer. When intact virion was treated with phospholipase C, marked decreases in hemolytic activity and infectivity mediated by viral fusion (F) glycoprotein were observed, but hemagglutinating and neuraminidase activities did not change significantly. Apparently complete hydrolysis of phospholipids in the outer half of the lipid bilayer with phospholipase D caused about 22% decrease in the original hemolytic activity. On the other hand, when all phosphatidylcholine and aminoglycerophospholipids in the outer half of the viral membrane were hydrolyzed with purified phospholipase A2, no significant change in viral hemolytic activity or morphology was detected. No marked change of hemagglutinating and neuraminidase activities was detected on treatment of NDV with phospholipases A2 and D. The above results suggest that the integrity of fatty acid ester of glycerophospholipids in NDV membrane is not essential for the manifestation of viral activities, though polar groups of the phospholipids in the outer half of the membrane may be involved in the function of fusion (F) glycoprotein, but not in that of hemagglutinating and neuraminidase (HN) glycoprotein of NDV.

Hydrolysis↗
PubMedDate not supplied

A method to rapidly convert Newcastle disease virus and infectious bronchitis virus ImmunoComb scores into conventional hemagglutination-inhibition titers.

ImmunoComb scores are highly correlated to hemagglutination-inhibition (HI) titers against infectious bronchitis virus and Newcastle disease virus. Statistical calculations permit using an individual COMBSCORE to predict the corresponding HI titer value. Tables are presented to facilitate the transformation of COMBSCORES into HI titers.

Antibodies, Viral↗
PubMed2003

Positive identification of Newcastle disease virus vaccine strains and detection of contamination in vaccine batches by restriction site analysis of the matrix protein gene.

Twelve vaccine batches prepared from avirulent vaccine strains of Newcastle disease virus produced by seven manufacturers were identified by analysis of the matrix (M) protein gene with restriction enzymes MboI and HinfI. The analyses have revealed the presence of the strain indicated by the manufacturers (namely B-1, LaSota or Ulster 2C), except in one case when the vaccine contained strain V4 Queensland instead of VGGA as indicated. In addition, several batches of both monovalent and combined vaccines containing strain LaSota of the same company consistently disclosed contamination with strain B-1. The mixed nature of the preparations was verified not only by the dual patterns of restriction fragments but also by separating the two components and identifying them individually. Restriction analysis of the M gene, by allowing positive identification of each of the lentogenic vaccine strains, should provide an improvement in controlling vaccine batches by revealing homologous contaminants or exchange of the vaccine strain.

Animals↗
PubMed1994

Mutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion.

Nonconservative mutations were introduced by site-specific mutagenesis into the fusion peptide and the adjacent heptad repeat region of the fusion protein of Newcastle disease virus in order to determine the role of both regions in the fusion activity of the protein. Mutations in both regions that allowed for proper folding and intracellular transport of the protein blocked the fusion activity of the protein when assayed in the presence of the hemagglutinin-neuraminidase protein.

Amino Acid Sequence↗
PubMedDate not supplied

Failure to demonstrate viscerotropic velogenic Newcastle disease in psittacine birds in the Republic of the Philippines.

Birds on the islands of Luzon, Mindanao, and Palawan in the Republic of the Philippines were surveyed for viscerotropic velogenic Newcastle disease (VVND). Virus isolation was attempted on 728 cloacal samples from native and exotic psittacine birds, non-psittacine birds, and domestic chickens and ducks. A VVND virus isolate was obtained from a single domestic chicken that had exhibited ocular discharge and diarrhea 3 days before sampling. All other birds were negative for VVND.

Animals↗
PubMed1984

Newcastle disease virus: the effect of monoclonal antibody in the overlay on virus penetration and the immunoselection of variants.

Monoclonal antibody to the haemagglutinin-neuraminidase or the fusion glycoprotein of Newcastle disease virus blocked virus penetration which otherwise occurred within 90 s of the temperature being increased from 4 degrees C to 37 degrees C. These antibodies regularly immunoselected variant plaques only when incorporated into the agarose overlay. Variant viruses then formed plaques whereas the growth of non-neutralized normal virus was suppressed.

Animals↗
PubMed2002

Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion.

We recently reported the first crystal structure of a paramyxovirus hemagglutinin-neuraminidase (HN) from Newcastle disease virus. This multifunctional protein is responsible for binding to cellular sialyl-glycoconjugate receptors, promotion of fusion through interaction with the second viral surface fusion (F) glycoprotein, and processing progeny virions by removal of sialic acid from newly synthesized viral coat proteins. Our structural studies suggest that HN possesses a single sialic acid recognition site that can be switched between being a binding site and a catalytic site. Here we examine the effect of mutation of several conserved amino acids around the binding site on the hemagglutination, neuraminidase, and fusion functions of HN. Most mutations around the binding site result in loss of neuraminidase activity, whereas the effect on receptor binding is more variable. Residues E401, R416, and Y526 appear to be key for receptor binding. The increase in fusion promotion seen in some mutants that lack receptor binding activity presents a conundrum. We propose that in these cases HN may be switched into a fusion-promoting state through a series of conformational changes that propagate from the sialic acid binding site through to the HN dimer interface. These results further support the single-site model and suggest certain residues to be important for the triggering of fusion.

Amino Acids↗
PubMed1991

Complementation between avirulent Newcastle disease virus and a fusion protein gene expressed from a retrovirus vector: requirements for membrane fusion.

The cDNA derived from the fusion gene of the virulent AV strain of Newcastle disease virus (NDV) was expressed in chicken embryo cells by using a retrovirus vector. The fusion protein expressed in this system was transported to the cell surface and was efficiently cleaved into the disulfide-linked F1-F2 form found in infectious virions. The cells expressing the fusion gene grew normally and could be passaged many times. Monolayers of these cells would plaque, in the absence of trypsin, avirulent NDV strains (strains which encode a fusion protein which is not cleaved in tissue culture). Fusion protein-expressing cells would not fuse if mixed with uninfected cells or uninfected cells expressing the hemagglutinin-neuraminidase (HN) protein. However, the fusion protein-expressing cells, if infected with avirulent strains of NDV, would fuse with uninfected cells, suggesting that fusion requires both the fusion protein and another viral protein expressed in the same cell. Fusion was also seen after transfection of the HN protein gene into fusion protein-expressing cells. Thus, the expressed fusion protein gene is capable of complementing the virus infection, providing an active cleaved fusion protein required for the spread of infection. However, the fusion protein does not mediate cell fusion unless the cell also expresses the HN protein. Fusion protein-expressing cells would not plaque influenza virus in the absence of trypsin, nor would influenza virus-infected fusion protein-expressing cells fuse with uninfected cells. Thus, the influenza virus HA protein will not substitute for the NDV HN protein in cell-to-cell fusion.

Animals↗
PubMed2004

Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus haemagglutinin-neuraminidase glycoprotein: a mutational and kinetic study.

Mutations were generated in residues at the putative catalytic site of the haemagglutinin-neuraminidase (HN) protein of Newcastle disease virus Clone 30 strain (Arg498, Glu258, Tyr262, Tyr317 and Ser418) and their effects on its three associated activities were studied. Expression of the mutant proteins at the surface of HeLa cells was similar to that of the wild-type. Sialidase, receptor-binding and fusion-promotion activities were affected to different degrees for all mutants studied. Mutant Arg498Lys lost most of its sialidase activity, although it retained most of the receptor-binding activity, suggesting that, for the former activity, besides the presence of a basic residue, the proximity to the substrate molecule is also important, as Lys is shorter than Arg. Proximity also seems to be important in substrate recognition, since Tyr262Phe retained most of its sialidase activity while Tyr262Ser lost most of it. Also, Ser418Ala displayed most of the wild-type sialidase activity. However, a kinetic and thermodynamic study of the sialidase activity of the Tyr262Ser and Ser418Ala mutants was performed and revealed that the hydroxyl group of these residues also plays an important role in catalysis, since such activity was much less effective than that of the wild-type and these mutations modified their activation energy for sialidase catalysis. The discrepancy of the modifications in sialidase and receptor-binding activities in the mutants analysed does not account for the topological coincidence of the two sites. These results also suggest that the globular head of HN protein may play a role in fusion-promotion activity.

Amino Acid Substitution↗
PubMed2003

Newcastle disease virus (NDV)-based assay demonstrates interferon-antagonist activity for the NDV V protein and the Nipah virus V, W, and C proteins.

We have generated a recombinant Newcastle disease virus (NDV) that expresses the green fluorescence protein (GFP) in infected chicken embryo fibroblasts (CEFs). This virus is interferon (IFN) sensitive, and pretreatment of cells with chicken alpha/beta IFN (IFN-alpha/beta) completely blocks viral GFP expression. Prior transfection of plasmid DNA induces an IFN response in CEFs and blocks NDV-GFP replication. However, transfection of known inhibitors of the IFN-alpha/beta system, including the influenza A virus NS1 protein and the Ebola virus VP35 protein, restores NDV-GFP replication. We therefore conclude that the NDV-GFP virus could be used to screen proteins expressed from plasmids for the ability to counteract the host cell IFN response. Using this system, we show that expression of the NDV V protein or the Nipah virus V, W, or C proteins rescues NDV-GFP replication in the face of the transfection-induced IFN response. The V and W proteins of Nipah virus, a highly lethal pathogen in humans, also block activation of an IFN-inducible promoter in primate cells. Interestingly, the amino-terminal region of the Nipah virus V protein, which is identical to the amino terminus of Nipah virus W, is sufficient to exert the IFN-antagonist activity. In contrast, the anti-IFN activity of the NDV V protein appears to be located in the carboxy-terminal region of the protein, a region implicated in the IFN-antagonist activity exhibited by the V proteins of mumps virus and human parainfluenza virus type 2.

Animals↗
PubMed1988

Temperature-sensitive mutants of Newcastle disease virus altered in HN glycoprotein size, stability, or antigenic maturity.

It has been suggested that the 11 group B, C, and BC temperature-sensitive (ts) mutants of Newcastle disease virus (NDV), strain Australia-Victoria (AV-WT), have lesions in the gene for the hemagglutinin/neuraminidase glycoprotein (HN), and that complementation between groups B and C is intracistronic. Virions produced by these mutants even at permissive temperature contain greatly reduced amounts of HN, and the accompanying hemagglutinating and neuraminidase functions. To explore the basis for decreased HN incorporation into virions and the temperature sensitivity of these mutants, infected chick embryo cells were examined for changes in HN characteristics. The HN of two of the mutants was clearly altered in electrophoretic migration rates in both virions and infected cells. The migrational differences were not due to differences in glycosylation because altered migration rates were also observed in the presence of tunicamycin. In all cases, cells infected by these mutants produced as much HN as did AV-WT-infected cells, but the HN of six of these mutants was metabolically unstable. All of the mutants, including those with metabolically stable HN, exhibited greatly restricted ability to convert HN to an antigenically reactive form, indicating an early block in processing. For most of these mutants, the neuraminidase activities of infected cells were somewhat temperature sensitive, but the production of hemadsorbing activities on cell surfaces was not temperature sensitive. In contrast, the hemadsorbing and neuraminidase activities of cells infected by one mutant, BC2, were temperature sensitive, probably a reflection of the previously described extreme thermolability of the HN of this mutant. The relationship between these mutant characteristics, their temperature sensitivity and the virion phenotypes, is discussed. The data presented here confirm the assignment of these 11 group B, C, and BC mutants to defects in HN and begin to separate them into groups with different characteristics.

Animals↗
PubMed1994

Glycosylation within an antigenic site on the HN glycoprotein of Newcastle disease virus interferes with its role in the promotion of membrane fusion.

The binding of monoclonal antibodies to antigenic site 3 on the hemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus neutralizes viral infectivity and prevents syncytium formation by a mechanism other than the prevention of viral attachment. The virus can escape neutralization by these antibodies by the addition of an N-glycan at a site introduced by a D287N mutation in HN. The variant has significantly reduced ability to induce fusion from within, the mode of fusion promoted by the viral glycoproteins deposited on the cell surface late in infection. Conversely, and unlike the parent virus, the variant has acquired the ability to promote fusion from without, the mode of fusion directly mediated by input virions at high multiplicity. This finding is consistent with different roles for the HN protein in virion-cell and cell-cell fusion. D287N-mutated HN with its additional N-glycan shows a markedly reduced ability, compared to wild-type HN, to complement the viral fusion protein in the promotion of fusion in a BHK cell transient expression system. This confirms that the addition of an N-glycan in HN antigenic site 3 and the deficiency in syncytium formation are causally related. Moreover, no alteration in cell surface expression, hemadsorption, or neuraminidase activity was detected in the mutated protein. This monoclonal antibody-selected mutation suggests that a fusion-related function, secondary to receptor recognition, may be defined by the globular head of the HN spike. However, D287C or D287S-mutated HN is as effective as the wild-type protein in the promotion of fusion in the coexpression system. This suggests that the diminished fusogenicity of the D287N-mutated protein is probably due to a more global effect of glycosylation in site 3 rather than an alteration at the amino acid level.

Base Sequence↗
PubMedDate not supplied

Agglutination-separation reactions of red blood cells sensitized with Newcastle disease virus: quantities, agglutination characteristics, and serology of altered virus and HN spikes released following neuraminidase reactivation.

Red blood cells (RBC) become sensitized following the elution of strain 575 Newcastle disease virus (NDV). The neuraminidase (NA) in the haemagglutinin (HA)-sialic acid configuration is inactive. The HA on sensitized RBC agglutinates normal RBC. The sialic acid on normal RBC initiated reactivation of the NA-a newly described function. Then normal-sensitized RBC agglomerates separated at 37 degrees C in the irreversible agglutination-separation (AS) reactions. With separation the AS products. HN spikes (150-200 kDa) and altered NDV, which contain fewer HN spikes than intact allantoic NDV, were removed from the sensitized RBC and the NDV membrane. Extraction of HN spikes from the membrane required more sialic acid than the removal of AS products from RBC. Thus 2 reactions were delineated for the orderly removal. Amounts of each released AS product suggest the source of the HN spikes. AS reactions and ether treatment of NDV increased the HA titres up to 19.2 fold. HA-sialic acid configurations were estimated by the amounts of normal RBC agglutinated by sensitized RBC and also by agglutination with fetuin. Elution of B1 vaccine, HN spikes from ether-treated NDV as well as AS products separated on sephadex resulted in incompletely sensitized RBC; fewer configurations were titrated with normal RBC; all failed to respond to anti-NA antibody. In contrast, sensitized RBC or suspensions of 575 NDV, but not the B1 vaccine strain, responded to both anti-NA and anti-HA antibody. Sensitization, slow elution, and responding to anti-NA antibody, which was accompanied by fluorescent foci on sensitized RBC, required intact NDV and the infrequent HA-sialic acid configuration. The NA was inactive for the HA-sialic acid configuration but cleaved fetuin, indicating substrate specificity. An inactive NA would allow time for fusion and NDV penetration rather than elution by an active NA early in NDV infection.

Animals↗