scholarly journals Safety and Clinical Usage of Newcastle Disease Virus in Cancer Therapy

2011 ◽  
Vol 2011 ◽  
pp. 1-13 ◽  
Author(s):  
Han Yuen Lam ◽  
Swee Keong Yeap ◽  
Mehdi Rasoli ◽  
Abdul Rahman Omar ◽  
Khatijah Yusoff ◽  
...  
Keyword(s):  
Cancer Therapy ◽  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Human Tumor ◽  
Wild Type ◽  
Anticancer Effect ◽  
Human Tumor Cells ◽  
Immunological Effects ◽  
Oncolytic Effect

Newcastle disease virus (NDV) is an avian virus that causes deadly infection to over 250 species of birds, including domestic and wild-type, thus resulting in substantial losses to the poultry industry worldwide. Many reports have demonstrated the oncolytic effect of NDV towards human tumor cells. The interesting aspect of NDV is its ability to selectively replicate in cancer cells. Some of the studies have undergone human clinical trials, and favorable results were obtained. Therefore, NDV strains can be the potential therapeutic agent in cancer therapy. However, investigation on the therapeutic perspectives of NDV, especially human immunological effects, is still ongoing. This paper provides an overview of the current studies on the cytotoxic and anticancer effect of NDV via direct oncolysis effects or immune stimulation. Safety of NDV strains applied for cancer immunotherapy is also discussed in this paper.

Newcastle disease virus selectively kills human tumor cells

1992 ◽  
Vol 52 (5) ◽  
pp. 448-453 ◽  
Author(s):  
Kirk W. Reichard ◽  
Robert M. Lorence ◽  
Christopher J. Cascino ◽  
Mark E. Peeples ◽  
Robert J. Walter ◽  
...  
Keyword(s):  
Newcastle Disease Virus ◽  
Tumor Cells ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Human Tumor ◽  
Human Tumor Cells

scholarly journals Oncolytic effect of wild-type Newcastle disease virus isolates in cancer cell lines in vitro and in vivo on xenograft model

PLoS ONE ◽  
2018 ◽  
Vol 13 (4) ◽  
pp. e0195425 ◽  
Author(s):  
Kseniya S. Yurchenko ◽  
Peipei Zhou ◽  
Anna V. Kovner ◽  
Evgenii L. Zavjalov ◽  
Lidiya V. Shestopalova ◽  
...  
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Cell Lines ◽  
Newcastle Disease ◽  
Xenograft Model ◽  
Wild Type ◽  
Virus Isolates ◽  
Oncolytic Effect

Newcastle disease virus therapy of human tumor xenografts: antitumor effects of local or systemic administration

2001 ◽  
Vol 172 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Anan Phuangsab ◽  
Robert M. Lorence ◽  
Kirk W. Reichard ◽  
Mark E. Peeples ◽  
Robert J. Walter
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Human Tumor ◽  
Systemic Administration ◽  
Antitumor Effects ◽  
Human Tumor Xenografts ◽  
Tumor Xenografts

scholarly journals Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus

1990 ◽  
Vol 10 (2) ◽  
pp. 449-457
Author(s):  
C Wilson ◽  
R Gilmore ◽  
T Morrison
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Cytoplasmic Domain ◽  
Mutant Protein ◽  
Membrane Insertion ◽  
Type Ii ◽  
Wild Type ◽  
Amino Terminal ◽  
Nascent Chain

The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus (NDV) is a type II glycoprotein oriented in the plasma membrane with its amino terminus in the cytoplasm and its carboxy terminus external to the cell. We have previously shown that the membrane insertion of HN protein requires signal recognition particle SRP, occurs cotranslationally, and utilizes the same GTP-dependent step that has been described for secretory proteins, type I proteins, and multispanning proteins (C. Wilson, R. Gilmore, and T. Morrison, Mol. Cell. Biol. 7:1386-1392, 1987; C. Wilson, T. Connolly, T. Morrison, and R. Gilmore, J. Cell Biol. 107:69-77, 1988). The role of the amino-terminal cytoplasmic domain in the faithful membrane insertion of this type II protein was explored by characterizing the membrane integration of a mutant lacking 23 of the 26 amino acids of the cytoplasmic domain. The mutant protein was able to interact with SRP, resulting in translation inhibition, membrane targeting, and membrane translocation, but the efficiency of translocation was considerably lower than for the wild-type HN protein. In addition, a significant proportion of the mutant protein synthesized in the presence of SRP and microsomal membranes was associated with the membrane in an EDTA- and alkali-insensitive manner yet integrated into membranes with its carboxy-terminal domain on the cytoplasmic side of membrane vesicles. Membrane-integrated molecules with this reverse orientation were not detected when the mutant protein was synthesized in the absence of SRP or a functional SRP receptor. Truncated mRNAs encoding amino-terminal segments of the wild-type and mutant proteins were translated to prepare ribosomes bearing arrested nascent chains. The arrested mutant nascent chain, in contrast to the wild-type nascent chain, was also able to insert into membranes in a GTP- and SRP-independent manner. Results suggest that the cytoplasmic domain plays a role in the proper membrane insertion of this type II glycoprotein.

scholarly journals Effect of Cleavage Mutants on Syncytium Formation Directed by the Wild-Type Fusion Protein of Newcastle Disease Virus

1998 ◽  
Vol 72 (5) ◽  
pp. 3789-3795 ◽  
Author(s):  
Zengji Li ◽  
Theresa Sergel ◽  
Enal Razvi ◽  
Trudy Morrison
Keyword(s):  
Amino Acids ◽  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Syncytium Formation ◽  
Dominant Negative ◽  
Wild Type ◽  
F Protein ◽  
Type Protein ◽  
Wild Type Protein

ABSTRACT The effects of Newcastle disease virus (NDV) fusion (F) glycoprotein cleavage mutants on the cleavage and syncytium-forming activity of the wild-type F protein were examined. F protein cleavage mutants were made by altering amino acids in the furin recognition region (amino acids 112 to 116) in the F protein of a virulent strain of NDV. Four mutants were made: Q114P replaced the glutamine residue with proline; K115G replaced lysine with glycine; double mutant K115G, R113G replaced both a lysine and an arginine with glycine residues; and a triple mutant, R112G, K115G, F117L, replaced three amino acids to mimic the sequence found in avirulent strains of NDV. All mutants except Q114P were cleavage negative and fusion negative. However, addition of exogenous trypsin cleaved all mutant F proteins and activated fusion. As expected for an oligomeric protein, the fusion-negative mutants had a dominant negative phenotype: cotransfection of wild-type and mutant F protein cDNAs resulted in an inhibition of syncytium formation. The presence of the mutant F protein did not inhibit cleavage of the wild-type protein. Furthermore, evidence is presented that suggests that the mutant protein and the wild-type protein formed heterooligomers. By measuring the syncytium-forming activity of the wild-type protein at various ratios of expression of mutant and wild-type protein, results were obtained that are most consistent with the notion that the size of the functionally active NDV F protein in these assays is a single oligomer, likely a trimer. That a larger oligomer, containing a mix of both wild-type and mutant F proteins, has partial activity cannot, however, be ruled out.

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

2004 ◽  
Vol 85 (7) ◽  
pp. 1981-1988 ◽  
Author(s):  
Laura Ferreira ◽  
Isabel Muñoz-Barroso ◽  
Fernando Marcos ◽  
Valery L. Shnyrov ◽  
Enrique Villar
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Receptor Binding ◽  
Newcastle Disease ◽  
Binding Activity ◽  
Hydroxyl Group ◽  
Wild Type ◽  
Basic Residue ◽  
Mutant Proteins ◽  
Sialidase Activity

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.

Sign in / Sign up

Export Citation Format

Share Document