Studies on Newcastle Disease: IX. Effect of Newcastle Disease Virus on the Volume of Chicken Red Blood Cells

1950 ◽  
Vol 53 (4) ◽  
pp. 488
Author(s):  
L. D. Bushnell ◽  
L. E. Erwin
2014 ◽  
Vol 2014 ◽  
pp. 1-4 ◽  
Author(s):  
Egbal Sidahmed Abdelrahim Bilal ◽  
Iman Mohammed Elnasri ◽  
Aymen Mohamed Alhassan ◽  
Khalda Abdelaziz Khalifa ◽  
Jedddha Ibrahim Elhag ◽  
...  

The biological properties and pathogenicity of seven Newcastle disease virus field isolates were studied. These isolates were recovered from different outbreaks in Sudan (5 from chickens and 2 from pigeons) during 2008–2013. Based on intracerebral pathogenicity index, four NDV isolates were characterized as velogenic (their ICPI ranged 2.0–1.6) and three isolates were characterized as mesogenic (ICPI ranged 1.2–1.3). The mean death time for all isolates ranged from 54 to 76.8 hours. The elution time of the viruses from chicken erythrocytes and the ability to haemagglutinate mammalian red blood cells differed considerably in their reactions.


1948 ◽  
Vol 88 (2) ◽  
pp. 233-240 ◽  
Author(s):  
F. B. Bang

The application of the 50 per cent embryo mortality to a study of the virus of Newcastle is described. It has been evaluated by a series of duplicate titrations of the same sample of virus. In seven such titrations the largest difference between the two was 10–0.4. It is therefore believed that a difference of 0.6 log is probably significant and of 1.0 log almost certainly significant. This would mean that we can almost certainly detect a loss of 90 per cent of activity. Neither temperature of incubation nor route of inoculation in the test embryos had consistent effect on the measurement of virus activity. The effect of increasing age of the incubated embryo, from 10 days up to 16 days, is slight and inconsistent. The addition of chicken red blood cells to a dilution of virus may lower the titer of the preparation, but the change is not sufficient to be of importance in the routine handling of the virus.


1966 ◽  
Vol 21 (3) ◽  
pp. 254-260 ◽  
Author(s):  
R. Drzeniek ◽  
M. S. Saber ◽  
R. Rott

After erythrocytes had been treated with NDV, antigens of the Forssman and mononucleosis type could be demonstrated on their surface. The Forssman antigen was found to be either transfered by the virus to the surface of the erythrocytes or unmasked by splitting off sialic acid from chicken red cells. The mononucleosis antigen could only be transfered to the erythrocytes by NDV. Both antigens demonstrable in NDV, proved to be parts of the normal, host-specific component of the virus. The mononucleosis antigen of NDV was similar to that in bovine erythrocytes, but different from the one in sheep red blood cells.


2002 ◽  
Vol 76 (24) ◽  
pp. 12622-12633 ◽  
Author(s):  
Lori W. McGinnes ◽  
Kathryn Gravel ◽  
Trudy G. Morrison

ABSTRACT Conformational changes in the Newcastle disease virus (NDV) fusion (F) protein during activation of fusion and the role of HN protein in these changes were characterized with a polyclonal antibody. This antibody was raised against a peptide with the sequence of the amino-terminal half of the F protein HR1 domain. This antibody immunoprecipitated both F0 and F1 forms of the fusion protein from infected and transfected cell extracts solubilized with detergent, and precipitation was unaffected by expression of the HN protein. In marked contrast, this antibody detected significant conformational differences in the F protein at cell surfaces, differences that depended upon HN protein expression. The antibody minimally detected the F protein, either cleaved or uncleaved, in the absence of HN protein expression. However, when coexpressed with HN protein, an uncleaved mutant F protein bound the anti-HR1 antibody, and this binding depended upon the coexpression of specifically the NDV HN protein. When the cleaved wild-type F protein was coexpressed with HN protein, the F protein bound anti-HR1 antibody poorly although significantly more than F protein expressed alone. Anti-HR1 antibody inhibited the fusion of R18 (octadecyl rhodamine B chloride)-labeled red blood cells to syncytia expressing HN and wild-type F proteins. This inhibition showed that fusion-competent F proteins present on surfaces of syncytia were capable of binding anti-HR1. Furthermore, only antibody which was added prior to red blood cell binding could inhibit fusion. These results suggest that the conformation of uncleaved cell surface F protein is affected by HN protein expression. Furthermore, the cleaved F protein, when coexpressed with HN protein and in a prefusion conformation, can bind anti-HR1 antibody, and the anti-HR1-accessible conformation exists prior to HN protein attachment to receptors on red blood cells.


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