scholarly journals THE RELATIONSHIP OF THE RECEPTORS OF A NEW STRAIN OF VIRUS TO THOSE OF THE MUMPS-NDV-INFLUENZA GROUP

1950 ◽  
Vol 91 (2) ◽  
pp. 177-184 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Egg White ◽  
The Other ◽  
Cellular Receptors ◽  
Relationship Of ◽  
The Relationship

The interrelationships of the cellular receptors and the hemagglutinin inhibitors of a new strain of virus (1233) to members of the mumps-Newcastle disease-influenza group have been investigated. It was found that strain. 1233 does not destroy the receptors or inhibitors of the other group, nor does the latter destroy 1233 receptors or inhibitor. The sole exception to this statement was a moderate destruction of 1233 inhibitor in egg white by Newcastle disease virus. The classification of strain 1233 was discussed in the light of this evidence, evidence which tends to place strain 1233 in a different category from that of any other strain of the MNI group.

Molecular classification of Newcastle disease virus based on degree of virulence

2014 ◽  
Author(s):  
Saleh Esmate Aly ◽  
Hanaa Ismail Elshazly ◽  
Ahmed Fouad Ali ◽  
Hussein Ali Hussein ◽  
Aboul Ella Hassanien ◽  
...  
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Molecular Classification

scholarly journals Mutated Form of the Newcastle Disease Virus Hemagglutinin-Neuraminidase Interacts with the Homologous Fusion Protein despite Deficiencies in both Receptor Recognition and Fusion Promotion

2004 ◽  
Vol 78 (10) ◽  
pp. 5299-5310 ◽  
Author(s):  
Jianrong Li ◽  
Edward Quinlan ◽  
Anne Mirza ◽  
Ronald M. Iorio
Keyword(s):  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Viral Entry ◽  
Newcastle Disease ◽  
Active Site ◽  
Specific Interaction ◽  
Cellular Receptors ◽  
Dimer Interface ◽  
F Protein ◽  
Receptor Recognition

ABSTRACT The Newcastle disease virus (NDV) hemagglutinin-neuraminidase (HN) protein mediates attachment to cellular receptors. The fusion (F) protein promotes viral entry and spread. However, fusion is dependent on a virus-specific interaction between the two proteins that can be detected at the cell surface by a coimmunoprecipitation assay. A point mutation of I175E in the neuraminidase (NA) active site converts the HN of the Australia-Victoria isolate of the virus to a form that can interact with the F protein despite negligible receptor recognition and fusion-promoting activities. Thus, I175E-HN could represent a fusion intermediate in which HN and F are associated and primed for the promotion of fusion. Both the attachment and fusion-promoting activities of this mutant HN protein can be rescued either by NA activity contributed by another HN protein or by a set of four substitutions at the dimer interface. These substitutions were identified by the evaluation of chimeras composed of segments from HN proteins derived from two different NDV strains. These findings suggest that the I175E substitution converts HN to an F-interactive form, but it is one for which receptor binding is still required for fusion promotion. The data also indicate that the integrity of the HN dimer interface is critical to its receptor recognition activity.

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