Hemagglutinating and fusogenic activities of Newcastle disease virus: studies on receptor binding specificity and pH-induced conformational changes.
Vaccinal and wild strains of Newcastle Disease virus (NDV) were analyzed for cell receptor binding and fusogenic biological properties associated with their HN (hemagglutinin-neuraminidase) and F (fusion protein) surface structures respectively. The evaluation of the biological activities of HN and F was carried out respectively by determination of hemagglutinating titers and hemolysis percentages, using erythrocytes from various animal origins at different pH values. Significant differences in hemagglutination titers for some strains of NDV were detected, when interacting with goose, sheep, guinea-pig and human "O" group erythrocytes at neutral pH. Diversity of hemolysis percentages was observed between different NDV strains at acid pH. These analysis were developed to evaluate particular aspects of the actual influence of the receptor specificity and pH on the receptor binding and fusogenic processes of Newcastle Disease viruses.
Couceiro
E S
ES
Departamento de Virologia, Instituto de Microbiologia, CCS-UFRJ Cidade Universitária, Rio de Janeiro, Brasil.
Couceiro
J N
JN
Cabral
M C
MC
D000818:Animals; D006168:Guinea Pigs; D015707:HN Protein / Q000502:physiology*; D006387:Hemagglutination, Viral; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009522:Newcastle disease virus / Q000502:physiology*; D012756:Sheep; D013045:Species Specificity; D014760:Viral Fusion Proteins / Q000502:physiology*
D015707:HN Protein; D014760:Viral Fusion Proteins