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J Gen Virol 71 (1990), 1189-1197; DOI 10.1099/0022-1317-71-5-1189
© 1990 Society for General Microbiology
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Monoclonal Antibodies to Three Structural Proteins of Newcastle Disease Virus: Biological Characterization with Particular Reference to the Conformational Change of Envelope Glycoproteins Associated with Proteolytic Cleavage

Y. Umino1, T. Kohama1, T. A. Sato1, A. Sugiura1, H.-D. Klenk2 and R. Rott3

1 Department of Measles Virus, National Institute of Health, Gakuen, 4-7-1, Musashimurayama, Tokyo 190-12, Japan
2 Institut für Virologie, Philipps-Universität Marburg
and3 Institut für Virologie, Justus-Liebig-Universität Giessen, F.R.G.

Monoclonal antibodies (MAbs) to the haemagglutinin—neuraminidase (HN), fusion (F) and matrix (M) proteins of Newcastle disease virus were prepared and characterized. At least three non-overlapping or partially overlapping antigenic sites were delineated on the HN, three on the F and three on the M proteins by competitive binding assays. Antigenic sites on the HN and F proteins roughly represented functional domains defined by serological tests. Two antigenic sites on the F protein were involved in virus neutralizing and haemolysis-inhibiting activity. These antigenic determinants were readily affected by treatment with certain surfactants and acetone. Proteolytic cleavage of the HN and F proteins was associated with conformational change, revealed by altered reactivity with MAbs and by altered topological arrangements of some epitopes. None of the anti-M MAbs inhibited any biological activities of the virus.

Received 26 September 1989; accepted 24 January 1990.


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