%0 Journal Article %A Umino, Y. %A Kohama, T. %A Sato, T. A. %A Sugiura, A. %A Klenk, H.-D. %A Rott, R. %T 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 %D 1990 %J Journal of General Virology, %V 71 %N 5 %P 1189-1197 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-71-5-1189 %I Microbiology Society, %X 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. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-71-5-1189