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J Gen Virol 67 (1986), 1531-1542; DOI 10.1099/0022-1317-67-8-1531
© 1986 Society for General Microbiology
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Characterization of Four Parainfluenza Virus Type 3 Proteins by Use of Monoclonal Antibodies

Robert Rydbeck1, Claes Örvell1,2,, Arthur Löve1 and Erling Norrby1

1 Department of Virology, Karolinska Institute, School of Medicine, c/o SBL, S-105 21 Stockholm
and2 Department of Virology, National Bacteriological Laboratory, S-105 21 Stockholm, Sweden

Monoclonal antibodies directed against four structural components of the ATCC strain C243 of parainfluenza virus type 3 were produced. The specific reaction of the antibodies with individual structural components was determined by radioimmune precipitation assay. In the collection of monoclonal antibodies, 21 reacted with the haemagglutinin-neuraminidase (HN) glycoprotein (mol. wt. 72000), eight with the fusion (F) glycoprotein (mol. wt. 64000), 27 with the nucleocapsid (NP) protein (mol. wt. 69000) and 24 with the matrix (M) protein (mol. wt. 40000). The F-specific monoclonal antibodies precipitated two proteins which were interpreted to represent intact F protein and the large cleavage product F1 (mol. wt. 52000). The numbers of epitopes were determined in a competition ELISA with the monoclonal antibodies. The epitopes found were six for the HN, two for the F, six for the NP and six for the M protein. The six groups of antibodies reacting with different epitopes on the HN molecule showed varying capacities to inhibit biological activities. Two exhibited high neutralization (NT), haemagglutination inhibition (HI) and haemolysis inhibition (HLI) activity. Three groups had somewhat lower NT, lower HI and no detectable HLI activity. One group showed no activity in these tests. Of the eight monoclonal antibodies directed to the F protein two had demonstrable HLI activity.

Keywords: parainfluenza type 3 virus, monoclonal antibodies, proteins, structural

Received 29 January 1986; accepted 23 April 1986.




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Copyright © 1986 by the Society for General Microbiology.