Characterization of Human Parainfluenza Viruses. I. The Structural Proteins of Parainfluenza Virus 2 and their Synthesis in Infected Cells

Comparison between Parainfluenza Virus Type 2 and Simian Virus 5: Monoclonal Antibodies Reveal Major Antigenic Differences

“…3) the overall pattern was very similar and clearly very distinct from that of SV5 (Randall et al, 1987). Thus, in general agreement with other published data on the polypeptides of PF-2 (Goswami & Russell, 1982;Cowley & Barry, 1983), SDS-PAGE analysis showed marked differences in the apparent Mr values of the L, HN, NP and F proteins of SV5 and PF-2, the P and M proteins having similar electrophoretic mobilities. We had previously shown that there was little variation between different human, dog or monkey isolates of SV5 either in terms of the apparent Mr of the virion proteins or in terms of their ability to react with the pool of SV5 MAbs used in this The autoradiogram shown in (a) represents an SDS-PAGE gel exposed for 2 weeks; that shown in (b) was exposed for 10 weeks.…”

Parainfluenza Virus Type 2 Haemagglutinin-Neuraminidase Glycoprotein Characterized with Monoclonal Antibodies

“…This study confirms that the 72K to 84K protein described by other workers (Cowley & Barry, 1983;Goswami & Russell, 1983;Ito et al, 1987b) is the HN protein. A band of 165K was also precipitated by the MAbs (Fig.…”

“…It causes mild upper respiratory tract disease in adults but can produce more severe symptoms in children, in whom interstitial pneumonia and croup occasionally occur (Glezen et al, 1982). PIV2 is a member of the Paramyxoviridae (Kingsbury et al, 1978) and has been demonstrated to possess six structural proteins, the large, haemagglutinin-neuraminidase (HN), fusion (F), phospho-, nucleocapsid (NP) and matrix proteins (Cowley & Barry, 1983 ;Goswami & Russell, 1982). The two envelope surface glycoproteins HN and F are, by analogy to other paramyxoviruses, believed to be responsible for attachment of virions to cells and for fusion of viral and cellular membranes (Choppin & Scheid, 1980).…”

Molecular Cloning and Sequence Analysis of Human Parainfluenza Type 2 Virus mRNA Encoding the Fusion Glycoprotein

“…The F protein is synthesized as a biologically inactive precursor molecule (F0) and is cleaved by a host protease into disulphidebonded F 1 and F2 subunits, thus bestowing it with fusion activity (Scheid & Choppin, 1977). Polypeptides of the fusion glycoprotein have also been identified in PIV2-infected cells (Cowley & Barry, 1983) and their relative sizes were estimated as 60K (F0), 46K (F1) and 22K (F2) (Ito et al, 1987). Despite its medical importance, very little information is available on the molecular biology of PIV2 and molecular cloning and characterization of individual PIV2 genes have been reported only very recently in the literature for the HN gene (Kawano et al, 1990a;Precious et al, 1990) and the P/V gene Ohgimoto et al, 1990).…”