Antigenic diversity of human parainfluenza virus type 1 isolates and their immunological relationship with Sendai virus revealed by using monoclonal antibodies.
Fifty-six monoclonal antibodies (MAbs) directed against human parainfluenza virus type 1 (hPIV-1) were prepared in order to identify the structural proteins of hPIV-1, to examine the immunological relationship between hPIV-1 and Sendai virus (SV), and to determine the antigenic diversity of clinical isolates of hPIV-1. In addition, 41 MAbs characterized previously and directed against SV were used for immunological comparison of SV and hPIV-1 isolates. Of the MAbs against hPIV-1, two reacted with phospho (P) protein, 11 with nucleocapsid protein (NP), 24 with haemagglutinin-neuraminidase (HN) protein and 19 with fusion (F) protein. With the aid of MAbs against hPIV-1 and those against SV showing cross-reactivity with hPIV-1, the structural proteins of hPIV-1 were identified; p83, p56, p34, gp74 and gp60 of hPIV-1 were identified as the P, NP, M, HN and F proteins, respectively. The MAbs against the P protein and NP of hPIV-1 showed limited cross-reactivity with SV, whereas they had high reactivity with clinical isolates of hPIV-1. Interestingly, one MAb against the NP of hPIV-1 lacked reactivity with clinical isolates which were isolated in the 1970s and 1980s. The MAbs against the HN of hPIV-1 also exhibited quite limited reactivity with SV and the clinical isolates; two groups of HN-specific MAbs showed almost no reactivity with the clinical isolates from the 1970s and 1980s, similarly to the NP-specific MAb. However, anti-HN MAbs belonging to the two groups showing specific activities (neuraminidase inhibition and haemolysis inhibition) reacted with almost all clinical isolates. On the other hand, although anti-F protein MAbs had limited reactivity with SV, they showed reactivity with almost all hPIV-1 isolates. The MAbs against the P, NP, M, HN and F proteins of SV also showed limited cross-reactivity with the clinical hPIV-1 isolates, and this reactivity was independent of the time and place of isolation, except for that of the F protein. These results confirm that although hPIV-1 is related to SV, it is antigenically distinct from it.
Komada
H
H
Department of Microbiology, Mie University School of Medicine, Japan.
Kusagawa
S
S
Orvell
C
C
Tsurudome
M
M
Nishio
M
M
Bando
H
H
Kawano
M
M
Matsumura
H
H
Norrby
E
E
Ito
Y
Y
D000911:Antibodies, Monoclonal; D003429:Cross Reactions; D000939:Epitopes / Q000276:immunology*; D005814:Genes, Viral; D014644:Genetic Variation; D006801:Humans; D009500:Neutralization Tests; D010222:Parainfluenza Virus 1, Human / Q000145:classification* / Q000276:immunology* / Q000302:isolation & purification; D018184:Paramyxoviridae Infections / Q000276:immunology*; D010750:Phosphoproteins / Q000276:immunology; D014760:Viral Fusion Proteins / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology*; D015678:Viral Structural Proteins / Q000235:genetics
D000911:Antibodies, Monoclonal; D000939:Epitopes; C075739:F protein, parainfluenza virus 1; D010750:Phosphoproteins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D015678:Viral Structural Proteins; C068855:P protein, parainfluenza virus 1