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Parainfluenza virus type 2 haemagglutinin-neuraminidase glycoprotein characterized with monoclonal antibodies
1Department of Virology, Karolinska Institute, School of Medicine, Stockholm, Sweden.
Abstract:
Thirteen monoclonal antibodies (MAbs) were prepared against human parainfluenza virus type 2 (PIV2). These MAbs reacted with the haemagglutinin-neuraminidase glycoprotein with an Mr of 84K. The MAbs defined one antigenic site which could be divided into five epitopes. A correlation between haemagglutination inhibition (HI) and neutralization activity could be seen although one MAb, which recognized a distinct epitope, showed neutralization and no HI activity to PIV2. The reactivity of the MAbs was tested against Sendai virus, parainfluenza virus type 3, simian virus 5 (SV5), mumps virus, Newcastle disease virus, measles virus and canine distemper virus. Only one MAb showed any cross-reaction with a low HI titre to SV5.
Insights
Thirteen monoclonal antibodies (MAbs) targeting human parainfluenza virus type 2 (PIV2) identified a key antigenic site on the HA-NA glycoprotein. One MAb showed neutralization without hemagglutination inhibition, indicating distinct epitope recognition.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Human parainfluenza virus type 2 (PIV2) is a significant respiratory pathogen.
- Understanding PIV2 antigenic structure is crucial for vaccine and therapeutic development.
- Monoclonal antibodies (MAbs) are vital tools for characterizing viral antigens.
Purpose of the Study:
- To generate and characterize MAbs against PIV2.
- To define the antigenic sites and epitopes on the PIV2 haemagglutinin-neuraminidase (HA-NA) glycoprotein.
- To investigate the correlation between antibody binding, hemagglutination inhibition (HI), and neutralization activities.
Main Methods:
- Production of thirteen MAbs against PIV2.
- Characterization of MAb reactivity with the PIV2 HA-NA glycoprotein (Mr 84K).
- Epitope mapping and analysis of HI and neutralization assays.
- Cross-reactivity testing against related paramyxoviruses.
Main Results:
- All thirteen MAbs recognized the PIV2 HA-NA glycoprotein.
- A single antigenic site comprising five distinct epitopes was defined.
- A correlation between HI and neutralization was observed, with one MAb showing neutralization but no HI activity.
- Minimal cross-reactivity was found with other paramyxoviruses, with one MAb showing low HI to SV5.
Conclusions:
- The HA-NA glycoprotein of PIV2 contains a major antigenic site with multiple epitopes.
- Distinct epitopes on the HA-NA protein can elicit differential antibody functions (neutralization vs. HI).
- These MAbs provide valuable tools for PIV2 research and diagnostics.