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Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein
1National Institute of Neuroscience, NCNP, Tokyo, Japan.
Abstract:
We have examined six different JHMV variants, sp-4 (recloned wt JHMV), cl-2, CNSV, DL, DS, and JHM-X, in terms of the sizes of the mRNA3 and E2 glycoprotein as well as their reactivity to a panel of monoclonal antibodies to the E2 glycoprotein. Two of these variants, sp-4 and JHM-X, were found to have smaller mRNA3 and E2 glycoprotein species compared with those of the other four variants. In addition, sp-4 and JHM-X were distinguished from the other four variants by their inability to bind to monoclonal antibodies recognizing two antigenic domains of the E2 molecule. Thus, six JHMV variants could clearly be divided into two groups with respect to the size and antigenicity of their E2 glycoproteins.
Insights
Researchers studied six JHMV variants, finding two (sp-4 and JHM-X) have smaller E2 glycoproteins and differ in antigenicity compared to the other four variants. This classifies JHMV variants into two distinct groups based on E2 glycoprotein characteristics.
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Murine hepatitis virus (MHV) is a significant pathogen, with the JHM strain (JHMV) being extensively studied.
- The E2 glycoprotein is a key viral protein involved in JHMV entry and is a target for neutralizing antibodies.
- Understanding variations in viral proteins is crucial for comprehending viral pathogenesis and immune responses.
Purpose of the Study:
- To characterize and compare six distinct JHMV variants.
- To investigate differences in the size and antigenicity of the E2 glycoprotein among JHMV variants.
- To determine if these variations correlate with distinct antigenic properties.
Main Methods:
- Analysis of mRNA3 and E2 glycoprotein sizes in six JHMV variants.
- Assessment of E2 glycoprotein reactivity using a panel of monoclonal antibodies.
- Comparison of binding affinities to specific antigenic domains on the E2 glycoprotein.
Main Results:
- Two JHMV variants, sp-4 and JHM-X, exhibited smaller mRNA3 and E2 glycoprotein species compared to the other four variants.
- The sp-4 and JHM-X variants showed distinct antigenic profiles.
- These two variants were unable to bind to monoclonal antibodies targeting two specific antigenic domains of the E2 glycoprotein.
Conclusions:
- The six JHMV variants can be clearly categorized into two distinct groups based on E2 glycoprotein size and antigenicity.
- Variations in E2 glycoprotein size and antigenic structure are significant differentiating factors among JHMV strains.
- These findings contribute to the molecular characterization of JHMV and may have implications for vaccine development and diagnostics.
