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Structural polypeptides of the murine coronavirus DVIM
Abstract:
The structural polypeptides of the murine coronavirus DVIM (diarrhoea virus of infant mice) have been analysed in comparison with other strains MHV-2, MHV-3, MHV-4 (JHM) and MHV-S by SDS-PAGE. In the presence of 2-mercaptoethanol, three major glycopolypeptides, gp180, gp69, gp25 (as a group of similar species) and one major non-glycosylated polypeptide p58 were detected. The gp69 is a DVIM specific glycopolypeptide, in which the glycosidic moieties are linked to the core polypeptide through N-glycosidic bonds, and hence may be correlated with the short projections of the viral envelope. Further gp140, which appears in the absence of reducing agents, is apparently a dimer of gp69 held together by disulfide linkages. The gp25 family, on the other hand, consists of four polypeptides, two of which are not metabolically inhibited by tunicamycin suggesting that they are O-linked glycopolypeptides. DVIM seems to be serologically closely related to the MHV-S strain as shown by neutralization.
Insights
Murine coronavirus DVIM structural polypeptides were analyzed using SDS-PAGE. DVIM features a unique N-linked glycopolypeptide (gp69) and O-linked glycopolypeptides, distinguishing it from other strains.
Area of Science:
- Virology
- Molecular Biology
- Structural Biology
Background:
- Murine coronaviruses (Murine Coronaviruses) are significant pathogens.
- Understanding the structural polypeptides of different strains is crucial for viral characterization.
Purpose of the Study:
- To analyze and compare the structural polypeptides of the murine coronavirus DVIM (diarrhoea virus of infant mice) with other strains.
- To identify strain-specific polypeptides and their glycosylation patterns.
Main Methods:
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was employed for polypeptide analysis.
- Analysis was performed in the presence and absence of reducing agents (2-mercaptoethanol).
- Tunicamycin treatment was used to investigate glycosylation types.
Main Results:
- Three major glycopolypeptides (gp180, gp69, gp25) and one non-glycosylated polypeptide (p58) were detected in DVIM.
- gp69, a DVIM-specific glycopolypeptide, features N-glycosidic linkages potentially related to viral envelope projections.
- The gp25 family includes O-linked glycopolypeptides, indicated by tunicamycin resistance, and gp140 is a disulfide-linked dimer of gp69.
Conclusions:
- DVIM possesses distinct glycopolypeptide profiles, including a unique N-linked gp69 and O-linked polypeptides within the gp25 family.
- These structural differences may correlate with specific viral properties and serological relationships.
- DVIM shows serological relatedness to the MHV-S strain, as confirmed by neutralization assays.