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Published on: January 9, 2019
Primary structures of hemagglutinin-esterase and spike glycoproteins of murine coronavirus DVIM
Abstract:
Diarrhea virus of infant mice (DVIM) is a member of murine hepatitis viruses (MHVs). The nucleotide sequences of the genes encoding the hemagglutinin-esterase (HE) and the spike (S) glycoproteins from DVIM were determined and compared with those of other MHVs. The deduced amino acid sequence of the HE protein was most similar to that of MHV-S strain (94% identity), and the S protein sequence was most similar to that of MHV-Y strain (90% identity). The DVIM HE protein has a unique N-linked glycosylation site in addition to other glycosylation sites common to many MHV strains. Unlike in some typical MHV strain, such as MHV-A59 and MHV-JHM, the vast majority of the S glycoprotein molecules in DVIM exist an uncleaved form probably due to several amino acid substitutions around the cleavage site.
Insights
Diarrhea virus of infant mice (DVIM) shares genetic similarities with other murine hepatitis viruses (MHVs). Researchers found unique glycosylation and uncleaved spike proteins in DVIM, distinguishing it from other strains.
Area of Science:
- Virology
- Molecular Biology
- Genomics
Background:
- Diarrhea virus of infant mice (DVIM) is classified within the murine hepatitis virus (MHV) family.
- Murine hepatitis viruses are known for their genetic diversity and impact on mouse models.
Purpose of the Study:
- To determine and compare the nucleotide sequences of hemagglutinin-esterase (HE) and spike (S) glycoprotein genes of DVIM with other MHV strains.
- To identify unique structural features of DVIM's HE and S glycoproteins.
Main Methods:
- Nucleotide sequencing of DVIM genes encoding HE and S glycoproteins.
- Comparative sequence analysis of deduced amino acid sequences against existing MHV strain data.
Main Results:
- DVIM HE protein sequence shows 94% identity to MHV-S strain.
- DVIM S protein sequence shows 90% identity to MHV-Y strain.
- DVIM HE protein possesses a unique N-linked glycosylation site; its S glycoprotein is predominantly uncleaved due to amino acid substitutions.
Conclusions:
- DVIM exhibits distinct molecular characteristics in its HE and S glycoproteins compared to other MHV strains.
- The unique glycosylation and uncleaved S protein in DVIM may influence its biological properties and pathogenesis.
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