Structure of Reovirus Attachment Protein σ1 with Carbohydrates
Author Information
Author(s): Reiter Dirk M., Frierson Johnna M., Halvorson Elizabeth E., Kobayashi Takeshi, Dermody Terence S., Stehle Thilo
Primary Institution: University of Tuebingen
Hypothesis
To understand how reoviruses engage carbohydrate receptors, we determined the crystal structures of reovirus attachment protein σ1 in complex with various sialylated oligosaccharides.
Conclusion
The study reveals that the reovirus attachment protein σ1 binds to sialic acid through specific residues, providing insights into viral attachment mechanisms.
Supporting Evidence
- The crystal structures show that σ1 binds to sialic acid through specific interactions involving key amino acids.
- Mutagenesis studies identified residues 198, 202, 203, 204, and 205 as critical for sialic acid binding.
- All three oligosaccharides studied terminate in sialic acid, which is essential for reovirus attachment.
Takeaway
The reovirus uses a special protein to grab onto sugars on cells, which helps it infect them. This study shows how that protein works.
Methodology
The researchers used X-ray crystallography to determine the structure of the σ1 protein in complex with sialylated oligosaccharides and performed mutagenesis studies to identify key binding residues.
Limitations
The study primarily focuses on a specific serotype of reovirus and may not fully represent other serotypes or viral interactions.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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