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A structure-guided mutation in the major capsid protein retargets BK polyomavirus
Ursula Neu1, Stacy-Ann A Allen, Bärbel S Blaum
1Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Plos Pathogens
|October 17, 2013
Summary
Human polyomavirus BKPyV binds to specific gangliosides, acting as cellular receptors. A single amino acid change in the viral capsid protein switches BKPyV
Area of Science:
- Virology
- Structural Biology
- Glycobiology
Background:
- Viral tropism and pathogenicity often depend on cell surface receptor interactions.
- Understanding viral receptor specificity is crucial for controlling viral infections.
- Carbohydrate-binding viruses present unique challenges for structural studies.
Purpose of the Study:
- To characterize the receptor specificity, structure, and infectivity of human polyomavirus BKPyV.
- To identify the molecular determinants of BKPyV's carbohydrate receptor binding.
- To explore the potential for retargeting viral specificity.
Main Methods:
- Crystal structure determination of BKPyV VP1 in complex with GD3.
- Biochemical assays to assess ganglioside binding.
- Site-directed mutagenesis to alter VP1 amino acid residues.
- In vitro and cell culture infectivity assays.
Main Results:
- BKPyV binds to b-series gangliosides GD3, GD2, GD1b, and GT1b.
- The crystal structure reveals BKPyV VP1 contacts two sialic acids in GD3.
- Amino acid residue 68 in VP1 is a key determinant of receptor specificity.
- Mutating residue 68 switches BKPyV specificity from GD3 to GM1.
Conclusions:
- Viral receptor binding sites exhibit significant plasticity.
- A single amino acid substitution can alter viral tropism.
- Findings provide a framework for engineering viruses with altered receptor specificities.
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