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Structure of an enteric pathogen, bovine parvovirus
Shweta Kailasan1, Sujata Halder1, Brittney Gurda1
1Department of Biochemistry and Molecular Biology and the McKnight Brain Institute, University of Florida, Gainesville, Florida, USA.
Journal of Virology
|December 19, 2014
Summary
This study reveals the unique structure of the bovine parvovirus (BPV) capsid, crucial for developing vaccines and antiviral drugs. Understanding BPV
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Bovine parvovirus (BPV) is a significant pathogen causing respiratory and gastrointestinal issues in cattle.
- BPV belongs to the Bocaparvovirus genus within the Parvoviridae family, known for causing infections in both animals and humans.
- The structure of BPV is essential for understanding its pathogenesis and for developing targeted interventions like vaccines and inhibitors.
Purpose of the Study:
- To determine the high-resolution structure of the BPV capsid.
- To provide a structural template for the development of vaccines and small-molecule inhibitors against BPV.
- To compare the BPV capsid structure with other bocaparvoviruses and parvoviruses to understand tropism and pathogenicity.
Main Methods:
- X-ray crystallography was employed to determine the BPV capsid structure to 3.2-Å resolution.
- Cryo-electron microscopy and three-dimensional image reconstruction (cryo-reconstruction) were used to achieve an 8.8-Å resolution.
- Analysis focused on the major capsid viral protein 2 (VP2) and its structural features.
Main Results:
- The BPV capsid structure conserves the common parvoviral eight-stranded jellyroll motif and an αA helix.
- Unique features include a raised surface loop at the 2-fold axes and extended N-terminal residues (29-38) in the interior channel.
- Surface loops exhibit high variability, conferring a unique topology distinct from other known bocaparvoviruses like human bocavirus 1 (HBoV1).
Conclusions:
- The determined BPV capsid structure provides critical insights into its molecular architecture.
- The unique surface topology, shaped by variable loops, likely influences receptor recognition, tropism, and pathogenicity.
- This structural information is vital for designing effective vaccines and antiviral therapies against bovine parvovirus.
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