The structure of parvoviruses |
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| Institution: | 1. Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907-1392;2. *James A. Baker Institute for Animal Health, New York State College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA;1. Rochester General Hospital Research Institute, Rochester, NY 14621, USA;2. Department of Biostatistics and Computational Biology, University of Rochester Medical Center, Rochester, NY 14642, USA;3. Clinical and Translational Research Center, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY 14214, USA;4. Department of Infectious Diseases, College of Veterinary Medicine University of Georgia, Athens, GA 30602, USA;5. Department of Microbiology and Immunology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY 14214, USA;1. Institute of Animal Husbandry and Veterinary Medicine, Fujian Academy of Agricultural Sciences, Fuzhou, 350013, China;2. Fujian Animal Diseases Control Technology Development Center, Fuzhou, 350013, China |
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| Abstract: | Capsids of autonomous parvoviruses are assembled from two proteins, VP1 and VP2, which overlap in sequence, with VP1 having additional amino-terminal residues. Empty capsids can be assembled from VP2 alone. Post-translational cleavage of assembled particles can modify some of the proteins by truncation of a few of the amino-terminal residues of VP2 to generate VP3 in full virions. The structures of canine parvovirus (CPV) and feline panleukopenia virus (FPV) have been solved to better than 3·5 Å resolution, while the structure of human parvovirus, B19, has been determined to 8 Å resolution only. In each case the T=1 icosahedron is made up of 60 copies of a mixture of VP1, VP2 and VP3, where each subunit has a structural motif common to many other RNA and DNA viruses, consisting of an eight-stranded anti-parallel β-barrel. The surface of the capsid is made up primarily of large elaborate loops which connect the β-strands that make up the barrel. Variation in the amino acid sequence and topology of these loops account for differing biological properties. |
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