The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid
Goose parvovirus (GPV) is an etiological agent of Derzsy’s disease, afflicting geese and Muscovy ducks worldwide. Its high mortality rate among goslings and ducklings causes large losses to the waterfowl industry. Toward molecular and structural characterization, virus-like particles (VLPs) of GPV w...
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2025-01-01
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| author | Korosh Jabbari Mario Mietzsch Jane Hsi Paul Chipman Jianming Qiu Robert McKenna |
| author_facet | Korosh Jabbari Mario Mietzsch Jane Hsi Paul Chipman Jianming Qiu Robert McKenna |
| author_sort | Korosh Jabbari |
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| description | Goose parvovirus (GPV) is an etiological agent of Derzsy’s disease, afflicting geese and Muscovy ducks worldwide. Its high mortality rate among goslings and ducklings causes large losses to the waterfowl industry. Toward molecular and structural characterization, virus-like particles (VLPs) of GPV were produced, and the capsid structure was determined by cryogenic electron microscopy (cryo-EM) at a resolution of 2.4 Å. The capsid exhibited structural features conserved among parvoviruses, including surface two-fold depressions, three-fold protrusions, and five-fold channels. A structural comparison of the GPV viral protein (VP) structure with other adeno-associated viruses (AAVs), including human AAV2, AAV5, and quail AAV (QAAV), revealed unique conformations of several surface-accessible variable regions (VRs). Furthermore, the GPV capsid was found to be thermally stable at physiological pH, but less so under lower pH conditions. As a member of the genus <i>Dependoparvovirus</i>, GPV could also be bound by cross-reactive anti-AAV capsid antibodies that bind to the five-fold region of the viruses, as shown by native immuno-dot blot analysis. Finally, the GPV VP structure was compared to those of other bird dependoparvoviruses, which revealed that VR-III may be important for GPV and Muscovy duck parvovirus (MDPV) infection. |
| format | Article |
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| institution | Kabale University |
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| language | English |
| publishDate | 2025-01-01 |
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| spelling | doaj-art-6c89b760d8114fcb93bb412771d56c2e2025-01-24T13:42:34ZengMDPI AGMicroorganisms2076-26072025-01-011318010.3390/microorganisms13010080The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus CapsidKorosh Jabbari0Mario Mietzsch1Jane Hsi2Paul Chipman3Jianming Qiu4Robert McKenna5Department of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USADepartment of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USADepartment of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USADepartment of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USADepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS 66103, USADepartment of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USAGoose parvovirus (GPV) is an etiological agent of Derzsy’s disease, afflicting geese and Muscovy ducks worldwide. Its high mortality rate among goslings and ducklings causes large losses to the waterfowl industry. Toward molecular and structural characterization, virus-like particles (VLPs) of GPV were produced, and the capsid structure was determined by cryogenic electron microscopy (cryo-EM) at a resolution of 2.4 Å. The capsid exhibited structural features conserved among parvoviruses, including surface two-fold depressions, three-fold protrusions, and five-fold channels. A structural comparison of the GPV viral protein (VP) structure with other adeno-associated viruses (AAVs), including human AAV2, AAV5, and quail AAV (QAAV), revealed unique conformations of several surface-accessible variable regions (VRs). Furthermore, the GPV capsid was found to be thermally stable at physiological pH, but less so under lower pH conditions. As a member of the genus <i>Dependoparvovirus</i>, GPV could also be bound by cross-reactive anti-AAV capsid antibodies that bind to the five-fold region of the viruses, as shown by native immuno-dot blot analysis. Finally, the GPV VP structure was compared to those of other bird dependoparvoviruses, which revealed that VR-III may be important for GPV and Muscovy duck parvovirus (MDPV) infection.https://www.mdpi.com/2076-2607/13/1/80goose parvoviruscryo-EMVLPscapsidthree-dimensional structureMuscovy duck parvovirus |
| spellingShingle | Korosh Jabbari Mario Mietzsch Jane Hsi Paul Chipman Jianming Qiu Robert McKenna The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid Microorganisms goose parvovirus cryo-EM VLPs capsid three-dimensional structure Muscovy duck parvovirus |
| title | The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid |
| title_full | The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid |
| title_fullStr | The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid |
| title_full_unstemmed | The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid |
| title_short | The Structural, Biophysical, and Antigenic Characterization of the Goose Parvovirus Capsid |
| title_sort | structural biophysical and antigenic characterization of the goose parvovirus capsid |
| topic | goose parvovirus cryo-EM VLPs capsid three-dimensional structure Muscovy duck parvovirus |
| url | https://www.mdpi.com/2076-2607/13/1/80 |
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