The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties
Viral protein 24 (VP24) from Ebola virus (EBOV) was first recognized as a minor matrix protein that associates with cellular membranes. However, more recent studies shed light on its roles in inhibiting viral genome transcription and replication, facilitating nucleocapsid assembly and transport, and...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-08-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/12/8/869 |
| _version_ | 1797559376384360448 |
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| author | Yuan Su Robert V. Stahelin |
| author_facet | Yuan Su Robert V. Stahelin |
| author_sort | Yuan Su |
| collection | DOAJ |
| description | Viral protein 24 (VP24) from Ebola virus (EBOV) was first recognized as a minor matrix protein that associates with cellular membranes. However, more recent studies shed light on its roles in inhibiting viral genome transcription and replication, facilitating nucleocapsid assembly and transport, and interfering with immune responses in host cells through downregulation of interferon (IFN)-activated genes. Thus, whether VP24 is a peripheral protein with lipid-binding ability for matrix layer recruitment has not been explored. Here, we examined the lipid-binding ability of VP24 with a number of lipid-binding assays. The results indicated that VP24 lacked the ability to associate with lipids tested regardless of VP24 posttranslational modifications. We further demonstrate that the presence of the EBOV major matrix protein VP40 did not promote VP24 membrane association in vitro or in cells. Further, no protein–protein interactions between VP24 and VP40 were detected by co-immunoprecipitation. Confocal imaging and cellular membrane fractionation analyses in human cells suggested VP24 did not specifically localize at the plasma membrane inner leaflet. Overall, we provide evidence that EBOV VP24 is not a lipid-binding protein and its presence in the viral matrix layer is likely not dependent on direct lipid interactions. |
| first_indexed | 2024-03-10T17:45:34Z |
| format | Article |
| id | doaj.art-08ad1ebaaa7c4799bb545f5d0b3e241b |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T17:45:34Z |
| publishDate | 2020-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-08ad1ebaaa7c4799bb545f5d0b3e241b2023-11-20T09:32:42ZengMDPI AGViruses1999-49152020-08-0112886910.3390/v12080869The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding PropertiesYuan Su0Robert V. Stahelin1Department of Medicinal Chemistry and Molecular Pharmacology and the Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USADepartment of Medicinal Chemistry and Molecular Pharmacology and the Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USAViral protein 24 (VP24) from Ebola virus (EBOV) was first recognized as a minor matrix protein that associates with cellular membranes. However, more recent studies shed light on its roles in inhibiting viral genome transcription and replication, facilitating nucleocapsid assembly and transport, and interfering with immune responses in host cells through downregulation of interferon (IFN)-activated genes. Thus, whether VP24 is a peripheral protein with lipid-binding ability for matrix layer recruitment has not been explored. Here, we examined the lipid-binding ability of VP24 with a number of lipid-binding assays. The results indicated that VP24 lacked the ability to associate with lipids tested regardless of VP24 posttranslational modifications. We further demonstrate that the presence of the EBOV major matrix protein VP40 did not promote VP24 membrane association in vitro or in cells. Further, no protein–protein interactions between VP24 and VP40 were detected by co-immunoprecipitation. Confocal imaging and cellular membrane fractionation analyses in human cells suggested VP24 did not specifically localize at the plasma membrane inner leaflet. Overall, we provide evidence that EBOV VP24 is not a lipid-binding protein and its presence in the viral matrix layer is likely not dependent on direct lipid interactions.https://www.mdpi.com/1999-4915/12/8/869Ebola virusfiloviruslipid bindingmatrix proteinVP24 |
| spellingShingle | Yuan Su Robert V. Stahelin The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties Viruses Ebola virus filovirus lipid binding matrix protein VP24 |
| title | The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties |
| title_full | The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties |
| title_fullStr | The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties |
| title_full_unstemmed | The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties |
| title_short | The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties |
| title_sort | minor matrix protein vp24 from ebola virus lacks direct lipid binding properties |
| topic | Ebola virus filovirus lipid binding matrix protein VP24 |
| url | https://www.mdpi.com/1999-4915/12/8/869 |
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