ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection
Hepatitis C virus (HCV) infects millions of people worldwide and is a leading cause of liver disease. Despite recent advances in antiviral therapies, viral resistance can limit drug efficacy and understanding the mechanisms that confer viral escape is important. We employ an unbiased interactome ana...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Microbiology Society
2023
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| _version_ | 1797111477895692288 |
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| author | Smirnov, A Magri, A Lotz, R Han, X Yin, C Harris, M Osterburg, C Dötsch, V McKeating, JA Lu, X |
| author_facet | Smirnov, A Magri, A Lotz, R Han, X Yin, C Harris, M Osterburg, C Dötsch, V McKeating, JA Lu, X |
| author_sort | Smirnov, A |
| collection | OXFORD |
| description | Hepatitis C virus (HCV) infects millions of people worldwide and is a leading cause of liver disease. Despite recent advances in antiviral therapies, viral resistance can limit drug efficacy and understanding the mechanisms that confer viral escape is important. We employ an unbiased interactome analysis to discover host binding partners of the HCV non-structural protein 5A (NS5A), a key player in viral replication and assembly. We identify ASPP2, apoptosis-stimulating protein of p53, as a new host co-factor that binds NS5A via its SH3 domain. Importantly, silencing ASPP2 reduces viral replication and spread. Our study uncovers a previously unknown role for ASPP2 to potentiate HCV RNA replication. |
| first_indexed | 2024-03-07T08:09:28Z |
| format | Journal article |
| id | oxford-uuid:5790debb-80c6-47c4-94bc-9e0282b208bc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T08:09:28Z |
| publishDate | 2023 |
| publisher | Microbiology Society |
| record_format | dspace |
| spelling | oxford-uuid:5790debb-80c6-47c4-94bc-9e0282b208bc2023-11-17T16:08:18ZASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infectionJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5790debb-80c6-47c4-94bc-9e0282b208bcEnglishSymplectic ElementsMicrobiology Society2023Smirnov, AMagri, ALotz, RHan, XYin, CHarris, MOsterburg, CDötsch, VMcKeating, JALu, XHepatitis C virus (HCV) infects millions of people worldwide and is a leading cause of liver disease. Despite recent advances in antiviral therapies, viral resistance can limit drug efficacy and understanding the mechanisms that confer viral escape is important. We employ an unbiased interactome analysis to discover host binding partners of the HCV non-structural protein 5A (NS5A), a key player in viral replication and assembly. We identify ASPP2, apoptosis-stimulating protein of p53, as a new host co-factor that binds NS5A via its SH3 domain. Importantly, silencing ASPP2 reduces viral replication and spread. Our study uncovers a previously unknown role for ASPP2 to potentiate HCV RNA replication. |
| spellingShingle | Smirnov, A Magri, A Lotz, R Han, X Yin, C Harris, M Osterburg, C Dötsch, V McKeating, JA Lu, X ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection |
| title | ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection |
| title_full | ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection |
| title_fullStr | ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection |
| title_full_unstemmed | ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection |
| title_short | ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection |
| title_sort | aspp2 binds to hepatitis c virus ns5a protein via an sh3 domain pxxp motif mediated interaction and potentiates infection |
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