Successful human adenovirus (HAdV) replication relies on multiple protein-protein interactions between viral and host proteins. HAdV type 5 (HAdV-5) pVI is a multifaceted protein necessary for viral endosomal escape, activation of viral protease, as well as nuclear shuttling of certain viral proteins. Preliminary mass spectrometry experiments indicated that pVI can bind cellular importins and histone chaperones, of which many are considered novel pVI targets. Here, the binding of the pVI protein to cellular importins was validated, and preliminary studies were done to characterize whether HAdV-5 infection changes importin levels in the infected cells. The validation studies were inconclusive, but it was observed that the accumulation of the importin proteins was not altered in during HAdV-5 infection. In addition, the role of NAP1L1 and NAP1L4, two ubiquitously expressed histone chaperones, was examined during HAdV-5 infection and their effect on HAdV-5 genome structure. Here, it is shown that NAP1L1 knockdown affected viral mRNA and protein as well as hindered viral histone-like protein pVII deposition onto viral DNA during the late stage of infection. In contrast, the NAP1L4 protein was shown to co-localize to viral replication centers (VRCs), and its elimination promoted the pVII protein deposition on virus DNA. These results suggest that NAP1L1 is involved in viral transcription and chromatin assembly, whereas NAP1L4 has anti-viral properties during the assembly process.
| Identifer | oai:union.ndltd.org:UPSALLA1/oai:DiVA.org:uu-507991 |
| Date | January 2023 |
| Creators | Taubert, Alexander |
| Publisher | Uppsala universitet, Institutionen för medicinsk biokemi och mikrobiologi |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Student thesis, info:eu-repo/semantics/bachelorThesis, text |
| Format | application/pdf |
| Rights | info:eu-repo/semantics/openAccess |
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