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The Interdomain Reg...
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Brooks, Andrew J
(författare)
The Interdomain Region of Dengue NS5 ProteinInteracts with NS3 and Host Proteins
- Artikel/kapitelEngelska2002
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LIBRIS-ID:oai:DiVA.org:sh-6066
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https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-6066URI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:vet swepub-contenttype
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Ämneskategori:art swepub-publicationtype
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Although dengue virus genome replication occurs in the cytoplasm of infected cells, it has been shown that the NS5 protein (RNA-dependent RNA polymerase) is hyperphosphorylated at a late stage in infection and localized to the cell nucleus. A 37 amino acid sequence of NS5 (residues 369-405) was shown to contain a functional nuclear localization signal (NLS) that interacted with the cellular nuclear transport factor, importin α/β heterodimer. Further studies using the yeast two-hybrid system revealed that the NS5 region (residues 320-368) immediately adjacent to the NLS contained an importin β-binding site that abuts or overlaps the binding site for the NS3 protein (protease/helicase). The importin β-binding site has also been shown to be a functional NLS (bNLS). Intriguingly, when both bNLS and NLS (residues 320-405) were present, the fused β -galactosidase protein did not accumulate in the nucleus. Here we provide a review of our studies on the NS5 interdomain region and compare it to other members of the Flavivirus genus in order to highlight the importance of this region as a possible target for developing broad-acting antiviral agent against dengue and other mechanistically-related viruses.
Ämnesord och genrebeteckningar
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NS5 protein
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protein interactions
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NS3 protein
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nuclear localization signal
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MEDICINE
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MEDICIN
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Johansson, MagnusSödertörns högskola,Avdelning Naturvetenskap(Swepub:sh)shmsjn02
(författare)
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Criswell, Erin
(författare)
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Jans, David A
(författare)
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Vasudevan, Subhash G
(författare)
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Södertörns högskolaAvdelning Naturvetenskap
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Dengue Bulletin26, s. 155-1611020-895X
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