This title appears in the Scientific Report :
2014
Solution NMR study of the interaction of HIV-1 VpU and human BST-2
Solution NMR study of the interaction of HIV-1 VpU and human BST-2
The human protein BST-2, also known as tetherin/CD317/HM1.24, is an important component of antiviral defence that restricts enveloped viruses from budding from the host cell [1]. Virus protein “U” (VpU), an accessory protein of human immunodeficiency virus type 1 (HIV-1), is able to antagonize and d...
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Personal Name(s): | Roes, Claas (Corresponding Author) |
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Neudecker, Philipp / Willbold, Dieter / König, Bernd | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | 2014 |
Imprint: |
2014
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Conference: | Annual Meeting of the German Biophysical Society, Lübeck (Germany), 2014-09-14 - 2014-09-17 |
Document Type: |
Poster |
Research Program: |
Structural Biology |
Publikationsportal JuSER |
The human protein BST-2, also known as tetherin/CD317/HM1.24, is an important component of antiviral defence that restricts enveloped viruses from budding from the host cell [1]. Virus protein “U” (VpU), an accessory protein of human immunodeficiency virus type 1 (HIV-1), is able to antagonize and downregulate BST-2 in infected cells [2]. The presence of VpU increases HIV-1 replication by one order of magnitude [3].We have studied the interaction of the two bitopic transmembrane (TM) proteins BST-2 and VpU in membrane mimicking DPC micelles using solution state nuclear magnetic resonance (NMR) spectroscopy. An E. coli-based cell-free expression (CFE) system was used for the production of isotope-labelled proteins, i.e., full-length VpU and a BST-2 construct that encompasses the cytoplasmic and the single transmembrane domain of this protein. Resonance assignment of backbone nuclei of the BST-2 construct is close to complete and allowed secondary structure analysis based on secondary chemical shifts. In particular, an α-helical stretch of amino acids was confirmed in the predicted TM region of BST-2. Further, isotope-labelled BST-2 was titrated with increasing amounts of unlabelled VpU in order to identify BST-2 residues that intimately approach VpU in the putative BST-2/VpU complex in DPC micelles. The observed chemical shift changes map to the TM helix of BST-2. Resonance assignment of full-length VpU is currently in progress and will enable a more detailed analysis of the BST-2 VpU complex. [1] Hammonds J., et al, PLoS Pathog. 6(2): e1000749 (2010) [2] Dubé M., et al, PLoS Pathog. 6(4): e1000856 (2010)[3] Fischer W.B., FEBS Lett. 552:39-46 (2003) |