Structural Basis of HIV-1 Tethering to Membranes by the BST-2/Tetherin Ectodomain
| Autor: | Yoshiko Usami, Ganesh Natrajan, Jean-Pierre Simorre, Heinrich G. Göttlinger, Andrew A. McCarthy, Nolwenn Miguet, Bettina Hartlieb, Patricia Renesto, Winfried Weissenhorn, Andreas Hinz, Hikaru Yamanaka |
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| Přispěvatelé: | Independent Department for Medical Psychology and Medical Sociology, Universität Leipzig, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Thérapeutique Recombinante Expérimentale (TIMC-IMAG-TheREx), Techniques de l'Ingénierie Médicale et de la Complexité - Informatique, Mathématiques et Applications, Grenoble - UMR 5525 (TIMC-IMAG), Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Unit of Virus Host Cell Interactions (UVHCI), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School [Worcester] (UMASS), University of Massachusetts System (UMASS)-University of Massachusetts System (UMASS), Universität Leipzig [Leipzig], Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF) |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Cancer Research MICROBIO Crystallography X-Ray GPI-Linked Proteins Microbiology Protein Structure Secondary Cell membrane 03 medical and health sciences Protein structure Antigens CD Immunology and Microbiology(all) Virology Scattering Small Angle medicine Animals Molecular Biology Virus Release ComputingMilieux_MISCELLANEOUS 030304 developmental biology Coiled coil 0303 health sciences Membrane Glycoproteins biology [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Protein Stability Circular Dichroism Cell Membrane 030302 biochemistry & molecular biology [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Protein Structure Tertiary Membrane glycoproteins Membrane medicine.anatomical_structure Ectodomain Biochemistry Host-Pathogen Interactions [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology HIV-1 Mutagenesis Site-Directed biology.protein Biophysics Tetherin CELLBIO Parasitology |
| Zdroj: | Cell Host and Microbe Cell Host and Microbe, 2010, 7 (4), pp.314-323. ⟨10.1016/j.chom.2010.03.005⟩ Cell Host and Microbe, Elsevier, 2010, 7 (4), pp.314-323. ⟨10.1016/j.chom.2010.03.005⟩ |
| ISSN: | 1931-3128 |
| Popis: | SummaryThe restriction factor BST-2/tetherin contains two membrane anchors employed to retain some enveloped viruses, including HIV-1 tethered to the plasma membrane in the absence of virus-encoded antagonists. The 2.77 Å crystal structure of the BST-2/tetherin extracellular core presented here reveals a parallel 90 Å long disulfide-linked coiled-coil domain, while the complete extracellular domain forms an extended 170 Å long rod-like structure based on small-angle X-ray scattering data. Mutagenesis analyses indicate that both the coiled coil and the N-terminal region are required for retention of HIV-1, suggesting that the elongated structure can function as a molecular ruler to bridge long distances. The structure reveals substantial irregularities and instabilities throughout the coiled coil, which contribute to its low stability in the absence of disulfide bonds. We propose that the irregular coiled coil provides conformational flexibility, ensuring that BST-2/tetherin anchoring both in the plasma membrane and in the newly formed virus membrane is maintained during virus budding. |
| Databáze: | OpenAIRE |
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