Structural basis for the shielding function of the dynamic trypanosome variant surface glycoprotein coat
| العنوان: | Structural basis for the shielding function of the dynamic trypanosome variant surface glycoprotein coat |
|---|---|
| المؤلفون: | Susanne F. Fenz, Marius Glogger, Jochen Kuper, Nicola G. Jones, Thomas Bartossek, Mark Carrington, Mislav Cvitković, Christin Schäfer, Ana-Sunčana Smith, Markus Engstler, Helen R. Mott, Martha Brennich, Caroline Kisker |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Microbiology (medical), Models, Molecular, Protein Conformation, Immunology, Trypanosoma brucei brucei, FOS: Physical sciences, Trypanosoma brucei, Crystallography, X-Ray, Applied Microbiology and Biotechnology, Microbiology, 03 medical and health sciences, Protein structure, Scattering, Small Angle, parasitic diseases, Genetics, Physics - Biological Physics, Lipid bilayer, chemistry.chemical_classification, biology, Chemistry, Biomolecules (q-bio.BM), Cell Biology, small-angle scattering, gpi-anchored proteins, n-terminal domain, biological macromolecules, linked oligosaccharides, resolution structure, membrane anchor, brucei-brucei, cell-surface, system, biology.organism_classification, 3. Good health, 030104 developmental biology, Quantitative Biology - Biomolecules, Membrane protein, Biological Physics (physics.bio-ph), FOS: Biological sciences, Biophysics, Protein Multimerization, Glycoprotein, Linker, Membrane biophysics, Function (biology), Variant Surface Glycoproteins, Trypanosoma |
| الوصف: | The most prominent defence of the unicellular parasite Trypanosoma brucei against the host immune system is a dense coat that comprises a variant surface glycoprotein (VSG). Despite the importance of the VSG family, no complete structure of a VSG has been reported. Making use of high-resolution structures of individual VSG domains, we employed small-angle X-ray scattering to elucidate the first two complete VSG structures. The resulting models imply that the linker regions confer great flexibility between domains, which suggests that VSGs can adopt two main conformations to respond to obstacles and changes of protein density, while maintaining a protective barrier at all times. Single-molecule diffusion measurements of VSG in supported lipid bilayers substantiate this possibility, as two freely diffusing populations could be detected. This translates into a highly flexible overall topology of the surface VSG coat, which displays both lateral movement in the plane of the membrane and variation in the overall thickness of the coat. Comment: 14 pages, 6 figures, Supplementary information linked |
| اللغة: | English |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80b0978de91ea62bd23dc6d22ee7e898Test https://doi.org/10.1038/s41564-017-0013-6Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....80b0978de91ea62bd23dc6d22ee7e898 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |