Evidence map›Paper›PMID 28894098›Full record

ArticleNature microbiology2017

Structural basis for the shielding function of the dynamic trypanosome variant surface glycoprotein coat.

Thomas Bartossek, Nicola G Jones, Christin Schäfer, Mislav Cvitković, Marius Glogger, Helen R Mott, Jochen Kuper, Martha Brennich, Mark Carrington, Ana-Sunčana Smith and 3 more

Abstract read
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In one paragraph

Article in Nature microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Thomas BartossekDepartment of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg, 97074, Würzburg, Germany.
Nicola G JonesDepartment of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg, 97074, Würzburg, Germany. nicola.jones@uni-wuerzburg.de.ORCID http://orcid.org/0000-0003-3384-0156
Christin SchäferRudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, 97080, Würzburg, Germany.
Mislav CvitkovićPULS Group, Institut für Theoretische Physik and the Excellence Cluster: Engineering of Advanced Materials, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91052, Erlangen, Germany.
Marius GloggerDepartment of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg, 97074, Würzburg, Germany.
Helen R MottDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK.ORCID http://orcid.org/0000-0002-7890-7097
Jochen KuperRudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, 97080, Würzburg, Germany.
Martha BrennichEuropean Synchrotron Radiation Facility, 71 Avenue des Martyrs, CS 40220, 38042, Grenoble, France.ORCID http://orcid.org/0000-0003-0415-8334
Mark CarringtonDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK.
Ana-Sunčana SmithPULS Group, Institut für Theoretische Physik and the Excellence Cluster: Engineering of Advanced Materials, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91052, Erlangen, Germany.
Susanne FenzDepartment of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg, 97074, Würzburg, Germany.ORCID http://orcid.org/0000-0002-8395-0727
Caroline KiskerRudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, 97080, Würzburg, Germany.
Markus EngstlerDepartment of Cell and Developmental Biology, Theodor-Boveri-Institute, Biocenter, University of Würzburg, 97074, Würzburg, Germany. markus.engstler@biozentrum.uni-wuerzburg.de.ORCID http://orcid.org/0000-0003-1436-5759

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Crystallography, X-RayModels, MolecularProtein ConformationProtein MultimerizationScattering, Small AngleTrypanosoma brucei bruceiVariant Surface Glycoproteins, TrypanosomaVariant Surface Glycoproteins, Trypanosoma

Identifiers

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.