Evidence map›Paper›PMID 31036849›Full record

ArticleNature communications2019

Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.

Jason J Paxman, Alvin W Lo, Matthew J Sullivan, Santosh Panjikar, Michael Kuiper, Andrew E Whitten, Geqing Wang, Chi-Hao Luan, Danilo G Moriel, Lendl Tan and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 13% of its field
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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. The role of adhesins ofGut microbes · 2026
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  5. Antigen 43 associated withMicrobiology spectrum · 2025
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  7. Avian pathogenicVeterinary world · 2024
    Review
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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

16 authors at 7 institutions in 2 countries.

Jason J PaxmanDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, VIC, Australia.ORCID http://orcid.org/0000-0002-1418-5910
Alvin W LoSchool of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.
Matthew J SullivanSchool of Medical Science, and Menzies Health Institute Queensland, Griffith University, Gold Coast, 4222, QLD, Australia.
Santosh PanjikarMacromolecular Crystallography, Australian Synchrotron, Clayton, 3168, VIC, Australia.ORCID http://orcid.org/0000-0001-7429-3879
Michael KuiperMolecular & Materials Modelling group Data61, CSIRO, Docklands, Melbourne, 8012, VIC, Australia.
Andrew E WhittenAustralian Centre for Neutron Scattering, Australian Nuclear Science and Technology Organisation, Lucas Heights, 2234, NSW, Australia.ORCID http://orcid.org/0000-0001-8856-3120
Geqing WangDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, VIC, Australia.
Chi-Hao LuanHigh Throughput Analysis Laboratory and Department of Molecular Biosciences, Northwestern University, Chicago, 60208, IL, USA.
Danilo G MorielSchool of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.
Lendl TanSchool of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.ORCID http://orcid.org/0000-0002-9955-2440
Kate M PetersSchool of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.
Minh-Duy PhanSchool of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.ORCID http://orcid.org/0000-0002-3426-1044
Christine L GeeMacromolecular Crystallography, Australian Synchrotron, Clayton, 3168, VIC, Australia.ORCID http://orcid.org/0000-0002-2632-6418
Glen C UlettSchool of Medical Science, and Menzies Health Institute Queensland, Griffith University, Gold Coast, 4222, QLD, Australia.ORCID http://orcid.org/0000-0002-9638-8091
Mark A SchembriSchool of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia. m.schembri@uq.edu.au.ORCID http://orcid.org/0000-0003-4863-9260
Begoña HerasDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, VIC, Australia. b.heras@latrobe.edu.au.ORCID http://orcid.org/0000-0003-3469-7988
The University of Queensland · AULa Trobe University · AUAustralian Synchrotron · AUGriffith University · AUAustralian Nuclear Science and Technology Organisation · AUCommonwealth Scientific and Industrial Research Organisation · AUNorthwestern University · US

Funding

Echo Acoustic Liquid Handler for High Throughput Analysis LabS10OD023681 · OD · NORTHWESTERN UNIVERSITY · PI WEISS, ERIC LYLE · 2018 to 2018
$550k
NIH HHS S10 OD023681
6 · The paper itself

Abstract

Autotransporters are the largest family of outer membrane and secreted proteins in Gram-negative bacteria. Most autotransporters are localised to the bacterial surface where they promote colonisation of host epithelial surfaces. Here we present the crystal structure of UpaB, an autotransporter that is known to contribute to uropathogenic E. coli (UPEC) colonisation of the urinary tract. We provide evidence that UpaB can interact with glycosaminoglycans and host fibronectin. Unique modifications to its core β-helical structure create a groove on one side of the protein for interaction with glycosaminoglycans, while the opposite face can bind fibronectin. Our findings reveal far greater diversity in the autotransporter β-helix than previously thought, and suggest that this domain can interact with host macromolecules. The relevance of these interactions during infection remains unclear.

Indexed as

Adhesins, BacterialBacterial Outer Membrane ProteinsEscherichia coli ProteinsGlycosaminoglycansProtein Structure, SecondaryProtein Structure, TertiaryUropathogenic Escherichia coliVirulence FactorsAdhesins, BacterialBacterial Outer Membrane ProteinsEscherichia coli ProteinsGlycosaminoglycansVirulence Factors

Identifiers

PMID31036849
PMCPMC6488583
OpenAlexW2942218837

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.