Evidence map›Paper›PMID 26032562›Full record

ArticleeLife2015

An internal thioester in a pathogen surface protein mediates covalent host binding.

Miriam Walden, John M Edwards, Aleksandra M Dziewulska, Rene Bergmann, Gerhard Saalbach, Su-Yin Kan, Ona K Miller, Miriam Weckener, Rosemary J Jackson, Sally L Shirran and 5 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 55 citations in OpenAlex.

  1. A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025
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  4. The current riboswitch landscape inMicrobiology (Reading, England) · 2024
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  8. Engineering Functional Membrane-Membrane Interfaces by InterSpy.Small (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. A new structural class of bacterial thioester domains reveals a slipknot topology.Protein science : a publication of the Protein Society · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 3 institutions in 2 countries.

Miriam WaldenDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
John M EdwardsBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Aleksandra M DziewulskaBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Rene BergmannCentral Facility for Microscopy, Helmholtz Centre for Infection Research, Braunschweig, Germany.
Gerhard SaalbachDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
Su-Yin KanBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Ona K MillerBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Miriam WeckenerBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Rosemary J JacksonBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Sally L ShirranBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Catherine H BottingBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Gordon J FlorenceBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
Manfred RohdeCentral Facility for Microscopy, Helmholtz Centre for Infection Research, Braunschweig, Germany.
Mark J BanfieldDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
Ulrich Schwarz-LinekBiomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom.
University of St Andrews · GBJohn Innes Centre · GBHelmholtz Centre for Infection Research · DE

Funding

Biotechnology and Biological Sciences Research Council BB/J00453Biotechnology and Biological Sciences Research Council BBS/E/J/000C0624Medical Research Council MR/K001485Medical Research Council MR/K001485/1Wellcome TrustWellcome Trust 063597Wellcome Trust 094476/Z/10/ZWellcome Trust 097831/Z/11/BWellcome Trust WT079272AIA
6 · The paper itself

Abstract

To cause disease and persist in a host, pathogenic and commensal microbes must adhere to tissues. Colonization and infection depend on specific molecular interactions at the host-microbe interface that involve microbial surface proteins, or adhesins. To date, adhesins are only known to bind to host receptors non-covalently. Here we show that the streptococcal surface protein SfbI mediates covalent interaction with the host protein fibrinogen using an unusual internal thioester bond as a 'chemical harpoon'. This cross-linking reaction allows bacterial attachment to fibrin and SfbI binding to human cells in a model of inflammation. Thioester-containing domains are unexpectedly prevalent in Gram-positive bacteria, including many clinically relevant pathogens. Our findings support bacterial-encoded covalent binding as a new molecular principle in host-microbe interactions. This represents an as yet unexploited target to treat bacterial infection and may also offer novel opportunities for engineering beneficial interactions.

Indexed as

Adhesins, BacterialCarrier ProteinsEscherichia coliFibrinFibrinogenHumansInflammationMembrane ProteinsAdhesins, BacterialCarrier ProteinsFibrinFibrinogenfibronectin-binding proteins, bacterialMembrane Proteinsbacterial surface proteinsbiophysicsClostridium perfringensfibrinogenhost-microbe interactionsinfectious diseasemicrobiologyStreptococcus pneumoniaeStreptococcus pyogenesstructural biology

Identifiers

PMID26032562
PMCPMC4450167
OpenAlexW2126827282

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.