Evidence map›Paper›PMID 20159471›Full record

ArticleStructure (London, England : 1993)2010

AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin.

Carrie-Lynn Keiski, Michael Harwich, Sumita Jain, Ana Mirela Neculai, Patrick Yip, Howard Robinson, John C Whitney, Laura Riley, Lori L Burrows, Dennis E Ohman and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

59 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Advances in alginate biosynthesis: regulation and production inFrontiers in bioengineering and biotechnology · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Boron Derivatives Accelerate Biofilm Formation of RecombinantInternational journal of molecular sciences · 2022
    Article
  12. Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022
    Article
  13. Frontiers in microbiology · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. TheThe Journal of biological chemistry · 2020
    Article
  18. TOR dynamically regulates plant cell-cell transport.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 2 countries.

Carrie-Lynn KeiskiMolecular Structure and Function, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Michael Harwich
Sumita Jain
Ana Mirela Neculai
Patrick Yip
Howard Robinson
John C Whitney
Laura Riley
Lori L Burrows
Dennis E Ohman
P Lynne Howell
Hospital for Sick Children · CAVirginia Commonwealth University Medical Center · USUniversity of Toronto · CABrookhaven National Laboratory · USMcMaster University · CA

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
GENETICS OF ALGINATE BIOSYNTHESIS IN P. AERUGINOSAR01AI019146 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI OHMAN, DENNIS EDWARD · 1985 to 2011
$2.7M
Activation of Alginate Genes in Pseudomonas aeruginosaR56AI019146 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI OHMAN, DENNIS EDWARD · 2006 to 2013
$682k
Pathogenic Mechanism for Lung Infection in Mucoid PseudomonasI01BX000477 · VA · VA VETERANS ADMINISTRATION HOSPITAL · PI OHMAN, DENNIS EDWARD, ZHOU, HUIPING · 2011 to 2025
–
BLRD VA I01 BX000477CIHR MT13337NIAID NIH HHS R01 AI019146NIAID NIH HHS R56 AI019146NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

The opportunistic pathogen Pseudomonas aeruginosa causes chronic biofilm infections in cystic fibrosis patients. During colonization of the lung, P. aeruginosa converts to a mucoid phenotype characterized by overproduction of the exopolysaccharide alginate. Here we show that AlgK, a protein essential for production of high molecular weight alginate, is an outer membrane lipoprotein that contributes to the correct localization of the porin AlgE. Our 2.5 A structure shows AlgK is composed of 9.5 tetratricopeptide-like repeats, and three putative sites of protein-protein interaction have been identified. Bioinformatics analysis suggests that BcsA, PgaA, and PelB, involved in the production and export of cellulose, poly-beta-1,6-N-Acetyl-D-glucosamine, and Pel exopolysaccharide, respectively, share the same topology as AlgK/E. Together, our data suggest that AlgK plays a role in the assembly of the alginate biosynthetic complex and represents the periplasmic component of a new type of outer membrane secretin that differs from canonical bacterial capsular polysaccharide secretion systems.

Indexed as

Pseudomonas aeruginosaAlginatesBacterial ProteinsBinding SitesBiofilmsCrystallography, X-RayGlucuronic AcidHexuronic AcidsHumansModels, MolecularMolecular Sequence DataPolysaccharides, BacterialProtein Structure, TertiarySecretinAlginatesAlgK protein, Pseudomonas aeruginosaBacterial ProteinsGlucuronic AcidHexuronic AcidsPolysaccharides, BacterialSecretin

Identifiers

PMID20159471
PMCPMC2857933
OpenAlexW1966701251

What OpenQuestion holds

Textmetadata
LicenceTDM
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.