Evidence map›Paper›PMID 24837291›Full record

ArticleJournal of bacteriology2014

Structural features of the Pseudomonas fluorescens biofilm adhesin LapA required for LapG-dependent cleavage, biofilm formation, and cell surface localization.

Chelsea D Boyd, T Jarrod Smith, Sofiane El-Kirat-Chatel, Peter D Newell, Yves F Dufrêne, George A O'Toole

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

61 citing papers in PubMed, 109 citations in OpenAlex.

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  19. Biology · 2022
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  20. TheMicrobiology spectrum · 2022
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1 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Chelsea D BoydDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
T Jarrod SmithDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
Sofiane El-Kirat-ChatelInstitute of Life Sciences, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Peter D NewellDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
Yves F DufrêneInstitute of Life Sciences, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
George A O'TooleDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA georgeo@dartmouth.edu.
Dartmouth College · USUCLouvain · BE

Funding

HOST-MICROBE INTERACTIONST32AI007519 · NIAID · DARTMOUTH COLLEGE · PI DEBORAH A HOGAN · 1997 to 2026
$5.9M
Molecular mechanism regulating periplasmic proteolysis in bacterial pathogenesisR01AI097307 · NIAID · CORNELL UNIVERSITY · PI O'TOOLE, GEORGE A., SONDERMANN, HOLGER · 2012 to 2016
$1.9M
NIAID NIH HHS R01 AI097307NIAID NIH HHS T32 AI007519
6 · The paper itself

Abstract

The localization of the LapA protein to the cell surface is a key step required by Pseudomonas fluorescens Pf0-1 to irreversibly attach to a surface and form a biofilm. LapA is a member of a diverse family of predicted bacterial adhesins, and although lacking a high degree of sequence similarity, family members do share common predicted domains. Here, using mutational analysis, we determine the significance of each domain feature of LapA in relation to its export and localization to the cell surface and function in biofilm formation. Our previous work showed that the N terminus of LapA is required for cleavage by the periplasmic cysteine protease LapG and release of the adhesin from the cell surface under conditions unfavorable for biofilm formation. We define an additional critical region of the N terminus of LapA required for LapG proteolysis. Furthermore, our results suggest that the domains within the C terminus of LapA are not absolutely required for biofilm formation, export, or localization to the cell surface, with the exception of the type I secretion signal, which is required for LapA export and cell surface localization. In contrast, deletion of the central repetitive region of LapA, consisting of 37 repeats of 100 amino acids, results in an inability to form a biofilm. We also used single-molecule atomic force microscopy to further characterize the role of these domains in biofilm formation on hydrophobic and hydrophilic surfaces. These studies represent the first detailed analysis of the domains of the LapA family of biofilm adhesin proteins.

Indexed as

Adhesins, BacterialAmino Acid MotifsAmino Acid SequenceBacterial ProteinsBase SequenceBiofilmsComputational BiologyGene ExpressionHydrophobic and Hydrophilic InteractionsLectinsMicroscopy, Atomic ForceMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryProteolysisPseudomonas fluorescensadhesin, PseudomonasAdhesins, BacterialBacterial ProteinsLectins

Identifiers

PMID24837291
PMCPMC4135675
OpenAlexW2059933240

What OpenQuestion holds

Textmetadata
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.