Evidence map›Paper›PMID 35486648›Full record

ArticlePLoS genetics2022

The differential expression of PilY1 proteins by the HsfBA phosphorelay allows twitching motility in the absence of exopolysaccharides.

Shuanghong Xue, Romain Mercier, Annick Guiseppi, Artemis Kosta, Rossella De Cegli, Severine Gagnot, Tâm Mignot, Emilia M F Mauriello

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Milestones in the development ofJournal of bacteriology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Deciphering the enigmatic PilY1 ofBiochemistry and biophysics reports · 2024
    Article
  11. Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Review
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

8 authors at 2 institutions in 2 countries.

Shuanghong XueLaboratoire de Chimie Bactérienne, CNRS, Aix-Marseille Univ, Marseille, France.ORCID 0000-0001-9066-4625
Romain MercierLaboratoire de Chimie Bactérienne, CNRS, Aix-Marseille Univ, Marseille, France.
Annick GuiseppiLaboratoire de Chimie Bactérienne, CNRS, Aix-Marseille Univ, Marseille, France.
Artemis KostaMicroscopy Platform, Institut de Microbiologie de la Méditerranée, CNRS, Marseille, France.ORCID 0000-0001-7115-4566
Rossella De CegliTelethon Institute of Genetics and Medicine (TIGEM), Naples, Italie.
Severine GagnotLaboratoire de Chimie Bactérienne, CNRS, Aix-Marseille Univ, Marseille, France.
Tâm MignotLaboratoire de Chimie Bactérienne, CNRS, Aix-Marseille Univ, Marseille, France.ORCID 0000-0003-4338-9063
Emilia M F MaurielloLaboratoire de Chimie Bactérienne, CNRS, Aix-Marseille Univ, Marseille, France.ORCID 0000-0001-9770-6138
Centre National de la Recherche Scientifique · FRTelethon Institute Of Genetics And Medicine · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type Four Pili (T4P) are extracellular appendages mediating several bacterial functions such as motility, biofilm formation and infection. The ability to adhere to substrates is essential for all these functions. In Myxococcus xanthus, during twitching motility, the binding of polar T4P to exopolysaccharides (EPS), induces pilus retraction and the forward cell movement. EPS are produced, secreted and weakly associated to the M. xanthus cell surface or deposited on the substrate. In this study, a genetic screen allowed us to identify two factors involved in EPS-independent T4P-dependent twitching motility: the PilY1.1 protein and the HsfBA phosphorelay. Transcriptomic analyses show that HsfBA differentially regulates the expression of PilY1 proteins and that the down-regulation of pilY1.1 together with the accumulation of its homologue pilY1.3, allows twitching motility in the absence of EPS. The genetic and bioinformatic dissection of the PilY1.1 domains shows that PilY1.1 might be a bi-functional protein with a role in priming T4P extension mediated by its conserved N-terminal domain and roles in EPS-dependent motility mediated by an N-terminal DUF4114 domain activated upon binding to Ca2+. We speculate that the differential transcriptional regulation of PilY1 homologs by HsfBA in response to unknown signals, might allow accessorizing T4P tips with different modules allowing twitching motility in the presence of alternative substrates and environmental conditions.

Indexed as

Fimbriae ProteinsMyxococcus xanthusBacterial ProteinsCell MovementFimbriae, BacterialBacterial ProteinsFimbriae Proteins

Identifiers

PMID35486648
PMCPMC9109919
OpenAlexW4225117090

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.