Evidence map›Paper›PMID 41309349›Full record

ReviewTrends in microbiology2026

PilY proteins: bimodular drivers of type IV pilus versatility.

Taylor A Yount, Niharika Shukla, Yi-Wei Chang, Joseph W St Geme

Abstract readReview
In one paragraph

Review in Trends in microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

4 authors.

Taylor A YountUniversity of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, USA; Department of Pediatrics, Children's Hospital of Philadelphia, Philadelphia, PA, USA.
Niharika ShuklaUniversity of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, USA; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA; Institute of Structural Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA; Department of Pediatrics, Children's Hospital of Philadelphia, Philadelphia, PA, USA.
Yi-Wei ChangDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA; Institute of Structural Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA. Electronic address: ywc@pennmedicine.upenn.edu.
Joseph W St GemeUniversity of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, USA; Department of Pediatrics, Children's Hospital of Philadelphia, Philadelphia, PA, USA. Electronic address: stgemeiiij@chop.edu.

Funding

Medical Scientist Training ProgramT32GM148377 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Michael Lee Atchison, LAWRENCE F BRASS · 2023 to 2026
$12.0M
Structural biology and molecular biophysics training programT32GM132039 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ben E. Black, Elizabeth Rhoades · 2019 to 2026
$3.3M
Pathogenicity of the emerging pathogen Kingella kingaeR01AI172841 · NIAID · CHILDREN'S HOSP OF PHILADELPHIA · PI Joseph W. St. Geme · 2023 to 2026
$1.8M
Training in Microbial Pathogenesis and GenomicsT32AI141393 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI GOULIAN, MARK D, ZHU, JUN · 2019 to 2023
$1.3M
Molecular Mechanisms and Evolution of the Rhoptry Secretion SystemR35GM156396 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI YI-WEI CHANG · 2025 to 2026
$957k
NIAID NIH HHS R01 AI172841NIAID NIH HHS T32 AI141393NIGMS NIH HHS R35 GM156396NIGMS NIH HHS T32 GM132039NIGMS NIH HHS T32 GM148377
6 · The paper itself

Abstract

Type IV pili (T4P) are dynamic surface fibers that mediate diverse bacterial activities, including adhesion, twitching motility, horizontal gene transfer, biofilm formation, and virulence. The PilY family of T4P-associated proteins are found across a wide range of bacterial species and are critical for key T4P functions. PilY proteins are characterized by a shared domain architecture which consists of a variable N-terminal region that mediates adhesion and a conserved C-terminal beta-propeller domain that facilitates pilus biogenesis. Given their surface exposure and roles in virulence, PilY family proteins represent an attractive target for novel therapeutic interventions, including small-molecule antivirulence therapies against pathogenic bacteria and potential as vaccine antigens. This review synthesizes our current understanding of PilY structure, localization, function, and evolutionary relationships across T4P systems.

Indexed as

BacteriaBacterial ProteinsFimbriae, BacterialFimbriae ProteinsBacterial AdhesionVirulenceBacterial ProteinsFimbriae Proteinsadhesinsbiofilmnatural competencetwitching motilitytype IV pilivirulence

Identifiers

PMID41309349
PMCPMC12671570

What Socratic 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 Socratic graph.