Evidence map›Paper›PMID 27416872›Full record

ArticleMolecular microbiology2016

Spirochetes flagellar collar protein FlbB has astounding effects in orientation of periplasmic flagella, bacterial shape, motility, and assembly of motors in Borrelia burgdorferi.

Ki Hwan Moon, Xiaowei Zhao, Akarsh Manne, Juyu Wang, Zhou Yu, Jun Liu, Md A Motaleb

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.2field-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

27 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026
    Review
  3. FlgY, PflA, and PflB form a spoke-ring network in the high-torque flagellar motor ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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

7 authors at 2 institutions in 1 country.

Ki Hwan MoonDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA.
Xiaowei ZhaoDepartment of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston, TX, USA.
Akarsh ManneDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA.
Juyu WangDepartment of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston, TX, USA.
Zhou YuDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA.
Jun LiuDepartment of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston, TX, USA. Jun.Liu.1@uth.tmc.edu.
Md A MotalebDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, USA. motalebm@ecu.edu.
East Carolina University · USThe University of Texas Health Science Center at Houston · US

Funding

Structure-Function Relationships in the Spirochetal Flagellar MotorR01AI087946 · NIAID · YALE UNIVERSITY · PI LIU, JUN · 2010 to 2025
$6.6M
Delineation of Borrelia burgdorferi motility and chemotaxis in the development ofR01AR060834 · NIAMS · EAST CAROLINA UNIVERSITY · PI MOTALEB, MD A · 2011 to 2015
$1.8M
Discovery and characterization of novel flagellar proteins in Borrelia burgdorferiR21AI113014 · NIAID · EAST CAROLINA UNIVERSITY · PI MOTALEB, MD A · 2015 to 2016
$423k
NIAID NIH HHS R01 AI087946NIAID NIH HHS R21 AI113014NIAMS NIH HHS R01 AR060834
6 · The paper itself

Abstract

Borrelia burgdorferi, the causative agent of Lyme disease, is a highly motile spirochete, and motility, which is provided by its periplasmic flagella, is critical for every part of the spirochete's enzootic life cycle. Unlike externally flagellated bacteria, spirochetes possess a unique periplasmic flagellar structure called the collar. This spirochete-specific novel component is linked to the flagellar basal body; however, nothing is known about the proteins encoding the collar or their function in any spirochete. To identify a collar protein and determine its function, we employed a comprehensive strategy that included genetic, biochemical, and microscopic analyses. We found that BB0286 (FlbB) is a novel flagellar motor protein, which is located around the flagellar basal body. Deletion of bb0286 has a profound effect on collar formation, assembly of other flagellar structures, morphology, and motility of the spirochete. Orientation of the flagella toward the cell body is critical for determination of wild-type spirochete's wave-like morphology and motility. Here, we provide the first evidence that FlbB is a key determinant of normal orientation of the flagella and collar assembly.

Indexed as

Bacterial ProteinsBorrelia burgdorferiFlagellaMolecular Motor ProteinsPeriplasmSpirochaetalesTrans-ActivatorsBacterial ProteinsMolecular Motor ProteinsTrans-Activators

Identifiers

PMID27416872
PMCPMC5055450
OpenAlexW2480350628

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.