Evidence map›Paper›PMID 27588694›Full record

ArticleMolecular microbiology2016

The TamB ortholog of Borrelia burgdorferi interacts with the β-barrel assembly machine (BAM) complex protein BamA.

Henna Iqbal, Melisha R Kenedy, Meghan Lybecker, Darrin R Akins

Open access · hybridAbstract 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 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 59 citations in OpenAlex.

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  13. YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2024
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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

4 authors at 2 institutions in 1 country.

Henna IqbalDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73104, USA.
Melisha R KenedyDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73104, USA.
Meghan LybeckerDepartment of Biology, University of Colorado - Colorado Springs, Colorado Springs, CO, 80918, USA.
Darrin R AkinsDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73104, USA.
University of Oklahoma Health Sciences Center · USUniversity of Colorado Colorado Springs · US

Funding

Outer Membrane Proteins of Borrelia burgdorferiR01AI059373 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI AKINS, DARRIN R. · 2005 to 2022
$4.7M
Outer membrane proteins of Borrelia burgdorferiR56AI059373 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI AKINS, DARRIN R. · 2011 to 2011
$329k
NIAID NIH HHS R01 AI059373NIAID NIH HHS R56 AI059373
6 · The paper itself

Abstract

Two outer membrane protein (OMP) transport systems in diderm bacteria assist in assembly and export of OMPs. These two systems are the β-barrel assembly machine (BAM) complex and the translocation and assembly module (TAM). The BAM complex consists of the OMP component BamA along with several outer membrane associated proteins. The TAM also consists of an OMP, designated TamA, and a single inner membrane (IM) protein, TamB. Together TamA and TamB aid in the secretion of virulence-associated OMPs. In this study we characterized the hypothetical protein BB0794 in Borrelia burgdorferi. BB0794 contains a conserved DUF490 domain, which is a motif found in all TamB proteins. All spirochetes lack a TamA ortholog, but computational and physicochemical characterization of BB0794 revealed it is a TamB ortholog. Interestingly, BB0794 was observed to interact with BamA and a BB0794 regulatable mutant displayed altered cellular morphology and antibiotic sensitivity. The observation that B. burgdorferi contains a TamB ortholog that interacts with BamA and is required for proper outer membrane biogenesis not only identifies a novel role for TamB-like proteins, but also may explain why most diderms harbor a TamB-like protein while only a select group encodes TamA.

Indexed as

Bacterial Outer Membrane ProteinsBorrelia burgdorferiDNA-Binding ProteinsProtein DomainsProtein FoldingProtein Structure, TertiaryProtein TransportStructure-Activity RelationshipBacterial Outer Membrane ProteinsDNA-Binding Proteins

Identifiers

PMID27588694
PMCPMC5582053
OpenAlexW2513227928

What OpenQuestion holds

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LicenceCC BY-NC
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.