Evidence map›Paper›PMID 22287518›Full record

ArticleJournal of bacteriology2012

Mutational analyses reveal overall topology and functional regions of NilB, a bacterial outer membrane protein required for host association in a model of animal-microbe mutualism.

Archna Bhasin, John M Chaston, Heidi Goodrich-Blair

Abstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026
    Review
  2. Pleiotropic role of PAX cyclolipopeptides in theApplied and environmental microbiology · 2025
    Article
  3. Article
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  13. Visualizing bacteria in nematodes using fluorescent microscopy.Journal of visualized experiments : JoVE · 2012
    Article
  14. 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

3 authors at 1 institution in 1 country.

Archna BhasinDepartment of Bacteriology, University of Wisconsin—Madison, Madison, WI, USA.
John M Chaston
Heidi Goodrich-Blair
University of Wisconsin–Madison · US

Funding

Microbial Pathogenesis &Host Responses Training ProgramT32AI055397 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KLEIN, BRUCE STEVEN · 2003 to 2024
$5.5M
Molecular mechanisms of X. nematophila-nematode interactionR01GM059776 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GOODRICH-BLAIR, HEIDI · 1999 to 2007
$2.4M
Mutualism between X. nematophila and S. carpocapsaeF32GM072342 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BHASIN, ARCHNA · 2004 to 2005
$91k
NIAID NIH HHS AI55397NIAID NIH HHS T32 AI055397NIGMS NIH HHS F32 GM072342NIGMS NIH HHS GM059776NIGMS NIH HHS R01 GM059776
6 · The paper itself

Abstract

The gammaproteobacterium Xenorhabdus nematophila is a mutualistic symbiont that colonizes the intestine of the nematode Steinernema carpocapsae. nilB (nematode intestine localization) is essential for X. nematophila colonization of nematodes and is predicted to encode an integral outer membrane beta-barrel protein, but evidence supporting this prediction has not been reported. The function of NilB is not known, but when expressed with two other factors encoded by nilA and nilC, it confers upon noncognate Xenorhabdus spp. the ability to colonize S. carpocapsae nematodes. We present evidence that NilB is a surface-exposed outer membrane protein whose expression is repressed by NilR and growth in nutrient-rich medium. Bioinformatic analyses reveal that NilB is the only characterized member of a family of proteins distinguished by N-terminal region tetratricopeptide repeats (TPR) and a conserved C-terminal domain of unknown function (DUF560). Members of this family occur in diverse bacteria and are prevalent in the genomes of mucosal pathogens. Insertion and deletion mutational analyses support a beta-barrel structure model with an N-terminal globular domain, 14 transmembrane strands, and seven extracellular surface loops and reveal critical roles for the globular domain and surface loop 6 in nematode colonization. Epifluorescence microscopy of these mutants demonstrates that NilB is necessary at early stages of colonization. These findings are an important step in understanding the function of NilB and, by extension, its homologs in mucosal pathogens.

Indexed as

SymbiosisAmino Acid SequenceAnimalsBacterial Outer Membrane ProteinsIntestinesModels, AnimalMolecular Sequence DataProtein Structure, TertiaryRhabditidaXenorhabdusBacterial Outer Membrane Proteins

Identifiers

PMID22287518
PMCPMC3302474
OpenAlexW2092490323

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.