Evidence map›Paper›PMID 19074376›Full record

ArticleJournal of bacteriology2009

Essential role for the BacA protein in the uptake of a truncated eukaryotic peptide in Sinorhizobium meliloti.

Victoria L Marlow, Andreas F Haag, Hajime Kobayashi, Vivien Fletcher, Marco Scocchi, Graham C Walker, Gail P Ferguson

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
9.5field-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

37 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. BacA(SbmA) importer of legume symbiotic NCR peptides: Protein architecture, function, and evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Expression and mutagenesis studies in theFrontiers in plant science · 2023
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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 3 institutions in 3 countries.

Victoria L MarlowInstitute of Medical Sciences, University of Aberdeen, Foresterhill, United Kingdom.
Andreas F Haag
Hajime Kobayashi
Vivien Fletcher
Marco Scocchi
Graham C Walker
Gail P Ferguson
University of Aberdeen · GBMassachusetts Institute of Technology · USUniversity of Trieste · IT

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI NILES, JACQUIN C · 1985 to 2020
$25.6M
Biotechnology and Biological Sciences Research Council BB/D000564/1Medical Research Council G0501107Medical Research Council G0501107(75682)NIEHS NIH HHS P30 ES002109NIGMS NIH HHS GM31010
6 · The paper itself

Abstract

The inner membrane BacA protein is essential for the establishment of chronic intracellular infections by Sinorhizobium meliloti and Brucella abortus within plant and mammalian hosts, respectively. In their free-living state, S. meliloti and B. abortus mutants lacking BacA have reductions in their outer membrane lipid A very-long-chain fatty acid (VLCFA) contents and exhibit low-level resistance to the glycopeptide bleomycin in comparison to their respective parent strains. In this paper we investigate the hypothesis that BacA is involved in peptide uptake in S. meliloti. We determined that an S. meliloti DeltabacA mutant is completely resistant to a truncated form of the eukaryotic peptide Bac7, Bac7(1-16), and this phenotype appears to be independent of its lipid A alteration. Subsequently, we discovered that BacA and/or Escherichia coli SbmA is essential for fluorescently labeled Bac7(1-16) uptake in S. meliloti. Given that there are hundreds of root nodule-specific peptides within the legume host, our data suggest that BacA-mediated peptide uptake could play a central role in the chronic infection process of S. meliloti. However, since we determined that two symbiotically defective S. meliloti bacA site-directed mutants (with the Q193G and R389G mutations, respectively) with known reductions in their lipid A VLCFA contents are still capable of peptide uptake, these findings suggest that BacA-dependent peptide uptake cannot fully account for the essential role of BacA in the legume symbiosis. Further, they provide evidence that the BacA function that leads to the S. meliloti lipid A VLCFA modification plays a key role in the chronic infection of legumes.

Indexed as

Amino Acid SequenceAnimalsAnti-Infective AgentsBacterial ProteinsCattleMembrane Transport ProteinsMicrobial Sensitivity TestsMolecular Sequence DataMutationNeutrophilsPeptides, CyclicSinorhizobium melilotiAnti-Infective AgentsbacA protein, Rhizobium melilotibactenecinBacterial ProteinsMembrane Transport ProteinsPeptides, Cyclic

Identifiers

PMID19074376
PMCPMC2648212
OpenAlexW2122442673

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.