Evidence map›Paper›PMID 30905896›Full record

ArticleMicrobes and environments2019

Antimicrobial Activities of Cysteine-rich Peptides Specific to Bacteriocytes of the Pea Aphid Acyrthosiphon pisum.

Nahoko Uchi, Mitsutaka Fukudome, Narumi Nozaki, Miyuzu Suzuki, Ken-Ichi Osuki, Shuji Shigenobu, Toshiki Uchiumi

Open access · diamondAbstract read
In one paragraph

Article in Microbes and environments, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

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  6. DNA-binding and protein structure of nuclear factors likely acting in genetic information processing in theProceedings of the National Academy of Sciences of the United States of America · 2023
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  13. Genome-Wide Comprehensive Analysis of theInternational journal of molecular sciences · 2021
    Article
  14. Review
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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.

Nahoko UchiGraduate School of Science and Engineering, Kagoshima University.
Mitsutaka FukudomeGraduate School of Science and Engineering, Kagoshima University.
Narumi NozakiGraduate School of Science and Engineering, Kagoshima University.
Miyuzu SuzukiNational Institute for Basic Biology.
Ken-Ichi OsukiGraduate School of Science and Engineering, Kagoshima University.
Shuji ShigenobuNational Institute for Basic Biology.
Toshiki UchiumiGraduate School of Science and Engineering, Kagoshima University.
Kagoshima University · JPNational Institute for Basic Biology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aphids have a mutualistic relationship with the bacterial endosymbiont Buchnera aphidicola. We previously reported seven cysteine-rich peptides in the pea aphid Acyrthosiphon pisum and named them Bacteriocyte-specific Cysteine-Rich (BCR) peptides; these peptides are exclusively expressed in bacteriocytes, special aphid cells that harbor symbionts. Similar symbiotic organ-specific cysteine-rich peptides identified in the root nodules of leguminous plants are named Nodule-specific Cysteine-Rich (NCR) peptides. NCR peptides target rhizobia in the nodules and are essential for symbiotic nitrogen fixation. A BacA (membrane protein) mutant of Sinorhizobium is sensitive to NCR peptides and is unable to establish symbiosis. Based on the structural and expressional similarities between BCR peptides and NCR peptides, we hypothesized that aphid BCR peptides exhibit antimicrobial activity, similar to some NCR peptides. We herein synthesized BCR peptides and investigated their antimicrobial activities and effects on the bacterial membrane of Escherichia coli. The peptides BCR1, BCR3, BCR5, and BCR8 exhibited antimicrobial activities with increased membrane permeability. An sbmA mutant of E. coli, a homolog of bacA of S. meliloti, was more sensitive to BCR peptides than the wild type. Our results suggest that BCR peptides have properties that may be required to control the endosymbiont, similar to NCR peptides in legumes.

Indexed as

AnimalsAnti-Infective AgentsAphidsBuchneraCell Membrane PermeabilityCysteineEscherichia coliInsect ProteinsMutationPeptidesSinorhizobium melilotiSymbiosisAnti-Infective AgentsCysteineInsect ProteinsPeptidesaphidbacteriocyteBuchneracysteine-rich peptidesymbiosis

Identifiers

PMID30905896
PMCPMC6594739
OpenAlexW2922727917

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.