Evidence map›Paper›PMID 29339761›Full record

ArticleScientific reports2018

New virulence factor CSK29544_02616 as LpxA binding partner in Cronobacter sakazakii.

Seongok Kim, Hyunjin Yoon, Sangryeol Ryu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. DecipheringMicroorganisms · 2026
    Review
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  3. Targeted dual-receptor phage cocktail againstFrontiers in microbiology · 2024
    Article
  4. Article
  5. Article
  6. The lipoprotein NlpD inVirulence · 2021
    Article
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 2 institutions in 1 country.

Seongok KimDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, and Center for Food and Bioconvergence, Seoul National University, Seoul, 08826, Korea.
Hyunjin YoonDepartment of Molecular Science and Technology, Department of Applied Chemistry and Biological Engineering, Ajou University, Suwon, 16499, South Korea. yoonh@ajou.ac.kr.
Sangryeol RyuDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, and Center for Food and Bioconvergence, Seoul National University, Seoul, 08826, Korea. sangryu@snu.ac.kr.
Seoul National University · KRAjou University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cronobacter sakazakii is an opportunistic pathogen that can cause meningitis and necrotizing enterocolitis in premature infants, but its virulence determinants remain largely unknown. In this study, a transposon-mediated random-mutant library of C. sakazakii was used to identify new virulence factors. Compared to wild-type bacteria, a mutant lacking CSK29544_02616 (referred to as labp) was defective in invasion into intestinal epithelial cells (by at least 1000-fold) and showed less phagocytosis by macrophages (by at least 50-fold). The lack of labp in C. sakazakii changed the profile of outer membrane proteins, decreased the production of lipopolysaccharides, and increased the production of membrane phospholipids. Bacterial physiological characteristics including surface hydrophobicity and motility were also altered in the absence of labp, presumably because of changes in the bacterial-envelope structure. To systematically determine the role of labp, ligand fishing was conducted using Labp as a bait, which revealed LpxA as a binding partner of Labp. LpxA is UDP-N-acetylglucosamine (GlcNAc) acyltransferase, the first enzyme in the pathway of lipid A biosynthesis. Labp increased the enzymatic activity of LpxA without influencing lpxA expression. Considering multifaceted roles of lipopolysaccharides in virulence regulation, Labp is a novel virulence factor that promotes the production of lipid A by LpxA in Cronobacter.

Indexed as

AcyltransferasesAnimalsBacterial Outer Membrane ProteinsCronobacter sakazakiiEpithelial CellsHeLa CellsHumansLipopolysaccharidesMacrophagesMiceMutagenesis, Site-DirectedPhagocytosisPhospholipidsProtein BindingRatsRats, Sprague-Dawleyacyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferaseAcyltransferasesBacterial Outer Membrane ProteinsLipopolysaccharidesPhospholipidsVirulence Factors

Identifiers

PMID29339761
PMCPMC5770445
OpenAlexW2783202188

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.