Evidence map›Paper›PMID 22144476›Full record

ArticleInfection and immunity2012

VimA-dependent modulation of acetyl coenzyme A levels and lipid A biosynthesis can alter virulence in Porphyromonas gingivalis.

A Wilson Aruni, J Lee, D Osbourne, Y Dou, F Roy, A Muthiah, D S Boskovic, H M Fletcher

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Protein lysine acetylation regulates oral microorganisms.Frontiers in cellular and infection microbiology · 2025
    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

8 authors at 2 institutions in 2 countries.

A Wilson AruniDivision of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, California, USA.
J Lee
D Osbourne
Y Dou
F Roy
A Muthiah
D S Boskovic
H M Fletcher
Loma Linda University · USKyung Hee University · KR

Funding

Studies on virulence regulation in PorphyromonasR01DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2002 to 2011
$3.3M
Mechanisms for adaptation to oxidative stress in Porphyromonas gingivalisR01DE019730 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2009 to 2013
$2.0M
Studies on the virulence regulation in PorphyromonasR56DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2014 to 2014
$291k
NIDCR NIH HHS DE-019730NIDCR NIH HHS DE-13664NIDCR NIH HHS R01 DE013664NIDCR NIH HHS R01 DE019730NIDCR NIH HHS R56 DE013664
6 · The paper itself

Abstract

The Porphyromonas gingivalis VimA protein has multifunctional properties that can modulate several of its major virulence factors. To further characterize VimA, P. gingivalis FLL406 carrying an additional vimA gene and a vimA-defective mutant in a different P. gingivalis genetic background were evaluated. The vimA-defective mutant (FLL451) in the P. gingivalis ATCC 33277 genetic background showed a phenotype similar to that of the vimA-defective mutant (FLL92) in the P. gingivalis W83 genetic background. In contrast to the wild type, gingipain activity was increased in P. gingivalis FLL406, a vimA chimeric strain. P. gingivalis FLL451 had a five times higher biofilm-forming capacity than the parent strain. HeLa cells incubated with P. gingivalis FLL92 showed a decrease in invasion, in contrast to P. gingivalis FLL451 and FLL406, which showed increases of 30 and 40%, respectively. VimA mediated coenzyme A (CoA) transfer to isoleucine and reduced branched-chain amino acid metabolism. The lipid A content and associated proteins were altered in the vimA-defective mutants. The VimA chimera interacted with several proteins which were found to have an LXXTG motif, similar to the sorting motif of gram-positive organisms. All the proteins had an N-terminal signal sequence with a putative sorting signal of L(P/T/S)X(T/N/D)G and two unique signatures of EXGXTX and HISXXGXG, in addition to a polar tail. Taken together, these observations further confirm the multifunctional role of VimA in modulating virulence possibly through its involvement in acetyl-CoA transfer and lipid A synthesis and possibly by protein sorting.

Indexed as

Acetyl Coenzyme AAdhesins, BacterialAmino AcidsAmino Acid SequenceBacterial ProteinsCysteine EndopeptidasesCytoskeletonEpithelial CellsGene Expression Regulation, BacterialGingipain Cysteine EndopeptidasesHeLa CellsHumansIsoleucineLipid AMolecular Sequence DataNeuraminidaseAcetyl Coenzyme AAdhesins, BacterialAmino AcidsBacterial ProteinsCysteine EndopeptidasesGingipain Cysteine EndopeptidasesIsoleucineLipid ANeuraminidase

Identifiers

PMID22144476
PMCPMC3264320
OpenAlexW2171087157

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.