Evidence map›Paper›PMID 15731033›Full record

ArticleInfection and immunity2005

Altered gingipain maturation in vimA- and vimE-defective isogenic mutants of Porphyromonas gingivalis.

Elaine Vanterpool, Francis Roy, Lawrence Sandberg, Hansel M Fletcher

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Complementation inJournal of bacteriology · 2021
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  10. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
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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

4 authors at 1 institution in 1 country.

Elaine VanterpoolDepartment of Biochemistry and Microbiology, School of Medicine, Loma Linda University, Loma Linda, California 92350, USA. eguiness02x@som.llu.edu
Francis Roy
Lawrence Sandberg
Hansel M Fletcher
Loma Linda University · US

Funding

NIH-LLU Initiative for Maximizing Student DiversityR25GM060507 · NIGMS · LOMA LINDA UNIVERSITY · PI DE LEON, MARINO · 2001 to 2022
$11.3M
Studies on virulence regulation in PorphyromonasR01DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2002 to 2011
$3.3M
Studies on the virulence regulation in PorphyromonasR56DE013664 · NIDCR · LOMA LINDA UNIVERSITY · PI FLETCHER, HANSEL M. · 2014 to 2014
$291k
NIDCR NIH HHS DE13664NIDCR NIH HHS DE13664-S1NIDCR NIH HHS R01 DE013664NIDCR NIH HHS R56 DE013664NIGMS NIH HHS GM60507NIGMS NIH HHS R25 GM060507
6 · The paper itself

Abstract

We have previously shown that gingipain activity in Porphyromonas gingivalis is modulated by the unique vimA and vimE genes. To determine if these genes had a similar phenotypic effect on protease maturation and activation, isogenic mutants defective in those genes were further characterized. Western blot analyses with antigingipain antibodies showed RgpA-, RgpB-, and Kgp-immunoreactive bands in membrane fractions as well as the culture supernatant of both P. gingivalis W83 and FLL93, the vimE-defective mutant. In contrast, the membrane of P. gingivalis FLL92, the vimA-defective mutant, demonstrated immunoreactivity only with RgpB antibodies. With mass spectrometry or Western blots, full-length RgpA and RgpB were identified from extracellular fractions. In similar extracellular fractions from P. gingivalis FLL92 and FLL93, purified RgpB activated only arginine-specific activity. In addition, the lipopolysaccharide profiles of the vimA and vimE mutants were truncated in comparison to that of W83. While glycosylated proteins were detected in the membrane and extracellular fractions from the vimA- and vimE-defective mutants, a monoclonal antibody (1B5) that reacts with specific sugar moieties of the P. gingivalis cell surface polysaccharide and membrane-associated Rgp gingipain showed no immunoreactivity with these fractions. Taken together, these results indicate a possible defect in sugar biogenesis in both the vimA- and vimE-defective mutants. These modulating genes play a role in the secretion, processing, and/or anchorage of gingipains on the cell surface.

Indexed as

MutationAdhesins, BacterialBacterial ProteinsCell MembraneCysteine EndopeptidasesEnzyme ActivationEnzyme PrecursorsGene Expression Regulation, BacterialGingipain Cysteine EndopeptidasesGlycosylationHemagglutininsHumansMembrane ProteinsPorphyromonas gingivalisAdhesins, BacterialBacterial ProteinsCysteine EndopeptidasesEnzyme PrecursorsGingipain Cysteine EndopeptidasesHemagglutininsMembrane Proteins

Identifiers

PMID15731033
PMCPMC1064936
OpenAlexW2172170936

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.