Evidence map›Paper›PMID 15972484›Full record

ArticleInfection and immunity2005

Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83.

Elaine Vanterpool, Francis Roy, Hansel M Fletcher

Abstract 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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

34 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
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  4. Complementation inJournal of bacteriology · 2021
    Article
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  15. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. 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

3 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
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

Regulation/activation of the Porphyromonas gingivalis gingipains is poorly understood. A 1.2-kb open reading frame, a putative glycosyltransferase, downstream of vimE, was cloned, insertionally inactivated using the ermF-ermAM antibiotic resistance cassette, and used to create a defective mutant by allelic exchange. In contrast to the wild-type W83 strain, this mutant, designated P. gingivalis FLL95, was nonpigmented and nonhemolytic when plated on Brucella blood agar. Arginine- and lysine-specific gingipain activities were reduced by approximately 97% and 96%, respectively, relative to that of the parent strain. These activities were unaffected by the growth phase, in contrast to the vimA-defective mutant P. gingivalis FLL92. Expression of the rgpA, rgpB, and kgp gingipain genes was unaffected in P. gingivalis FLL95 in comparison to the wild-type strain. In nonactive gingipain extracellular protein fractions, multiple high-molecular-weight proteins immunoreacted with gingipain-specific antibodies. The specific gingipain-associated sugar moiety recognized by monoclonal antibody 1B5 was absent in FLL95. Taken together, these results suggest that the vimE downstream gene, designated vimF (virulence modulating gene F), which is a putative glycosyltransferase group 1, is involved in the regulation of the major virulence factors of P. gingivalis.

Indexed as

Adhesins, BacterialAllelesComputational BiologyCysteine EndopeptidasesEnzyme ActivationFibronectinsGingipain Cysteine EndopeptidasesGlycosylationGlycosyltransferasesHemagglutinationHemagglutininsPolymerase Chain ReactionPorphyromonas gingivalisVirulence FactorsAdhesins, BacterialCysteine EndopeptidasesFibronectinsGingipain Cysteine EndopeptidasesGlycosyltransferasesHemagglutininsVirulence Factors

Identifiers

PMID15972484
PMCPMC1168568
OpenAlexW2152462538

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.