Evidence map›Paper›PMID 21858145›Full record

ArticlePloS one2011

Probing the role of protein surface charge in the activation of PrfA, the central regulator of Listeria monocytogenes pathogenesis.

Bobbi Xayarath, Karl W Volz, Jennifer I Smart, Nancy E Freitag

Abstract read
In one paragraph

Article in PloS one, 2011. 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
–field-weighted citation impact
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.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Regulation ofMicrobiology spectrum · 2019
    Review
  7. Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. How Listeria monocytogenes organizes its surface for virulence.Frontiers in cellular and infection microbiology · 2014
    Review
  14. Article
  15. Review
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.

Bobbi XayarathDepartment of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois, United States of America.
Karl W Volz
Jennifer I Smart
Nancy E Freitag

Funding

Listeria Virulence Gene Expression Within Host CellsR01AI041816 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI FREITAG, NANCY ELIZABETH · 2001 to 2010
$3.9M
Listeria virulence gene expression within host cellsR56AI041816 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI FREITAG, NANCY ELIZABETH · 2012 to 2012
$399k
LISTERIA VIRULENCE GENE EXPRESSION WITHIN HOST CELLSR29AI041816 · NIAID · WAYNE STATE UNIVERSITY · PI FREITAG, NANCY · 1997 to 2001
$253k
NIAID NIH HHS AI41816NIAID NIH HHS R01 AI041816NIAID NIH HHS R29 AI041816NIAID NIH HHS R56 AI041816
6 · The paper itself

Abstract

Listeria monocytogenes is a food-borne intracellular bacterial pathogen capable of causing serious human disease. L. monocytogenes survival within mammalian cells depends upon the synthesis of a number of secreted virulence factors whose expression is regulated by the transcriptional activator PrfA. PrfA becomes activated following bacterial entry into host cells where it induces the expression of gene products required for bacterial spread to adjacent cells. Activation of PrfA appears to occur via the binding of a small molecule cofactor whose identity remains unknown. Electrostatic modeling of the predicted PrfA cofactor binding pocket revealed a highly positively charged region with two lysine residues, K64 and K122, located at the edge of the pocket and another (K130) located deep within the interior. Mutational analysis of these residues indicated that K64 and K122 contribute to intracellular activation of PrfA, whereas a K130 substitution abolished protein activity. The requirement of K64 and K122 for intracellular PrfA activation could be bypassed via the introduction of the prfA G145S mutation that constitutively activates PrfA in the absence of cofactor binding. Our data indicate that the positive charge of the PrfA binding pocket contributes to intracellular activation of PrfA, presumably by facilitating binding of an anionic cofactor.

Indexed as

Amino Acid SubstitutionAnimalsBacterial ProteinsBinding SitesBlotting, WesternHumansListeria monocytogenesListeriosisLysineMiceModels, MolecularMutationPeptide Termination FactorsProtein BindingProtein ConformationProtein Structure, TertiaryBacterial ProteinsLysinePeptide Termination FactorsPrfA protein, Listeria monocytogenes

Identifiers

PMID21858145
PMCPMC3155570

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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.