Evidence map›Paper›PMID 10074489›Full record

ArticleThe Journal of clinical investigation1999

Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against Gram-positive bacteria.

A K Foreman-Wykert, Y Weinrauch, P Elsbach, J Weiss

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Modulation of the immune response by theFrontiers in cellular and infection microbiology · 2022
    Review
  6. Human Group IIA Phospholipase AMolecules (Basel, Switzerland) · 2021
    Review
  7. Article
  8. Group IIA-Secreted Phospholipase AInfection and immunity · 2018
    Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Genetics of kidney failure and the evolving story of APOL1.The Journal of clinical investigation · 2011
    Review
  19. Article
  20. Bacterial resistance mechanisms against host defense peptides.Cellular and molecular life sciences : CMLS · 2011
    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 at 2 institutions in 1 country.

A K Foreman-WykertDepartment of Microbiology, New York University School of Medicine, New York 10016, USA.
Y Weinrauch
P Elsbach
J Weiss
New York University · USUniversity of Iowa · US

Funding

NEUTROPHILS AND BACTERIAL PHOSPHOLIPID DEGRADATIONR01AI018571 · NIAID · UNIVERSITY OF IOWA · PI WEISS, JERROLD P · 1985 to 2002
$1.0M
NIAID NIH HHS AI-18571NIAID NIH HHS R01 AI018571
6 · The paper itself

Abstract

We have shown previously that a group IIA phospholipase A2 (PLA2) is responsible for the potent bactericidal activity of inflammatory fluids against many Gram-positive bacteria. To exert its antibacterial activity, this PLA2 must first bind and traverse the bacterial cell wall to produce the extensive degradation of membrane phospholipids (PL) required for bacterial killing. In this study, we have examined the properties of the cell-wall that may determine the potency of group IIA PLA2 action. Inhibition of bacterial growth by nutrient deprivation or a bacteriostatic antibiotic reversibly increased bacterial resistance to PLA2-triggered PL degradation and killing. Conversely, pretreatment of Staphylococcus aureus or Enterococcus faecium with subinhibitory doses of beta-lactam antibiotics increased the rate and extent of PL degradation and/or bacterial killing after addition of PLA2. Isogenic wild-type (lyt+) and autolysis-deficient (lyt-) strains of S. aureus were equally sensitive to the phospholipolytic action of PLA2, but killing and lysis was much greater in the lyt+ strain. Thus, changes in cell-wall cross-linking and/or autolytic activity can modulate PLA2 action either by affecting enzyme access to membrane PL or by the coupling of massive PL degradation to autolysin-dependent killing and bacterial lysis or both. Taken together, these findings suggest that the bacterial envelope sites engaged in cell growth may represent preferential sites for the action and cytotoxic consequences of group IIA PLA2 attack against Gram-positive bacteria.

Indexed as

Anti-Bacterial AgentsCell WallDrug InteractionsEnterococcus faeciumLactamsPhospholipases APhospholipases A2Staphylococcus aureusAnti-Bacterial AgentsLactamsPhospholipases APhospholipases A2

Identifiers

PMID10074489
PMCPMC408128
OpenAlexW2146904916

What OpenQuestion holds

Texttitle and abstract
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.