Evidence map›Paper›PMID 26079797›Full record

ReviewBiochimica et biophysica acta2015

Molecular determinants of bacterial sensitivity and resistance to mammalian Group IIA phospholipase A2.

Jerrold P Weiss

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Secretory phospholipase ACommunications biology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Group IIA-Secreted Phospholipase AInfection and immunity · 2018
    Article
  15. Article
  16. Article
  17. Biogenesis, transport and remodeling of lysophospholipids in Gram-negative bacteria.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  18. Article
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

1 author at 1 institution in 1 country.

Jerrold P WeissThe Inflammation Program, University of Iowa, Iowa City, IA 52242, USA; Department of Internal Medicine, University of Iowa, Iowa City, IA 52242, USA; Department of Microbiology, University of Iowa, Iowa City, IA 52242, USA; Veterans Administration Medical Center, Iowa City, IA 52246, USA. Electronic address: jerrold-weiss@uiowa.edu.
University of Iowa · US

Funding

Pulmonary Toxicology Facility CoreP30ES005605 · NIEHS · UNIVERSITY OF IOWA · PI HANS-JOACHIM LEHMLER · 1990 to 2026
$40.5M
NEUTROPHILS AND BACTERIAL PHOSPHOLIPID DEGRADATIONR01AI018571 · NIAID · UNIVERSITY OF IOWA · PI WEISS, JERROLD P · 1985 to 2002
$1.0M
NIAID NIH HHS R01 AI018571NIEHS NIH HHS P30 ES005605
6 · The paper itself

Abstract

Group IIA secretory phospholipase A2 (sPLA(2)-IIA) of mammalian species is unique among the many structurally and functionally related mammalian sPLA(2) in their high net positive charge and potent (nM) antibacterial activity. Toward the Gram-positive bacteria tested thus far, the global cationic properties of sPLA(2)-IIA are necessary for optimal binding to intact bacteria and penetration of the multi-layered thick cell wall, but not for the degradation of membrane phospholipids that is essential for bacterial killing. Various Gram-positive bacterial species can differ as much as 1000-fold in sPLA(2)-IIA sensitivity despite similar intrinsic enzymatic activity of sPLA(2)-IIA toward the membrane phospholipids of various bacteria. d-alanylation of wall- and lipo-teichoic acids in Staphylococcus aureus and sortase function in Streptococcus pyogenes increase bacterial resistance to sPLA(2)-IIA by up to 100-fold apparently by affecting translocation of bound sPLA(2)-IIA to the cell membrane. Action of the sPLA(2)-IIA and other related sPLA(2) against Gram-negative bacteria is more dependent on cationic properties of the enzyme near the amino-terminus of the protein and collaboration with other host defense proteins that produce alterations of the unique Gram-negative bacterial outer membrane that normally represents a barrier to sPLA(2)-IIA action. This article is part of a Special Issue entitled: Bacterial Resistance to Antimicrobial Peptides.

Indexed as

AnimalsAnti-Bacterial AgentsDrug Resistance, BacterialGram-Negative BacteriaGram-Negative Bacterial InfectionsGram-Positive BacteriaGram-Positive Bacterial InfectionsGroup II Phospholipases A2Host-Pathogen InteractionsHumansLipolysisMicrobial ViabilityPhospholipidsSignal TransductionSubstrate SpecificityAnti-Bacterial AgentsGroup II Phospholipases A2PhospholipidsBacterial sensitivityMammalian Group IIAMolecular determinantsPhospholipase A2Resistance to

Identifiers

PMID26079797
PMCPMC4605856
OpenAlexW593788348

What OpenQuestion holds

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LicenceTDM
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.