Evidence map›Paper›PMID 27307578›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2016

Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.

Marietta Flores-Díaz, Laura Monturiol-Gross, Claire Naylor, Alberto Alape-Girón, Antje Flieger

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

103 citing papers in PubMed, 207 citations in OpenAlex.

  1. Article
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  10. Extracellular Vesicles fromInternational journal of molecular sciences · 2025
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  14. The virulence toolkit of Staphylococcus aureus: a comprehensive review of toxin diversity, molecular mechanisms, and clinical implications.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Review
  15. Dual Role for Pld1 inJournal of proteome research · 2025
    Article
  16. Article
  17. Article
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  19. Review
  20. Article

43 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 3 countries.

Marietta Flores-DíazInstituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
Laura Monturiol-GrossInstituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
Claire NaylorDepartment of Biological Sciences, Birkbeck College, London, United Kingdom.
Alberto Alape-GirónInstituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica Departamento de Bioquímica, Escuela de Medicina, Universidad de Costa Rica, San José, Costa Rica alberto.alape@ucr.ac.cr fliegera@rki.de.
Antje FliegerDivision of Enteropathogenic Bacteria and Legionella, Robert Koch-Institut, Wernigerode, Germany alberto.alape@ucr.ac.cr fliegera@rki.de.
Universidad de Costa Rica · CRBirkbeck, University of London · GBRobert Koch Institute · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial sphingomyelinases and phospholipases are a heterogeneous group of esterases which are usually surface associated or secreted by a wide variety of Gram-positive and Gram-negative bacteria. These enzymes hydrolyze sphingomyelin and glycerophospholipids, respectively, generating products identical to the ones produced by eukaryotic enzymes which play crucial roles in distinct physiological processes, including membrane dynamics, cellular signaling, migration, growth, and death. Several bacterial sphingomyelinases and phospholipases are essential for virulence of extracellular, facultative, or obligate intracellular pathogens, as these enzymes contribute to phagosomal escape or phagosomal maturation avoidance, favoring tissue colonization, infection establishment and progression, or immune response evasion. This work presents a classification proposal for bacterial sphingomyelinases and phospholipases that considers not only their enzymatic activities but also their structural aspects. An overview of the main physiopathological activities is provided for each enzyme type, as are examples in which inactivation of a sphingomyelinase- or a phospholipase-encoding gene impairs the virulence of a pathogen. The identification of sphingomyelinases and phospholipases important for bacterial pathogenesis and the development of inhibitors for these enzymes could generate candidate vaccines and therapeutic agents, which will diminish the impacts of the associated human and animal diseases.

Indexed as

BacillotaBacteriaFungiPhospholipase DPhosphoric Diester HydrolasesProteobacteriaSphingomyelin PhosphodiesteraseStaphylococcus aureusType C PhospholipasesVirulence FactorsPhospholipase DPhosphoric Diester HydrolasesSphingomyelin Phosphodiesterasesphingomyelin phosphodiesterase DType C PhospholipasesVirulence Factors

Identifiers

PMID27307578
PMCPMC4981679
OpenAlexW2425269867

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.