Evidence map›Paper›PMID 22422753›Full record

ReviewMicrobiology (Reading, England)2012

Multiple leptospiral sphingomyelinases (or are there?).

Suneel A Narayanavari, Manjula Sritharan, David A Haake, James Matsunaga

Erratum issuedOpen access · bronzeAbstract readReview
In one paragraph

Review in Microbiology (Reading, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Leptospirosis.Nature reviews. Disease primers · 2025
    Review
  3. Article
  4. Article
  5. Evolutionary insights into the emergence of virulentbioRxiv : the preprint server for biology · 2024
    Article
  6. Sph2Vaccines · 2023
    Article
  7. PathogenicFrontiers in microbiology · 2022
    Article
  8. Pathogen-specific leptospiral proteins in urine of patients with febrile illness aids in differential diagnosis of leptospirosis from dengue.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2018
    Article
  9. PathogenicOpen veterinary journal · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Leptospiral pathogenomics.Pathogens (Basel, Switzerland) · 2014
    Review
  14. Article
  15. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Suneel A NarayanavariDepartment of Animal Sciences, University of Hyderabad, Hyderabad, India.
Manjula SritharanDepartment of Animal Sciences, University of Hyderabad, Hyderabad, India.
David A HaakeDepartment of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
James MatsunagaResearch Service, VA Greater Los Angeles Healthcare System, Los Angeles, CA, USA.
University of Hyderabad · INVA Greater Los Angeles Healthcare System · US

Funding

Outer Membrane Proteins of Pathogenic Leptospira SpeciesR01AI034431 · NIAID · BRENTWOOD BIOMEDICAL RESEARCH INSTITUTE · PI GOMES-SOLECKI, MARIA, HAAKE, DAVID A · 2003 to 2015
$4.1M
OUTER MEMBRANE PROTEINS OF PATHOGENIC LEPTOSPIRA SPECIESR21AI034431 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HAAKE, DAVID A · 2001 to 2001
$252k
OUTER MEMBRANE PROTEINS OF PATHOGENIC LEPTOSPIRA SPECIESR29AI034431 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HAAKE, DAVID A · 1996 to 2000
$91k
NIAID NIH HHS AI-034431NIAID NIH HHS R01 AI034431NIAID NIH HHS R21 AI034431NIAID NIH HHS R29 AI034431
6 · The paper itself

Abstract

Culture supernatants of leptospiral pathogens have long been known to haemolyse erythrocytes. This property is due, at least in part, to sphingomyelinase activity. Indeed, genome sequencing reveals that pathogenic Leptospira species are richly endowed with sphingomyelinase homologues: five genes have been annotated to encode sphingomyelinases in Leptospira interrogans. Such redundancy suggests that this class of genes is likely to benefit leptospiral pathogens in their interactions with the mammalian host. Surprisingly, sequence comparison with bacterial sphingomyelinases for which the crystal structures are known reveals that only one of the leptospiral homologues has the active site amino acid residues required for enzymic activity. Based on studies of other bacterial toxins, we propose that leptospiral sphingomyelinase homologues, irrespective of their catalytic activity, may possess additional molecular functions that benefit the spirochaete. Potential secretion pathways and roles in pathogenesis are discussed, including nutrient acquisition, dissemination, haemorrhage and immune evasion. Although leptospiral sphingomyelinase-like proteins are best known for their cytolytic properties, we believe that a better understanding of their biological role requires the examination of their sublytic properties as well.

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainCell MembraneLeptospira interrogansLeptospirosisPhylogenySphingolipidsSphingomyelin PhosphodiesteraseSphingomyelinsBacterial ProteinsSphingolipidsSphingomyelin PhosphodiesteraseSphingomyelins

Identifiers

PMID22422753
PMCPMC3542825
OpenAlexW2159845756

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.