Evidence map›Paper›PMID 23323152›Full record

ArticlePloS one2013

LipL32 Is a Subsurface Lipoprotein of Leptospira interrogans: presentation of new data and reevaluation of previous studies.

Marija Pinne, David A Haake

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
8.6field-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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. UnveilingFrontiers in public health · 2025
    Article
  5. Article
  6. Article
  7. Lipoproteome screening of the Lyme disease agent identifies inhibitors of antibody-mediated complement killing.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Analytical evaluation of an immunomagnetic separation PCR assay to detect pathogenicJournal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2021
    Article
  12. Article
  13. Article
  14. Protein Secretion in Spirochetes.Microbiology spectrum · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Marija PinneResearch Service, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California, United States of America.
David A Haake
University of California, Los Angeles · 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 R01 AI034431NIAID NIH HHS R21 AI034431NIAID NIH HHS R29 AI034431
6 · The paper itself

Abstract

The agents of leptospirosis, a zoonosis with worldwide distribution, are pathogenic spirochetes belonging to the genus Leptospira. The leptospiral life cycle involves transmission via fresh water and colonization of the renal tubules of their reservoir hosts. Infection of accidental hosts, including humans, may result in life-threatening sequelae. Bacterial outer membrane proteins (OMPs), particularly those with surface-exposed regions, play crucial roles in pathogen virulence mechanisms and adaptation to environmental conditions, including those found in the mammalian host. Therefore, elucidation and characterization of the surface-exposed OMPs of Leptospira spp. is of great interest in the leptospirosis field. A thorough, multi-pronged approach for assessing surface exposure of leptospiral OMPs is essential. Herein, we present evidence for a sub-surface location for most or all of the major leptospiral lipoprotein, LipL32, based on surface immunofluorescence utilizing three different types of antibodies and four different permeabilization methods, as well as surface proteolysis of intact and lysed leptospires. We reevaluate prior evidence presented in support of LipL32 surface-exposure and present a novel perspective on a protein whose location has been misleading researchers, due in large part to its extraordinary abundance in leptospiral cells.

Indexed as

Antibodies, BacterialBacterial Outer Membrane ProteinsHumansLeptospira interrogansLipoproteinsVirulence FactorsAntibodies, BacterialBacterial Outer Membrane ProteinsLipL32 protein, LeptospiraLipoproteinsVirulence Factors

Identifiers

PMID23323152
PMCPMC3544172
OpenAlexW2023580202

What OpenQuestion holds

Textmetadata
LicenceCC0
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.