Evidence map›Paper›PMID 19124604›Full record

ArticleInfection and immunity2009

The Schistosoma mansoni protein Sm16/SmSLP/SmSPO-1 assembles into a nine-subunit oligomer with potential To inhibit Toll-like receptor signaling.

Kristoffer Brännström, Mikael E Sellin, Per Holmfeldt, Maria Brattsand, Martin Gullberg

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Pooled it
  2. TRPV1+ neurons promote cutaneous immunity against Schistosoma mansoni.Journal of immunology (Baltimore, Md. : 1950) · 2025
    Article
  3. Review
  4. Nitric oxide in parasitic infections: a friend or foe?Journal of parasitic diseases : official organ of the Indian Society for Parasitology · 2022
    Review
  5. Schistosome immunomodulators.PLoS pathogens · 2021
    Review
  6. Parasite-bacteria interrelationship.Parasitology research · 2020
    Review
  7. Article
  8. Immune Evasion Strategies of Schistosomes.Frontiers in immunology · 2020
    Review
  9. Review
  10. Sm16, AJournal of immunology research · 2019
    Article
  11. Article
  12. Article
  13. TLR Specific Immune Responses against Helminth Infections.Journal of parasitology research · 2017
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

Kristoffer BrännströmDepartment of Molecular Biology, Umeå University, Umeå, Sweden.
Mikael E Sellin
Per Holmfeldt
Maria Brattsand
Martin Gullberg
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Sm16/SmSLP/SmSPO-1 (Sm16) protein is secreted by the parasite Schistosoma mansoni during skin penetration and has been ascribed immunosuppressive activities. Here we describe the strategy behind the design of a modified Sm16 protein with a decreased aggregation propensity, thus facilitating the expression and purification of an Sm16 protein that is soluble in physiological buffers. The Stokes radii and sedimentation coefficients of recombinant and native proteins indicate that Sm16 is an approximately nine-subunit oligomer. Analysis of truncated Sm16 derivatives showed that both oligomerization and binding to the plasma membrane of human cells depend on multiple C-terminal regions. For analysis of immunomodulatory activities, Sm16 was expressed in Pichia pastoris to facilitate the preparation of a pyrogen/endotoxin-free purified protein. Recombinant Sm16 was found to have no effect on T-lymphocyte activation, cell proliferation, or the basal level of cytokine production by whole human blood or monocytic cells. However, Sm16 exerts potent inhibition of the cytokine response to the Toll-like receptor (TLR) ligands lipopolysaccharide (LPS) and poly(I:C) while being less efficient at inhibiting the response to the TLR ligand peptidoglycan or a synthetic lipopeptide. Since Sm16 specifically inhibits the degradation of the IRAK1 signaling protein in LPS-stimulated monocytes, our findings indicate that inhibition is exerted proximal to the TLR complex.

Indexed as

AnimalsCytokinesFlow CytometryHelminth ProteinsHumansImmunoblottingLymphocyte ActivationRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSchistosoma mansoniSignal TransductionT-LymphocytesToll-Like ReceptorsCytokinesHelminth ProteinsRecombinant ProteinsSM16 protein, Schistosoma mansoniToll-Like Receptors

Identifiers

PMID19124604
PMCPMC2643650
OpenAlexW2121215912

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.