Evidence map›Paper›PMID 20194599›Full record

ArticleInfection and immunity2010

Interaction of pneumococcal histidine triad proteins with human complement.

Merit Melin, Emmanuel Di Paolo, Leena Tikkanen, Hanna Jarva, Cecile Neyt, Helena Käyhty, Seppo Meri, Jan Poolman, Merja Väkeväinen

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-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

32 citing papers in PubMed, 54 citations in OpenAlex.

  1. Trial
  2. Human vaccines & immunotherapeutics · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Frontiers in cellular and infection microbiology · 2022
    Review
  8. Review
  9. Article
  10. Proteomic Adaptation ofMicroorganisms · 2020
    Article
  11. Proteomic Adaptation ofMicroorganisms · 2020
    Article
  12. Article
  13. Article
  14. Defining the Role of theJournal of bacteriology · 2019
    Article
  15. Complement factor H in host defense and immune evasion.Cellular and molecular life sciences : CMLS · 2017
    Review
  16. Role ofFrontiers in microbiology · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Multiplex genome editing by natural transformation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

9 authors at 3 institutions in 2 countries.

Merit MelinNational Institute for Health and Welfare, Department of Vaccination and Immune Protection, Mannerheimintie 166, 00300 Helsinki, Finland. merit.melin@thl.fi
Emmanuel Di Paolo
Leena Tikkanen
Hanna Jarva
Cecile Neyt
Helena Käyhty
Seppo Meri
Jan Poolman
Merja Väkeväinen
Finnish Institute for Health and Welfare · FIGlaxoSmithKline (Belgium) · BEHelsinki University Hospital · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pneumococcal histidine triad (Pht) proteins PhtA, PhtB, PhtD, and PhtE form a group of conserved pneumococcal surface proteins. Humans produce antibodies to Pht proteins upon exposure to pneumococcus, and immunization of mice has provided protective immunity against sepsis and pneumonia and reduced nasopharyngeal colonization. Pht proteins are candidates for inclusion in multicomponent pneumococcal protein vaccines. Their biological function in pneumococcal infections is not clear, but a role in complement inhibition has been suggested. We measured complement deposition on wild-type and Pht mutant strains in four genetic backgrounds: Streptococcus pneumoniae D39 (serotype 2) and R36A (unencapsulated derivative of D39) and strains of serotypes 3, 4, and 19F. PspA and PspC single and double mutants were compared to the wild-type and Pht-deficient D39 strains. Factor H binding was measured to bacterial cells, lysates, and protein antigens. Deletion of all four Pht proteins (Pht(-)) resulted in increased C3 deposition on the serotype 4 strain but not on the other strains. Pht antigens did not bind factor H, and deletion of Pht proteins did not affect factor H binding by bacterial lysates. The Pht(-) mutant serotype 4 strain bound slightly less factor H than the wild-type strain when binding was measured by flow cytometry. Pht proteins may play a role in immune evasion, but the mechanism of function is unlikely to be mediated by factor H binding. The relative contribution of Pht proteins to the inhibition of complement deposition is likely to be affected by the presence of other pneumococcal proteins and to depend on the genetic background.

Indexed as

Bacterial ProteinsComplement C3Complement Factor HHumansHydrolasesProtein BindingStreptococcus pneumoniaeBacterial ProteinsComplement C3Complement Factor Hhistidine triad proteinHydrolases

Identifiers

PMID20194599
PMCPMC2863542
OpenAlexW2121035448

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.