Evidence map›Paper›PMID 22139844›Full record

ArticleThe Journal of biological chemistry2012

Critical role for heat shock protein 20 (HSP20) in migration of malarial sporozoites.

Georgina N Montagna, Carlos A Buscaglia, Sylvia Münter, Christian Goosmann, Friedrich Frischknecht, Volker Brinkmann, Kai Matuschewski

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. An OptimizedBio-protocol · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.Advances in experimental medicine and biology · 2021
    Article
  11. Article
  12. Frontiers in microbiology · 2020
    Article
  13. Review
  14. Review
  15. Article
  16. Journal of fungi (Basel, Switzerland) · 2019
    Article
  17. Article
  18. Review
  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

7 authors at 4 institutions in 2 countries.

Georgina N MontagnaMax Planck Institute for Infection Biology, 10117 Berlin, Germany.
Carlos A Buscaglia
Sylvia Münter
Christian Goosmann
Friedrich Frischknecht
Volker Brinkmann
Kai Matuschewski
Heidelberg University · DEMax Planck Institute for Infection Biology · DEMax Planck Society · DEInstituto Tecnológico de Chascomús · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasmodium sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.

Indexed as

ActinsAnimalsHSP20 Heat-Shock ProteinsLocomotionMalariaMicePlasmodium bergheiProtozoan ProteinsSporozoitesActinsHSP20 Heat-Shock ProteinsProtozoan Proteins

Identifiers

PMID22139844
PMCPMC3268402
OpenAlexW2068753337

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.