Evidence map›Paper›PMID 10231011›Full record

ReviewInfectious diseases in obstetrics and gynecology1999

Surface-associated heat shock proteins of Legionella pneumophila and Helicobacter pylori: roles in pathogenesis and immunity.

P S Hoffman, R A Garduno

Open access · hybridAbstract readReview
In one paragraph

Review in Infectious diseases in obstetrics and gynecology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

22 citing papers in PubMed, 49 citations in OpenAlex.

  1. The Role ofInternational journal of molecular sciences · 2025
    Review
  2. Article
  3. Review
  4. Pathogens (Basel, Switzerland) · 2021
    Article
  5. Review
  6. Article
  7. Frontiers in microbiology · 2017
    Review
  8. Intestinal M cells.Journal of biochemistry · 2016
    Review
  9. Article
  10. Article
  11. Article
  12. Heat shock protein 70 (hsp70) as an emerging drug target.Journal of medicinal chemistry · 2010
    Review
  13. Article
  14. Review
  15. Genotypic diversity of Haemophilus parasuis field strains.Applied and environmental microbiology · 2006
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

2 authors at 1 institution in 1 country.

P S HoffmanDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada. phoffman@tupdean2.med.dal.ca
R A Garduno
Dalhousie University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial heat shock proteins (Hsps) are abundantly produced during the course of most microbial infections and are often targeted by the mammalian immune response. While Hsps have been well characterized for their roles in protein folding and secretion activities, little attention has been given to their participation in pathogenesis. In the case of Legionella pneumophila, an aquatic intracellular parasite of protozoa and cause of Legionnaires' disease, Hsp60 is uniquely located in the periplasm and on the bacterial surface. Surface-associated Hsp60 promotes attachment and invasion in a HeLa cell model and may alter an early step associated with the fusion of phagosomes with lysosomes. Avirulent strains of L. pneumophila containing defined mutations in several dot/icm genes are defective in localizing Hsp60 onto their surface and are reduced approximately 1000-fold in their invasiveness towards HeLa cells. For the ulcer-causing bacterium Helicobacter pylori, surface-associated Hsp60 and Hsp70 mediate attachment to gastric epithelial cells. The increased expression of these Hsps following acid shock correlates with both increased association with and inflammation of the gastric mucosa. A role for Hsps in colonization, mucosal infection and in promoting inflammation is discussed.

Indexed as

Bacterial AdhesionHeat-Shock ProteinsHelicobacter InfectionsHelicobacter pyloriHumansLegionella pneumophilaLegionnaires' DiseaseVirulenceHeat-Shock Proteins

Identifiers

PMID10231011
PMCPMC1784713
OpenAlexW2119321586

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.