Evidence map›Paper›PMID 20231409›Full record

ArticleInfection and immunity2010

Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion.

Andrew M Moorhead, Joo-Yong Jung, Asya Smirnov, Susanne Kaufer, Marci A Scidmore

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 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 101 citations in OpenAlex.

  1. Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Infection and immunity · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023
    Review
  10. Article
  11. Article
  12. Idiosyncratic Biogenesis of Intracellular Pathogens-Containing Vacuoles.Frontiers in cellular and infection microbiology · 2021
    Review
  13. Article
  14. Hijacking and Use of Host Kinases by Chlamydiae.Pathogens (Basel, Switzerland) · 2020
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Chlamydial Infection From Outside to Inside.Frontiers in microbiology · 2019
    Review
  20. Sphingolipid Metabolism and Transport inFrontiers in cell and developmental biology · 2019
    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

5 authors at 2 institutions in 1 country.

Andrew M MoorheadDepartment of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Joo-Yong Jung
Asya Smirnov
Susanne Kaufer
Marci A Scidmore
Cornell University · USNew York State College of Veterinary Medicine · US

Funding

The Role of Rab GTPases in Chlamydia-Infected CellsR01AI073831 · NIAID · CORNELL UNIVERSITY · PI SCIDMORE, MARCI A · 2008 to 2012
$1.9M
NIAID NIH HHS R01 AI073831PHS HHS R01A1073831
6 · The paper itself

Abstract

Chlamydiae replicate within a nonacidified vacuole, termed an inclusion. As obligate intracellular bacteria, chlamydiae actively modify their vacuole to exploit host signaling and trafficking pathways. Recently, we demonstrated that several Rab GTPases are actively targeted to the inclusion. To define the biological roles of inclusion localized Rab GTPases, we have begun to identify inclusion-localized Rab effectors. Here we demonstrate that oculocerebrorenal syndrome of Lowe protein 1 (OCRL1), a Golgi complex-localized phosphatidylinositol (PI)-5-phosphatase that binds to multiple Rab GTPases, localizes to chlamydial inclusions. By examining the intracellular localization of green fluorescent protein (GFP) fusion proteins that bind to unique phosphoinositide species, we also demonstrate that phosphatidylinositol-4-phosphate (PI4P), the product of OCRL1, is present at the inclusion membrane. Furthermore, two additional host proteins, Arf1, which together with PI4P mediates the recruitment of PI4P-binding proteins to the Golgi complex, and PI4KII alpha, a major producer of Golgi complex-localized PI4P, also localize to chlamydial inclusions. Depletion of OCRL1, Arf1, or PI4KII alpha by small interfering RNA (siRNA) decreases inclusion formation and the production of infectious progeny. Infectivity is further decreased in cells simultaneously depleted for all three host proteins, suggesting partially overlapping functions in infected cells. Collectively, these data demonstrate that Chlamydia species create a unique replication-competent vacuolar environment by modulating both the Rab GTPase and the PI composition of the chlamydial inclusion.

Indexed as

ADP-Ribosylation Factor 1BacteriaCell MembraneChlamydiaHeLa CellsHumansMinor Histocompatibility AntigensPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesPhosphotransferases (Alcohol Group Acceptor)rab GTP-Binding ProteinsVacuolesADP-Ribosylation Factor 1Minor Histocompatibility AntigensOCRL protein, humanphosphatidylinositol 4-phosphatephosphatidylinositol phosphate 4-kinasePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesPhosphotransferases (Alcohol Group Acceptor)rab GTP-Binding Proteins

Identifiers

PMID20231409
PMCPMC2863499
OpenAlexW2062348048

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.