Evidence map›Paper›PMID 17517859›Full record

ArticleInfection and immunity2007

Surface-exposed proteins of Ehrlichia chaffeensis.

Yan Ge, Yasuko Rikihisa

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
6.0field-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

45 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Proceedings of the National Academy of Sciences of the United States of America · 2024
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  3. Host Cells Upregulate Phosphate Transporter PIT1 to InhibitInternational journal of molecular sciences · 2024
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  4. Proteome analysis ofFrontiers in cellular and infection microbiology · 2022
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  5. Review
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  10. Review
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  12. Review
  13. Article
  14. Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015
    Review
  15. 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.

Yan GeDepartment of Veterinary Biosciences, College of Veterinary Medicine, The Ohio State University, 1925 Coffey Road, Columbus, OH 43210, USA.
Yasuko Rikihisa
The Ohio State University · US

Funding

EHRLICHIACIDAL MECHANISM IN MACROPHAGESR01AI030010 · NIAID · OHIO STATE UNIVERSITY · PI RIKIHISA, YASUKO · 1990 to 2009
$2.4M
NIAID NIH HHS R01 AI030010NIAID NIH HHS R01 AI 30010
6 · The paper itself

Abstract

The surface proteins of Ehrlichia chaffeensis provide an important interface for pathogen-host interactions. To investigate the surface proteins of E. chaffeensis, membrane-impermeable, cleavable Sulfo-NHS-SS-Biotin was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin-agarose affinity purification. The affinity-captured proteins were separated by electrophoresis, and five relatively abundant protein bands containing immunoreactive proteins were subjected to capillary-liquid chromatography-nanospray tandem mass spectrometry analysis. Nineteen out of 22 OMP-1/P28 family proteins, including P28 (which previously was shown to be surface exposed), were detected in E. chaffeensis cultured in human monocytic leukemia THP-1 cells. For the first time, with the exception of P28 and P28-1, 17 OMP-1/P28 family proteins were demonstrated to be expressed at the protein level. The surface exposure of OMP-1A and OMP-1N was verified by immunofluorescence microscopy. OMP-1B was undetectable either by surface biotinylation or by Western blotting of the whole bacterial lysate, suggesting that it is not expressed by E. chaffeensis cultured in THP-1 cells. Additional E. chaffeensis surface proteins detected were OMP85, hypothetical protein ECH_0525 (here named Esp73), immunodominant surface protein gp47, and 11 other proteins. The identification of E. chaffeensis surface-exposed proteins provides novel insights into the E. chaffeensis surface and lays the foundation for rational studies on pathogen-host interactions and vaccine development.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBiotinBiotinylationCell Line, TumorChromatography, AffinityEhrlichia chaffeensisElectrophoresis, Polyacrylamide GelHumansMembrane ProteinsMicroscopy, FluorescenceModels, MolecularMonocytesStaining and LabelingSuccinimidesTandem Mass SpectrometryBacterial Outer Membrane ProteinsBacterial ProteinsBiotinMembrane ProteinsSuccinimidessulfo-N-hydroxysuccinimide-biotin

Identifiers

PMID17517859
PMCPMC1951975
OpenAlexW2129358913

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.