Evidence map›Paper›PMID 17766422›Full record

ArticleJournal of bacteriology2007

Identification of novel surface proteins of Anaplasma phagocytophilum by affinity purification and proteomics.

Yan Ge, Yasuko Rikihisa

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. 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
3.0field-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, 59 citations in OpenAlex.

  1. Adaptation ofmSphere · 2026
    Article
  2. mBio · 2026
    Article
  3. Article
  4. Article
  5. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Frontiers in cellular and infection microbiology · 2017
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015
    Review
  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 Rd., 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
GENE EXPRESSION BY HUMAN GRANULOCYTIC EHRLICHIOSIS AGR01AI047407 · NIAID · OHIO STATE UNIVERSITY · PI RIKIHISA, YASUKO · 2000 to 2004
$1.6M
NIAID NIH HHS R01 AI030010NIAID NIH HHS R01 AI047407NIAID NIH HHS R01 AI30010NIAID NIH HHS R01 AI47407
6 · The paper itself

Abstract

Anaplasma phagocytophilum is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of A. phagocytophilum plays a crucial role in subverting the hostile host cell environment. However, except for the P44/Msp2 outer membrane protein family, the surface components of A. phagocytophilum are largely unknown. To identify the major surface proteins of A. phagocytophilum, a membrane-impermeable, cleavable biotin reagent, sulfosuccinimidyl-2-[biotinamido]ethyl-1,3-dithiopropionate (Sulfo-NHS-SS-Biotin), was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin agarose affinity purification and then separated by electrophoresis, followed by capillary liquid chromatography-nanospray tandem mass spectrometry analysis. Among the major proteins captured by affinity purification were five A. phagocytophilum proteins, Omp85, hypothetical proteins APH_0404 (designated Asp62) and APH_0405 (designated Asp55), P44 family proteins, and Omp-1A. The surface exposure of Asp62 and Asp55 was verified by immunofluorescence microscopy. Recombinant Asp62 and Asp55 proteins were recognized by an HGA patient serum. Anti-Asp62 and anti-Asp55 peptide sera partially neutralized A. phagocytophilum infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family Anaplasmataceae. With the exception of P44-18, all of the proteins were newly revealed major surface-exposed proteins whose study should facilitate understanding the interaction between A. phagocytophilum and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines.

Indexed as

Reverse Transcriptase Polymerase Chain ReactionAnaplasma phagocytophilumBacterial ProteinsBase SequenceChromatography, AffinityDNA PrimersLipid BilayersMembrane LipidsMembrane ProteinsProteomicsBacterial ProteinsDNA PrimersLipid BilayersMembrane LipidsMembrane Proteins

Identifiers

PMID17766422
PMCPMC2168727
OpenAlexW2045801003

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.