Evidence map›Paper›PMID 18285495›Full record

ArticleInfection and immunity2008

Anaplasma phagocytophilum MSP2(P44)-18 predominates and is modified into multiple isoforms in human myeloid cells.

Madhubanti Sarkar, Matthew J Troese, Sarah A Kearns, Tian Yang, Dexter V Reneer, Jason A Carlyon

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Global Transcription Profiles ofFrontiers in veterinary science · 2020
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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

6 authors at 2 institutions in 1 country.

Madhubanti SarkarDepartment of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, Kentucky 40504, USA.
Matthew J Troese
Sarah A Kearns
Tian Yang
Dexter V Reneer
Jason A Carlyon
University of Kentucky · USVirginia Commonwealth University · US

Funding

The roles of Anaplasma phagocytophilum surface proteins in infectionR01AI072683 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CARLYON, JASON A · 2007 to 2021
$5.8M
The roles of Anaplasma phagocytophilum surface proteins in infectionR37AI072683 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI Jason A Carlyon · 2022 to 2026
$2.6M
Inhibition of NADPH oxidase by Anaplasma phagocytophilaK01DK065039 · NIDDK · YALE UNIVERSITY · PI CARLYON, JASON A · 2003 to 2007
$619k
The roles of Anaplasma phagocytophilum surface proteins in cellular invasionR56AI072683 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CARLYON, JASON A · 2012 to 2012
$368k
NIAID NIH HHS AI072683NIAID NIH HHS R01 AI072683NIAID NIH HHS R37 AI072683NIAID NIH HHS R56 AI072683NIDDK NIH HHS DK065039NIDDK NIH HHS K01 DK065039
6 · The paper itself

Abstract

Anaplasma phagocytophilum is the etiologic agent of human granulocytic anaplasmosis. MSP2(P44), the bacterium's major surface protein, is encoded by a paralogous gene family and has been implicated in a variety of pathobiological processes, including antigenic variation, host adaptation, adhesion, porin activity, and structural integrity. The consensus among several studies performed at the DNA and RNA levels is that a heterogeneous mix of a limited number of msp2(p44) transcripts is expressed by A. phagocytophilum during in vitro cultivation. Such analyses have yet to be extended to the protein level. In this study, we used proteomic and molecular approaches to determine that MSP2(P44)-18 is the predominant if not the only paralog expressed and is modified into multiple 42- to 44-kDa isoforms by A. phagocytophilum strain HGE1 during infection of HL-60 cells. The msp2(p44) expression profile was homogeneous for msp2(p44)-18. Thus, MSP2(P44)-18 may have a fitness advantage in HL-60 cell culture in the absence of selective immune pressure. Several novel 22- to 27-kDa MSP2 isoforms lacking most of the N-terminal conserved region were also identified. A. phagocytophilum MSP2(P44) orthologs expressed by other pathogens in the family Anaplasmataceae are glycosylated. Gas chromatography revealed that recombinant MSP2(P44)-18 is modified by glucose, galactose, xylose, mannose, and trace amounts of other glycosyl residues. These data are the first to confirm differential modification of any A. phagocytophilum MSP2(P44) paralog and the first to provide evidence for expression of truncated versions of such proteins.

Indexed as

Amino Acid SequenceAnaplasma phagocytophilumBacterial Outer Membrane ProteinsBlotting, WesternCarbohydratesCell LineChromatography, GasElectrophoresis, Gel, Two-DimensionalGlycosylationHumansMolecular Sequence DataMyeloid CellsProtein IsoformsBacterial Outer Membrane ProteinsCarbohydratesmsp2 protein, Anaplasma phagocytophilumProtein Isoforms

Identifiers

PMID18285495
PMCPMC2346672
OpenAlexW2097046682

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.