Evidence map›Paper›PMID 16963142›Full record

ArticleVirus research2007

The chemokine receptor homologue encoded by US27 of human cytomegalovirus is heavily glycosylated and is present in infected human foreskin fibroblasts and enveloped virus particles.

Barry J Margulies, Wade Gibson

Open access · greenAbstract read
In one paragraph

Article in Virus research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Methods for Studying the Function of Cytomegalovirus GPCRs.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Evolution of the ability to modulate host chemokine networks via gene duplication in human cytomegalovirus (HCMV).Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2017
    Article
  13. Mechanisms of Regulation of the Chemokine-Receptor Network.International journal of molecular sciences · 2017
    Review
  14. Article
  15. Hijacking GPCRs by viral pathogens and tumor.Biochemical pharmacology · 2016
    Review
  16. Article
  17. Review
  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 2 institutions in 1 country.

Barry J MarguliesTowson University Herpes Virus Lab, Department of Biological Sciences, Towson University, Towson, MD 21252, USA. bjmarg@alum.mit.edu
Wade Gibson
Johns Hopkins University · USTowson University · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
HERPESVIRUS PROTEIN SYNTHESIS &VIRION ASSEMBLYR01AI013718 · NIAID · JOHNS HOPKINS UNIVERSITY · PI GIBSON, D. WADE · 1985 to 2005
$2.1M
Herpesvirus Protein Synthesis And Virion AssemblyR56AI013718 · NIAID · JOHNS HOPKINS UNIVERSITY · PI GIBSON, D WADE · 2008 to 2008
$410k
NIAID NIH HHS AI13718NIAID NIH HHS AI227711NIAID NIH HHS R01 AI013718NIAID NIH HHS R56 AI013718NIGMS NIH HHS T32 GM007445NIGMS NIH HHS T32 GM07445
6 · The paper itself

Abstract

Human cytomegalovirus (HCMV), a member of the beta-herpesvirus family, encodes four homologues of cellular G protein-coupled receptors (GPCRs). One of these, the protein product of HCMV open reading frame (ORF) UL33, has been identified in HCMV-infected cells and virus particles and shown to be heat-aggregatable and N-glycosylated. Another, the product of ORF US28, has been functionally characterized as a beta-chemokine receptor. Here we report the use of RT-PCR, coupled in vitro transcription-translation, immunoprecipitation, and Western immunoassays to (i) show that RNA from the open reading frame US27 appears predominantly during the late phase of replication; (ii) identify the protein encoded by HCMV US27 in infected cells and enveloped virus particles; (iii) demonstrate that the US27-encoded protein is heterogeneously N-glycosylated and resolves as two species following treatment with peptide N-glycosidase F; and (iv) show that both the recombinant and deglycoylated infected cell US27 protein aggregate when heated in the presence of SDS prior to electrophoresis in polyacrylamide gels, a property which is abrogated with the addition of urea to sample buffer.

Indexed as

Cells, CulturedCytomegalovirusCytomegalovirus InfectionsFibroblastsGlycosylationHumansReceptors, ChemokineViral ProteinsVirulenceVirus ReplicationReceptors, ChemokineUS27 protein, human cytomegalovirusViral Proteins

Identifiers

PMID16963142
PMCPMC2676329
OpenAlexW2022630679

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.