Evidence map›Paper›PMID 15254205›Full record

ArticleJournal of virology2004

Coiled-coil domains in glycoproteins B and H are involved in human cytomegalovirus membrane fusion.

Matthew Lopper, Teresa Compton

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Entry of Alphaherpesviruses.Current issues in molecular biology · 2021
    Review
  7. Article
  8. Battle between Host Immune Cellular Responses and HCMV Immune Evasion.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Development of novel vaccines against human cytomegalovirus.Human vaccines & immunotherapeutics · 2019
    Review
  11. Article
  12. Article
  13. Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Journal of peptide science : an official publication of the European Peptide Society · 2017
    Article
  14. Article
  15. Zika Fetal Neuropathogenesis: Etiology of a Viral Syndrome.PLoS neglected tropical diseases · 2016
    Review
  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.

Matthew LopperDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Teresa Compton
University of Wisconsin–Madison · US

Funding

Role of Glycoprotein B in HCMV infectionR01AI034998 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KALEJTA, ROBERT F · 1995 to 2010
$2.8M
HUMAN CYTOMEGALOVIRUS ENVELOPE GLYCOPROTEINSR01AI044203 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI COMPTON, TERESA G · 1999 to 2002
$682k
NIAID NIH HHS R01 AI034998NIAID NIH HHS R01 AI-34998NIAID NIH HHS R01 AI-44203
6 · The paper itself

Abstract

Human cytomegalovirus (CMV) utilizes a complex route of entry into cells that involves multiple interactions between viral envelope proteins and cellular receptors. Three conserved viral glycoproteins, gB, gH, and gL, are required for CMV-mediated membrane fusion, but little is known of how these proteins cooperate during entry (E. R. Kinzler and T. Compton, submitted for publication). The goal of this study was to begin defining the molecular mechanisms that underlie membrane fusion mediated by herpesviruses. We identified heptad repeat sequences predicted to form alpha-helical coiled coils in two glycoproteins required for fusion, gB and gH. Peptides derived from gB and gH containing the heptad repeat sequences inhibited virus entry when introduced coincident with virus inoculation onto cells or when mixed with virus prior to inoculation. Neither peptide affected binding of CMV to fibroblasts, suggesting that the peptides inhibit membrane fusion. Both gB and gH coiled-coil peptides blocked entry of several laboratory-adapted and clinical strains of human CMV, but neither peptide affected entry of murine CMV or herpes simplex virus type 1 (HSV-1). Although murine CMV and HSV-1 gB and gH have heptad repeat regions, the ability of human CMV gB and gH peptides to inhibit virus entry correlates with the specific residues that comprise the heptad repeat region. The ability of gB and gH coiled-coil peptides to inhibit virus entry independently of cell contact suggests that the coiled-coil regions of gB and gH function differently from those of class I, single-component fusion proteins. Taken together, these data support a critical role for alpha-helical coiled coils in gB and gH in the entry pathway of CMV.

Indexed as

Membrane FusionAmino Acid SequenceAnimalsCytomegalovirusFibroblastsHumansMiceMolecular Sequence DataNIH 3T3 CellsProtein Structure, SecondaryRepetitive Sequences, Amino AcidViral Envelope ProteinsVirionglycoprotein B, Simplexvirusglycoprotein H, Cytomegalovirusglycoprotein H, Human cytomegalovirusViral Envelope Proteins

Identifiers

PMID15254205
PMCPMC446119
OpenAlexW2133073089

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.