Evidence map›Paper›PMID 17392372›Full record

ArticleJournal of virology2007

Cytoplasmic envelopment of human cytomegalovirus requires the postlocalization function of tegument protein pp28 within the assembly compartment.

Jun-Young Seo, William J Britt

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

35 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Review
  7. Article
  8. Quantitative Electron Microscopy to Study HCMV Morphogenesis.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
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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

2 authors at 1 institution in 1 country.

Jun-Young SeoDepartment of Microbiology, University of Alabama School of Medicine, and Department of Pediatrics, Children's Hospital, 1600 7th Ave. South, Birmingham, AL 35233, USA.
William J Britt
University of Alabama at Birmingham · US

Funding

ENVELOPE ASSEMBLY OF HUMAN CYTOMEGALOVIRUSR01AI035602 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 1995 to 2018
$4.5M
gM/gN and Envelopment of HCMVR01AI050189 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 2002 to 2012
$3.1M
NIAID NIH HHS R01 AI035602NIAID NIH HHS R01 AI050189NIAID NIH HHS R01 AI35602NIAID NIH HHS R01 AI50189
6 · The paper itself

Abstract

The assembly of herpesvirus remains incompletely defined due to the structural complexity of these viruses. Although the assembly of the capsid of these large DNA viruses is well studied and reasonably well conserved for all members of this diverse family of viruses, the cytoplasmic processes of tegumentation and envelopment are not well understood. The virion of the largest human herpesvirus, human cytomegalovirus (HCMV), contains over 70 virus-encoded proteins that are incorporated during a nuclear and cytoplasmic phase of assembly. Envelopment of this virus requires the function of at least one tegument protein, pp28, the product of the UL99 open reading frame. However, the role of pp28 in the envelopment of HCMV remains undefined. We have generated a pp28 mutant virus that encodes only the first 50 amino acids (aa) of this 190-aa virion protein. This virus is replication impaired and is defective in virus assembly. Characterization of both intracellular and extracellular virions from cells infected with this viral mutant indicated that the decrease in production of infectious virus was secondary to a defect in envelopment and the accumulation of tegumented, noninfectious intracellular particles. Image analysis using fluorescence recovery after photobleaching indicated that the pp28 mutant protein encoded by this virus failed to efficiently accumulate in the virus assembly compartment (AC). Our results suggest that pp28 must accumulate in the AC for efficient envelopment of the particle and provide evidence for a direct role of this tegument protein in the late stages of assembly, such as envelopment.

Indexed as

Gene Expression Regulation, ViralAmino Acid SequenceCell NucleusCodonCytomegalovirusCytoplasmFibroblastsGreen Fluorescent ProteinsHumansKineticsMicroscopy, ElectronModels, GeneticMolecular Sequence DataPhosphoproteinsTime FactorsViral ProteinsCodonGreen Fluorescent Proteinshuman cytomegalovirus protein pp28PhosphoproteinsViral Proteins

Identifiers

PMID17392372
PMCPMC1900121
OpenAlexW2140585491

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.