Evidence map›Paper›PMID 9525659›Full record

ArticleJournal of virology1998

Localization of human cytomegalovirus structural proteins to the nuclear matrix of infected human fibroblasts.

V Sanchez, P C Angeletti, J A Engler, W J Britt

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.1field-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

30 citing papers in PubMed, 69 citations in OpenAlex.

  1. Cytomegalovirus disrupts Lamin A/C to control microtubule-mediated nuclear movement and cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

4 authors at 2 institutions in 2 countries.

V SanchezDepartment of Microbiology, University of Alabama at Birmingham, 35233, USA.
P C Angeletti
J A Engler
W J Britt
University of Alabama at Birmingham · USCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

ENVELOPE ASSEMBLY OF HUMAN CYTOMEGALOVIRUSR01AI035602 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 1995 to 2018
$4.5M
BASIC MECHANISMS IN VIROLOGYT32AI007150 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI PREVELIGE, PETER E. · 1985 to 2007
$1.7M
INITIATION OF ADENOVIRUS-2 DNA REPLICATIONR01AI020408 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ENGLER, JEFFREY ALLEN · 1985 to 1997
–
ANTIBODY RECOGNITION OF CYTOMEGALOVIRUS GLYCOPROTEINSR01AI030105 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM J · 1991 to 1995
–
NIAID NIH HHS R01 AI035602NIAID NIH HHS R01 AI20408NIAID NIH HHS R01 AI30105NIAID NIH HHS T32 AI007150NIAID NIH HHS T32 AI07150
6 · The paper itself

Abstract

The intranuclear assembly of herpesvirus subviral particles remains an incompletely understood process. Previous studies have described the nuclear localization of capsid and tegument proteins as well as intranuclear tegumentation of capsid-like particles. The temporally and spatially regulated replication of viral DNA suggests that assembly may also be regulated by compartmentalization of structural proteins. We have investigated the intranuclear location of several structural and nonstructural proteins of human cytomegalovirus (HCMV). Tegument components including pp65 (ppUL83) and ppUL69 and capsid components including the major capsid protein (pUL86) and the small capsid protein (pUL48/49) were retained within the nuclear matrix (NM), whereas the immediate-early regulatory proteins IE-1 and IE-2 were present in the soluble nuclear fraction. The association of pp65 with the NM resisted washes with 1 M guanidine hydrochloride, and direct binding to the NM could be demonstrated by far-Western blotting. Furthermore, pp65 exhibited accumulation along the nuclear periphery and in far-Western analysis bound to proteins which comigrated with proteins of the size of nuclear lamins. A direct interaction between pp65 and lamins was demonstrated by coprecipitation of lamins in immune complexes containing pp65. Together, our findings provide evidence that major virion structural proteins localized to a nuclear compartment, the NM, during permissive infection of human fibroblasts.

Indexed as

AnimalsCapsidCell LineChlorocebus aethiopsCOS CellsCytomegalovirusFibroblastsHumansLaminsNuclear MatrixNuclear ProteinsPhosphoproteinsViral Matrix ProteinsViral Structural Proteinscytomegalovirus matrix protein 65kDaLaminsNuclear ProteinsPhosphoproteinsViral Matrix ProteinsViral Structural Proteins

Identifiers

PMID9525659
PMCPMC109810
OpenAlexW2143857423

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.