Evidence map›Paper›PMID 20089288›Full record

ArticleVirology2010

Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry.

Katie M Stiles, Claude Krummenacher

Abstract read
In one paragraph

Article in Virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

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  19. Human cytomegalovirus entry into cells.Current opinion in virology · 2012
    Review
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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.

Katie M StilesDepartment of Microbiology, School of Dental Medicine University of Pennsylvania, 240 S. 40th St., Philadelphia, PA 19104, USA. Electronic address: stileskm@mail.med.upenn.edu.
Claude KrummenacherDepartment of Biochemistry, School of Dental Medicine University of Pennsylvania, Philadelphia, PA 19104, USA.
University of Pennsylvania · US

Funding

TRAINING IN VIROLOGYT32AI007324 · NIAID · WISTAR INSTITUTE · PI Paul Bates, Matthew D. Weitzman · 1989 to 2026
$6.8M
Studies of Herpes Simplex Virus GlycoproteinsR37AI018289 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI COHEN, GARY H · 2005 to 2014
$3.9M
STUDIES OF HERPES SIMPLEX VIRUS GLYCOPROTEINSR01AI018289 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI COHEN, GARY H · 1985 to 2019
$3.8M
Uncovering the Regulatory Role of gH/gL in HSV FusionR01AI056045 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI EISENBERG, ROSELYN J · 2004 to 2015
$3.7M
Early Events in Herpes Simplex Virus EntryR01AI076231 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI EISENBERG, ROSELYN J · 2008 to 2012
$1.9M
Interactions of herpes simplex virus with nectin-1 at cell junctions R21AI073384 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI KRUMMENACHER, CLAUDE F · 2007 to 2008
$429k
Study of the structure, function and regulation of gB, the fusion protein of HSVR56AI076231 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI EISENBERG, ROSELYN J · 2013 to 2013
$362k
HSV-Receptor Interaction in Entry and PathogenesisR21AI056045 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI EISENBERG, ROSELYN J. · 2003 to 2003
$310k
NIAID NIH HHS AI-056045NIAID NIH HHS AI-073384NIAID NIH HHS AI-076231NIAID NIH HHS AI-18289NIAID NIH HHS R01 AI018289NIAID NIH HHS R01 AI056045NIAID NIH HHS R01 AI076231NIAID NIH HHS R21 AI056045NIAID NIH HHS R21 AI073384NIAID NIH HHS R37 AI018289NIAID NIH HHS R56 AI076231NIAID NIH HHS T32 AI007324NIAID NIH HHS T32-AI07324
6 · The paper itself

Abstract

Entry of herpes simplex virus (HSV) occurs either by fusion at the plasma membrane or by endocytosis and fusion with an endosome. Binding of glycoprotein D (gD) to a receptor such as nectin-1 is essential in both cases. We show that virion gD triggered the rapid down-regulation of nectin-1 with kinetics similar to those of virus entry. In contrast, nectin-1 was not constitutively recycled from the surface of uninfected cells. Both the nectin-1alpha and beta isoforms were internalized in response to gD despite having different cytoplasmic tails. However, deletion of the nectin-1 cytoplasmic tail slowed down-regulation of nectin-1 and internalization of virions. These data suggest that nectin-1 interaction with a cytoplasmic protein is not required for its down-regulation. Overall, this study shows that gD binding actively induces the rapid internalization of various forms of nectin-1. We suggest that HSV activates a nectin-1 internalization pathway to use for endocytic entry.

Indexed as

Virus InternalizationAnimalsCell Adhesion MoleculesCell LineDown-RegulationEndocytosisFlow CytometryFluorescent Antibody TechniqueGene Expression Regulation, ViralHerpes SimplexHerpesvirus 1, HumanHumansMiceNectinsProtein IsoformsViral Envelope ProteinsCell Adhesion Moleculesglycoprotein D, Human herpesvirus 1NECTIN1 protein, humanNectin1 protein, mouseNectinsProtein IsoformsViral Envelope Proteins

Identifiers

PMID20089288
PMCPMC2830393
OpenAlexW2068084794

What OpenQuestion holds

Textmetadata
LicenceTDM
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.