Evidence map›Paper›PMID 17942555›Full record

ArticleJournal of virology2008

Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that mediates entry into epithelial and endothelial cells.

Brent J Ryckman, Barb L Rainish, Marie C Chase, Jamie A Borton, Jay A Nelson, Michael A Jarvis, David C Johnson

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
195citing papers in PubMed, 1 pooled it
7.8field-weighted citation impact, top 2% 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

195 citing papers in PubMed, 1 synthesis or guideline pooled it, 308 citations in OpenAlex.

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135 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Brent J Ryckman6366 Basic Sciences Building, Mail Code L-220, Department of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 Sam Jackson Park Rd., Portland, OR 97239, USA. ryckmanb@ohsu.edu
Barb L Rainish
Marie C Chase
Jamie A Borton
Jay A Nelson
Michael A Jarvis
David C Johnson
Oregon Health & Science University · US

Funding

MOLECULAR ASPECTS OF CYTOMEGALOVIRUS LATENCYR01AI021640 · NIAID · UNIVERSITY OF GUELPH · PI Meaghan H Hancock · 1985 to 2026
$8.1M
Molecular Aspects of Cytomegalovirus LatencyR37AI021640 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI HANCOCK, MEAGHAN H · 2018 to 2024
$4.0M
INHIBITION OF CLASS I ANTIGEN PRESENTATION BY HSV ICP47R01EY011245 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI JOHNSON, DAVID C. · 1996 to 2008
$3.6M
Herpes Simplex Virus US9 in Ocular DiseaseF32EY015965 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI RYCKMAN, BRENT J. · 2004 to 2006
$134k
NEI NIH HHS EY015965NEI NIH HHS EY11245NEI NIH HHS F32 EY015965NEI NIH HHS R01 EY011245NIAID NIH HHS AI21640NIAID NIH HHS AI73996NIAID NIH HHS R01 AI021640NIAID NIH HHS R37 AI021640
6 · The paper itself

Abstract

The entry of human cytomegalovirus (HCMV) into biologically relevant epithelial and endothelial cells involves endocytosis followed by low-pH-dependent fusion. This entry pathway is facilitated by the HCMV UL128, UL130, and UL131 proteins, which form one or more complexes with the virion envelope glycoprotein gH/gL. gH/gL/UL128-131 complexes appear to be distinct from the gH/gL/gO complex, which likely facilitates entry into fibroblasts. In order to better understand the assembly and protein-protein interactions of gH/gL/UL128-131 complexes, we generated HCMV mutants lacking UL128-131 proteins and nonreplicating adenovirus vectors expressing gH, gL, UL128, UL130, and UL131. Our results demonstrate that UL128, UL130, and UL131 can each independently assemble onto gH/gL scaffolds. However, the binding of individual UL128-131 proteins onto gH/gL can significantly affect the binding of other proteins; for example, UL128 increased the binding of both UL130 and UL131 to gH/gL. Direct interactions between gH/UL130, UL130/UL131, gL/UL128, and UL128/UL130 were also observed. The export of gH/gL complexes from the endoplasmic reticulum (ER) to the Golgi apparatus and cell surface was dramatically increased when all of UL128, UL130, and UL131 were coexpressed with gH/gL (with or without gO expression). Incorporation of gH/gL complexes into the virion envelope requires transport beyond the ER. Thus, we concluded that UL128, UL130, and UL131 must all bind simultaneously onto gH/gL for the production of complexes that can function in entry into epithelial and endothelial cells.

Indexed as

Virus InternalizationCell MembraneCytomegalovirusEndoplasmic ReticulumEndothelial CellsEpithelial CellsGolgi ApparatusHumansProtein BindingProtein TransportViral ProteinsViral Proteins

Identifiers

PMID17942555
PMCPMC2224386
OpenAlexW2133392557

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.