Evidence map›Paper›PMID 23946456›Full record

ArticleJournal of virology2013

Structural and functional studies on the interaction of adenovirus fiber knobs and desmoglein 2.

Hongjie Wang, Roma Yumul, Hua Cao, Liang Ran, Xiaolong Fan, Maximilian Richter, Forrest Epstein, Julie Gralow, Chloe Zubieta, Pascal Fender and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. 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
2.6field-weighted citation impact, top 10% 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, 42 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
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  6. Molecular therapy. Methods & clinical development · 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

11 authors at 6 institutions in 3 countries.

Hongjie WangUniversity of Washington, Division of Medical Genetics, Seattle, Washington, USA.
Roma Yumul
Hua Cao
Liang Ran
Xiaolong Fan
Maximilian Richter
Forrest Epstein
Julie Gralow
Chloe Zubieta
Pascal Fender
André Lieber
University of Washington Medical Center · USBeijing Normal University · CNUniversity of Washington · USEuropean Synchrotron Radiation Facility · FRFred Hutch Cancer Center · USUnit of Virus Host Cell Interactions · FR

Funding

Vaccinating against IGFBP-2 to prevent ovarian cancer relapseP50CA083636 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI DRESCHER, CHARLES, URBAN, NICOLE DENISE · 1999 to 2015
$35.1M
ONCOLYTIC ADENOVIRUSES FOR CERVICAL CANCER GENE THERAPYR01CA080192 · NCI · UNIVERSITY OF WASHINGTON · PI LIEBER, ANDRE MICHAEL · 1999 to 2009
$2.0M
NCI NIH HHS P50 CA083636NCI NIH HHS R01 CA080192PHS HHS R01 HLA078836
6 · The paper itself

Abstract

Human adenovirus (Ad) serotypes Ad3, Ad7, Ad11, and Ad14, as well as a recently emerged strain of Ad14 (Ad14p1), use the epithelial junction protein desmoglein 2 (DSG2) as a receptor for infection. Unlike Ad interaction with CAR and CD46, structural details for Ad binding to DSG2 are still elusive. Using an approach based on Escherichia coli expression libraries of random Ad3 and Ad14p1 fiber knob mutants, we identified amino acid residues that, when mutated individually, ablated or reduced Ad knob binding to DSG2. These residues formed three clusters inside one groove at the extreme distal end of the fiber knob. The Ad3 fiber knob mutant library was also used to identify variants with increased affinity to DSG2. We found a number of mutations within or near the EF loop of the Ad3 knob that resulted in affinities to DSG2 that were several orders of magnitude higher than those to the wild-type Ad3 knob. Crystal structure analysis of one of the mutants showed that the introduced mutations make the EF loop more flexible, which might facilitate the interaction with DSG2. Our findings have practical relevance for cancer therapy. We have recently reported that an Ad3 fiber knob-containing recombinant protein (JO-1) is able to trigger opening of junctions between epithelial cancer cells which, in turn, greatly improved the intratumoral penetration and efficacy of therapeutic agents (I. Beyer, et al., Clin. Cancer Res. 18:3340-3351, 2012; I. Beyer, et al., Cancer Res. 71:7080-7090, 2011). Here, we show that affinity-enhanced versions of JO-1 are therapeutically more potent than the parental protein in a series of cancer models.

Indexed as

Host-Pathogen InteractionsProtein Interaction MappingAdenoviruses, HumanCapsid ProteinsCell LineCrystallography, X-RayDesmoglein 2DNA Mutational AnalysisHumansMutant ProteinsProtein BindingProtein ConformationProtein Interaction Domains and MotifsReceptors, VirusRecombinant ProteinsCapsid ProteinsDesmoglein 2DSG2 protein, humanhexon capsid protein, AdenovirusMutant ProteinsReceptors, VirusRecombinant Proteins

Identifiers

PMID23946456
PMCPMC3807342
OpenAlexW2115143194

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.