Evidence map›Paper›PMID 25999342›Full record

ArticleNucleic acids research2015

Characterization of human herpesvirus 6A/B U94 as ATPase, helicase, exonuclease and DNA-binding proteins.

Frédéric Trempe, Annie Gravel, Isabelle Dubuc, Nina Wallaschek, Vanessa Collin, Shella Gilbert-Girard, Guillaume Morissette, Benedikt B Kaufer, Louis Flamand

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Vertebrate-tropism of a cressdnavirus lineage implicated by poxvirus gene capture.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

9 authors at 2 institutions in 2 countries.

Frédéric TrempeDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada.
Annie GravelDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada.
Isabelle DubucDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada.
Nina WallaschekInstitut für Virologie, Freie Universität Berlin, Berlin 14163, Germany.
Vanessa CollinDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada.
Shella Gilbert-GirardDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada.
Guillaume MorissetteDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada.
Benedikt B KauferInstitut für Virologie, Freie Universität Berlin, Berlin 14163, Germany.
Louis FlamandDivision of Infectious Disease and Immunity, CHU de Québec Research Center, Quebec city, Quebec G1V 4G2, Canada Department of microbiology, infectious disease and immunology, Faculty of Medicine, Université Laval, Quebec city, Québec,G1V 0A6 Canada Louis.flamand@crchul.ulaval.ca.
Freie Universität Berlin · DEUniversité Laval · CA

Funding

Canadian Institutes of Health Research MOP 123214
6 · The paper itself

Abstract

Human herpesvirus-6A (HHV-6A) and HHV-6B integrate their genomes into the telomeres of human chromosomes, however, the mechanisms leading to integration remain unknown. HHV-6A/B encode a protein that has been proposed to be involved in integration termed U94, an ortholog of adeno-associated virus type 2 (AAV-2) Rep68 integrase. In this report, we addressed whether purified recombinant maltose-binding protein (MBP)-U94 fusion proteins of HHV-6A/B possess biological functions compatible with viral integration. We could demonstrate that MBP-U94 efficiently binds both dsDNA and ssDNA containing telomeric repeats using gel shift assay and surface plasmon resonance. MBP-U94 is also able to hydrolyze adenosine triphosphate (ATP) to ADP, providing the energy for further catalytic activities. In addition, U94 displays a 3' to 5' exonuclease activity on dsDNA with a preference for 3'-recessed ends. Once the DNA strand reaches 8-10 nt in length, the enzyme dissociates it from the complementary strand. Lastly, MBP-U94 compromises the integrity of a synthetic telomeric D-loop through exonuclease attack at the 3' end of the invading strand. The preferential DNA binding of MBP-U94 to telomeric sequences, its ability to hydrolyze ATP and its exonuclease/helicase activities suggest that U94 possesses all functions required for HHV-6A/B chromosomal integration.

Indexed as

Adenosine TriphosphatasesDNA-Binding ProteinsDNA HelicasesExodeoxyribonucleasesHerpesvirus 6, HumanProtein BindingSequence AlignmentViral ProteinsAdenosine TriphosphatasesDNA-Binding ProteinsDNA HelicasesExodeoxyribonucleasesrep proteins, Adeno-associated virus 2Viral Proteins

Identifiers

PMID25999342
PMCPMC4499131
OpenAlexW2148886003

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.