Evidence map›Paper›PMID 35653410›Full record

ArticlePLoS pathogens2022

The small nonstructural protein NP1 of human bocavirus 1 directly interacts with Ku70 and RPA70 and facilitates viral DNA replication.

Kang Ning, Zekun Wang, Fang Cheng, Ziying Yan, Jianming Qiu

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

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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

5 authors at 2 institutions in 1 country.

Kang NingDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Zekun WangDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Fang ChengDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Ziying YanDepartment of Anatomy and Cell Biology, University of Iowa, Iowa City, Iowa, United States of America.
Jianming QiuDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas, United States of America.ORCID 0000-0001-9850-1695
University of Kansas Medical Center · USUniversity of Iowa · US

Funding

Vector Core-Core 2P30DK054759 · NIDDK · UNIVERSITY OF IOWA · PI Alejandro Antonio Pezzulo · 1998 to 2026
$30.5M
Viral and Host Determinants of Parvovirus ReplicationR01AI150877 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI QIU, JIANMING · 2020 to 2024
$2.4M
Mechanisms Underlying the Transduction Polarity of AAV in Polarized Human Airway EpitheliumR21AI151542 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI QIU, JIANMING, YAN, ZIYING · 2020 to 2021
$435k
Human bocavirus 1 (HBoV1) capsid entry and intracellular trafficking of polarized human airway epitheliumR21AI139572 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI QIU, JIANMING, YAN, ZIYING · 2018 to 2019
$434k
NIAID NIH HHS R01 AI150877NIAID NIH HHS R21 AI139572NIAID NIH HHS R21 AI151542NIDDK NIH HHS P30 DK054759
6 · The paper itself

Abstract

Human bocavirus 1 (HBoV1), a member of the genus Bocaparvovirus of the family Parvoviridae, causes acute respiratory tract infections in young children. Well-differentiated pseudostratified human airway epithelium cultured at an air-liquid interface (HAE-ALI) is an ideal in vitro culture model to study HBoV1 infection. Unique to other parvoviruses, bocaparvoviruses express a small nonstructured protein NP1 of ~25 kDa from an open reading frame (ORF) in the center of the viral genome. NP1 plays an important role in viral DNA replication and pre-mRNA processing. In this study, we performed an affinity purification assay to identify HBoV1 NP1-inteacting proteins. We identified that Ku70 and RPA70 directly interact with the NP1 at a high binding affinity, characterized with an equilibrium dissociation constant (KD) of 95 nM and 122 nM, respectively. Furthermore, we mapped the key NP1-interacting domains of Ku70 at aa266-439 and of RPA70 at aa181-422. Following a dominant negative strategy, we revealed that the interactions of Ku70 and RPA70 with NP1 play a significant role in HBoV1 DNA replication not only in an in vitro viral DNA replication assay but also in HBoV1-infected HAE-ALI cultures. Collectively, our study revealed a novel mechanism by which HBoV1 NP1 enhances viral DNA replication through its direct interactions with Ku70 and RPA70.

Indexed as

Human bocavirusParvoviridae InfectionsChildChild, PreschoolDNA ReplicationDNA, ViralGenome, ViralHumansVirus ReplicationDNA, Viral

Identifiers

PMID35653410
PMCPMC9197078
OpenAlexW4281666193

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.