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MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6
Creator
Wang, Jianhua
Feng, Yong
Hou, Wei
Chen, Lang
Yu, Ting
Zeng, Yan
Hu, Haitao
Ju, Zhao
Wang, Meirong
Xie, Linlin
Xiong, Hairong
Zhong, Chaojie
Source
PMC
abstract
BACKGROUND: The human myxovirus resistance 2 (Mx2/MxB) protein was originally found to regulate cytoplasmic-nuclear transport but was recently reported to restrict HIV-1 replication by binding to HIV-1 capsid (CA), preventing uncoating, the nuclear import of pre-integration complex (PIC) and viral DNA integration. This work explores the mechanisms of MxB-mediated HIV-1 inhibition. RESULTS: We demonstrated that MxB represses NUP358-mediated PIC nuclear import and HIV-1 replication. Moreover, MxB’s effects on PIC nuclear import and HIV-1 replication depend critically on cofactor cleavage and polyadenylation specificity factor subunit 6 (CPSF6). MxB binds nucleoporin NUP358, blocks NUP358-CA interaction, thereby impeding the nuclear import of HIV-1 PIC with CPSF6 binding to PIC. More intriguingly, CPSF6’s role in nuclear import depends on MxB, being a facilitator of HIV-1 nuclear import on its own, but becoming an inhibitor when MxB is present. CONCLUSIONS: Our work establishes that MxB impedes the NUP358-mediated HIV-1 nuclear import and viral replication cooperatively with CPSF6.
has issue date
2020-06-29
(
xsd:dateTime
)
bibo:doi
10.1186/s12977-020-00524-2
has license
no-cc
sha1sum (hex)
156b408dabc8aa1d5147b11878420f43b83fd1b5
schema:url
https://doi.org/10.1186/s12977-020-00524-2
resource representing a document's title
MxB impedes the NUP358-mediated HIV-1 pre-integration complex nuclear import and viral replication cooperatively with CPSF6
has PubMed Central identifier
PMC7322711
schema:publication
Retrovirology
resource representing a document's body
covid:156b408dabc8aa1d5147b11878420f43b83fd1b5#body_text
is
schema:about
of
named entity 'PIC'
named entity 'pre-integration complex'
named entity 'viral replication'
named entity 'nuclear import'
named entity 'mediated'
covid:arg/156b408dabc8aa1d5147b11878420f43b83fd1b5
named entity 'replication'
named entity 'HIV-1'
named entity 'HIV-1'
named entity 'protein'
named entity 'PIC'
named entity 'pre-integration complex'
named entity 'NUP358'
named entity 'HIV-1'
named entity 'PIC'
named entity 'NUP358'
named entity 'vector'
named entity 'nuclear import'
named entity 'streptomycin'
named entity 'HIV-1'
named entity 'nuclear pore'
named entity 'Statistical significance'
named entity 'lysis buffer'
named entity 'CPSF6'
named entity 'phenotypes'
named entity 'integrase'
named entity 'NUP98'
named entity 'cloned'
named entity 'HIV-1'
named entity 'antiviral'
named entity 'CPSF6'
named entity 'CPSF6'
named entity 'plasmids'
named entity 'Hemagglutinin'
named entity 'PIC'
named entity 'colocalization'
named entity 'paraformaldehyde'
named entity 'viral replication'
named entity 'HIV-1'
named entity 'NUP358'
named entity 'HIV-1'
named entity 'Immunoprecipitation'
named entity 'plasmids'
named entity 'nuclear import'
named entity 'Assay'
named entity 'nuclear import'
named entity 'HIV-1'
named entity 'nuclear import'
named entity 'incubation'
named entity 'siRNA'
named entity 'colocalization'
named entity 'nucleoporins'
named entity 'Protein'
named entity 'nucleoporins'
named entity 'NUP358'
named entity 'Infectivity'
named entity 'NIH'
named entity 'infection'
named entity 'biochemical'
named entity 'PIC'
named entity 'infection'
named entity 'HeLa'
named entity 'CPSF6'
named entity 'N-terminal'
named entity 'viral replication'
named entity 'HIV-1'
named entity 'host cell'
named entity 'HIV-1'
named entity 'antiviral activity'
named entity 'HIV-1'
named entity 'NUP358'
named entity 'transfected'
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