StressCovidV1, Ncbi, Merge, bibRecord, 000A29

Structural basis for influenza virus NS1 protein block of mRNA nuclear export.

Identifieur interne : 000A29 ( Ncbi/Merge ); précédent : 000A28; suivant : 000A30

Structural basis for influenza virus NS1 protein block of mRNA nuclear export.

Auteurs : Ke Zhang [États-Unis] ; Yihu Xie [États-Unis] ; Raquel Mu Oz-Moreno [États-Unis] ; Juan Wang [États-Unis] ; Liang Zhang [République populaire de Chine] ; Matthew Esparza [États-Unis] ; Adolfo García-Sastre [États-Unis] ; Beatriz M A. Fontoura [États-Unis] ; Yi Ren [États-Unis]

Source :

Nature microbiology [ 2058-5276 ] ; 2019.

RBID : pubmed:31263181

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English descriptors

Abstract

Influenza viruses antagonize key immune defence mechanisms via the virulence factor non-structural protein 1 (NS1). A key mechanism of virulence by NS1 is blocking nuclear export of host messenger RNAs, including those encoding immune factors^1-3; however, the direct cellular target of NS1 and the mechanism of host mRNA export inhibition are not known. Here, we identify the target of NS1 as the mRNA export receptor complex, nuclear RNA export factor 1-nuclear transport factor 2-related export protein 1 (NXF1-NXT1), which is the principal receptor mediating docking and translocation of mRNAs through the nuclear pore complex via interactions with nucleoporins^4,5. We determined the crystal structure of NS1 in complex with NXF1-NXT1 at 3.8 Å resolution. The structure reveals that NS1 prevents binding of NXF1-NXT1 to nucleoporins, thereby inhibiting mRNA export through the nuclear pore complex into the cytoplasm for translation. We demonstrate that a mutant influenza virus deficient in binding NXF1-NXT1 does not block host mRNA export and is attenuated. This attenuation is marked by the release of mRNAs encoding immune factors from the nucleus. In sum, our study uncovers the molecular basis of a major nuclear function of influenza NS1 protein that causes potent blockage of host gene expression and contributes to inhibition of host immunity.

DOI: 10.1038/s41564-019-0482-x
PubMed: 31263181

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<term>Cells, Cultured</term>
<term>Crystallography, X-Ray</term>
<term>Humans</term>
<term>Influenza A virus (genetics)</term>
<term>Influenza A virus (metabolism)</term>
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<term>Nucleocytoplasmic Transport Proteins (metabolism)</term>
<term>Protein Binding</term>
<term>RNA, Messenger (metabolism)</term>
<term>RNA-Binding Proteins (chemistry)</term>
<term>RNA-Binding Proteins (genetics)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Viral Nonstructural Proteins (genetics)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (métabolisme)</term>
<term>Cellules A549</term>
<term>Cellules cultivées</term>
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<term>Complexe protéique du pore nucléaire (métabolisme)</term>
<term>Complexes multiprotéiques ()</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Cristallographie aux rayons X</term>
<term>Grippe humaine (métabolisme)</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Noyau de la cellule (métabolisme)</term>
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<term>Protéines de liaison à l'ARN (génétique)</term>
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<front><div type="abstract" xml:lang="en">Influenza viruses antagonize key immune defence mechanisms via the virulence factor non-structural protein 1 (NS1). A key mechanism of virulence by NS1 is blocking nuclear export of host messenger RNAs, including those encoding immune factors<sup>1-3</sup>
; however, the direct cellular target of NS1 and the mechanism of host mRNA export inhibition are not known. Here, we identify the target of NS1 as the mRNA export receptor complex, nuclear RNA export factor 1-nuclear transport factor 2-related export protein 1 (NXF1-NXT1), which is the principal receptor mediating docking and translocation of mRNAs through the nuclear pore complex via interactions with nucleoporins<sup>4,5</sup>
. We determined the crystal structure of NS1 in complex with NXF1-NXT1 at 3.8 Å resolution. The structure reveals that NS1 prevents binding of NXF1-NXT1 to nucleoporins, thereby inhibiting mRNA export through the nuclear pore complex into the cytoplasm for translation. We demonstrate that a mutant influenza virus deficient in binding NXF1-NXT1 does not block host mRNA export and is attenuated. This attenuation is marked by the release of mRNAs encoding immune factors from the nucleus. In sum, our study uncovers the molecular basis of a major nuclear function of influenza NS1 protein that causes potent blockage of host gene expression and contributes to inhibition of host immunity.</div>
</front>
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<DateCompleted><Year>2020</Year>
<Month>01</Month>
<Day>20</Day>
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<Issue>10</Issue>
<PubDate><Year>2019</Year>
<Month>10</Month>
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<Title>Nature microbiology</Title>
<ISOAbbreviation>Nat Microbiol</ISOAbbreviation>
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<ArticleTitle>Structural basis for influenza virus NS1 protein block of mRNA nuclear export.</ArticleTitle>
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<Abstract><AbstractText>Influenza viruses antagonize key immune defence mechanisms via the virulence factor non-structural protein 1 (NS1). A key mechanism of virulence by NS1 is blocking nuclear export of host messenger RNAs, including those encoding immune factors<sup>1-3</sup>
; however, the direct cellular target of NS1 and the mechanism of host mRNA export inhibition are not known. Here, we identify the target of NS1 as the mRNA export receptor complex, nuclear RNA export factor 1-nuclear transport factor 2-related export protein 1 (NXF1-NXT1), which is the principal receptor mediating docking and translocation of mRNAs through the nuclear pore complex via interactions with nucleoporins<sup>4,5</sup>
. We determined the crystal structure of NS1 in complex with NXF1-NXT1 at 3.8 Å resolution. The structure reveals that NS1 prevents binding of NXF1-NXT1 to nucleoporins, thereby inhibiting mRNA export through the nuclear pore complex into the cytoplasm for translation. We demonstrate that a mutant influenza virus deficient in binding NXF1-NXT1 does not block host mRNA export and is attenuated. This attenuation is marked by the release of mRNAs encoding immune factors from the nucleus. In sum, our study uncovers the molecular basis of a major nuclear function of influenza NS1 protein that causes potent blockage of host gene expression and contributes to inhibition of host immunity.</AbstractText>
</Abstract>
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<ForeName>Ke</ForeName>
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<AffiliationInfo><Affiliation>Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xie</LastName>
<ForeName>Yihu</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Muñoz-Moreno</LastName>
<ForeName>Raquel</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, NY, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Global Health and Emerging Pathogens Institute, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, NY, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Juan</ForeName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Liang</ForeName>
<Initials>L</Initials>
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</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Esparza</LastName>
<ForeName>Matthew</ForeName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>García-Sastre</LastName>
<ForeName>Adolfo</ForeName>
<Initials>A</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-6551-1827</Identifier>
<AffiliationInfo><Affiliation>Department of Microbiology, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, NY, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Global Health and Emerging Pathogens Institute, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, NY, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Medicine, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, NY, USA.</Affiliation>
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Structural basis for influenza virus NS1 protein block of mRNA nuclear export.

Structural basis for influenza virus NS1 protein block of mRNA nuclear export.

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