Nucleolin interacts with influenza A nucleoprotein and contributes to viral ribonucleoprotein complexes nuclear trafficking and efficient influenza viral replication

Terrier, B.; Carron, Coralie; Chassey, Beno it de; Dubois, Julia; Traversier, Aurélien; Julien, Thomas; Cartet, Gaëlle; Proust, Anaïs; Hacot, Sabine; Ressnikoff, Denis; Lotteau, Vincent; Lina, Bruno; Diaz, Jean‐Jacques; Moulés, Vincent; Rosa‐Calatrava, Manuel

doi:10.1038/srep29006

Cited by 32 publications

(29 citation statements)

References 85 publications

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“…The discovery that Ncl could be acetylated on Lysine residues in the N-terminal domain and that this Ac-Ncl is specifically co-localized with nuclear speckles suggested that Ac-Ncl could be involved in some aspect of pre-mRNA processing [16]. Ncl has been implicated in different aspects of mRNA metabolism/regulation, such as mRNA adenylation [38,39], mRNA stability [13,40], translation regulation [41][42][43][44][45][46], nuclear export of RNPs particles [47], but there are no report demonstrating a direct Ncl implication in pre-mRNA splicing. Ncl binds to SLS2-A7 stem-loop structure present in HIV RNA sequences [20] that are involved in HIV-RNA splicing and export, and seems to affects the processing of several miRNA [21], but there are no experimental demonstration of a direct function of Ncl in these processes.…”

Section: Discussionmentioning

confidence: 99%

Nucleolin Interacts and Co-Localizes with Components of Pre-Catalytic Spliceosome Complexes

Ugrinova¹,

Chalabi-Dchar²,

Monier³

et al. 2019

Sci

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Nucleolin is an RNA binding protein that is involved in many post-transcriptional regulation steps of messenger RNAs in addition to its nucleolar role in ribosomal RNA transcription and assembly in pre-ribosomes. Acetylated nucleolin was found to be associated with nuclear speckles and to co-localize with the splicing factor SC35. Previous nuclear pull down of nucleolin identified several splicing components and factors involved in RNA polymerase II transcription associated with nucleolin. In this report, we show that these splicing components are specifics of the pre-catalytic A and B spliceosomes, while proteins recruited in the Bact, C and P complexes are absent from the nucleolin interacting proteins. Furthermore, we show that acetylated nucleolin co-localized with P-SF3B1, a marker of co-transcriptional active spliceosomes. P-SF3B1 complexes can be pulled down with nucleolin specific antibodies. Interestingly, the alternative splicing of Fibronectin at the IIICS and EDB sites was affected by nucleolin depletion. These data are consistent with a model where nucleolin could be a factor bridging RNA polymerase II transcription and assembly of pre-catalytic spliceosome similarly to its function in the co-transcriptional maturation of pre-rRNA.

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Section: Discussionmentioning

confidence: 99%

Nucleolin Interacts and Co-Localizes with Components of Pre-Catalytic Spliceosome Complexes

Ugrinova¹,

Chalabi-Dchar²,

Monier³

et al. 2019

Sci

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“…HA interacted with cell surface NCL which is required for virus internalization 34 . NP was demonstrated as an interaction partner of endogenous NCL during early infection in cytoplasm after its translocation 35 , 36 . Terrier et al .…”

Section: Discussionmentioning

confidence: 99%

“…Multiple IAV viral proteins interact with NCL during infection 34 – 36 . However, it is currently unknown about the physiological consequences of interaction between IAV NS1 and NCL.…”

Section: Introductionmentioning

confidence: 99%

Non-structural protein 1 of H3N2 influenza A virus induces nucleolar stress via interaction with nucleolin

Yan

Wang

et al. 2017

Sci Rep

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The nucleolus is a stress sensor associated with cell cycle progression and a central hub for the replication of pathogenic RNA viruses. However, the role of nucleolus in influenza A virus infection has not been well studied. Here we show that the interaction between NS1 protein of influenza A/Shantou/602/06 (H3N2) and nucleolin, a ubiquitous protein of nucleolus repressed RNA Pol I-dependent transcription via establishing hyper-methylation in the UCE of rRNA gene promoter. NS1 expressed cells showed significant association of ribosomal proteins with MDM2, and p53 accumulation, suggesting induced nucleolar stress. Disruption of the interaction of NS1 with nucleolin or overexpression of nucleolin in NS1 expressed cells revived RNA Pol I-dependent transcription, indicating nucleolin could be one target for NS1 to repress rRNA synthesis of host cells. Our present study suggests that NS1 protein of H3N2 could induce nucleolar stress based on epigenetic alteration of rRNA gene promoter via interaction with nucleolin.

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“…The A549 human lung adenocarcinoma epithelial cell line and the Calu-3, a human bronchial epithelial cell line, have been widely used to study influenza virus-host interactions [63][64][65][66][67][68][69][70][71][72][73][74][75][76][77][78], viral protein biochemistry [79,80], drug studies [81][82][83] and for performing large-scale screens, such as a CRISPR activation screen, to identify genes that inhibit influenza virus infection when they are overexpressed [82].…”

Section: Immortalized Lung Cells Eg A549 and Calu-3mentioning

confidence: 99%

Alternative Experimental Models for Studying Influenza Proteins, Host–Virus Interactions and Anti-Influenza Drugs

Chua

Engelberg

et al. 2019

Pharmaceuticals

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Ninety years after the discovery of the virus causing the influenza disease, this malady remains one of the biggest public health threats to mankind. Currently available drugs and vaccines only partially reduce deaths and hospitalizations. Some of the reasons for this disturbing situation stem from the sophistication of the viral machinery, but another reason is the lack of a complete understanding of the molecular and physiological basis of viral infections and host-pathogen interactions. Even the functions of the influenza proteins, their mechanisms of action and interaction with host proteins have not been fully revealed. These questions have traditionally been studied in mammalian animal models, mainly ferrets and mice (as well as pigs and non-human primates) and in cell lines. Although obviously relevant as models to humans, these experimental systems are very complex and are not conveniently accessible to various genetic, molecular and biochemical approaches. The fact that influenza remains an unsolved problem, in combination with the limitations of the conventional experimental models, motivated increasing attempts to use the power of other models, such as low eukaryotes, including invertebrate, and primary cell cultures. In this review, we summarized the efforts to study influenza in yeast, Drosophila, zebrafish and primary human tissue cultures and the major contributions these studies have made toward a better understanding of the disease. We feel that these models are still under-utilized and we highlight the unique potential each model has for better comprehending virus-host interactions and viral protein function.

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Nucleolin interacts with influenza A nucleoprotein and contributes to viral ribonucleoprotein complexes nuclear trafficking and efficient influenza viral replication

Cited by 32 publications

References 85 publications

Nucleolin Interacts and Co-Localizes with Components of Pre-Catalytic Spliceosome Complexes

Nucleolin Interacts and Co-Localizes with Components of Pre-Catalytic Spliceosome Complexes

Non-structural protein 1 of H3N2 influenza A virus induces nucleolar stress via interaction with nucleolin

Alternative Experimental Models for Studying Influenza Proteins, Host–Virus Interactions and Anti-Influenza Drugs

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