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      Nucleolin interacts with the rabbit hemorrhagic disease virus replicase RdRp, nonstructural proteins p16 and p23, playing a role in virus replication

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          Abstract

          Rabbit hemorrhagic disease virus (RHDV) is a member of the Caliciviridae family and cannot be propagated in vitro, which has impeded the progress of investigating its replication mechanism. Construction of an RHDV replicon system has recently provided a platform for exploring RHDV replication in host cells. Here, aided by this replicon system and using two-step affinity purification, we purified the RHDV replicase and identified its associated host factors. We identified rabbit nucleolin (NCL) as a physical link, which mediating the interaction between other RNA-dependent RNA polymerase (RdRp)-related host proteins and the viral replicase RdRp. We found that the overexpression or knockdown of NCL significantly increased or severely impaired RHDV replication in RK-13 ​cells, respectively. NCL was identified to directly interact with RHDV RdRp, p16, and p23. Furthermore, NCL knockdown severely impaired the binding of RdRp to RdRp-related host factors. Collectively, these results indicate that the host protein NCL is essential for RHDV replication and acts as a physical link between viral replicase and host proteins.

          Highlights

          • •

            The host protein associated to rabbit hemorrhagic disease virus (RHDV) replicase was identified.

          • •

            Rabbit nucleolin (NCL) is essential for RHDV replication.

          • •

            NCL directly interacts with RHDV RdRp, p16, and p23.

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          Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories.

          Johan A den Boon, Paul Ahlquist (2010)
          Positive-strand RNA virus genome replication is invariably associated with extensively rearranged intracellular membranes. Recent biochemical and electron microscopy analyses, including three-dimensional electron microscope tomographic imaging, have fundamentally advanced our understanding of the ultrastructure and function of organelle-like RNA replication factories. Notably, for a range of positive-strand RNA viruses embodying many major differences, independent studies have revealed multiple common principles. These principles include that RNA replication often occurs inside numerous virus-induced vesicles invaginated or otherwise elaborated from a continuous, often endoplasmic reticulum-derived membrane network. Where analyzed, each such vesicle typically contains only one or a few genome replication intermediates in conjunction with many copies of viral nonstructural proteins. In addition, these genome replication compartments often are closely associated with sites of virion assembly and budding. Our understanding of these complexes is growing, providing substantial new insights into the organization, coordination, and potential control of crucial processes in virus replication.
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            RNA-binding protein nucleolin in disease.

            Kotb Abdelmohsen, Myriam Gorospe (2012)
            Nucleolin is a multifunctional protein localized primarily in the nucleolus, but also found in the nucleoplasm, cytoplasm and cell membrane. It is involved in several aspects of DNA metabolism, and participates extensively in RNA regulatory mechanisms, including transcription, ribosome assembly, mRNA stability and translation, and microRNA processing. Nucleolin's implication in disease is linked to its ability to associate with target RNAs via its four RNA-binding domains and its arginine/glycin-rich domain. By modulating the post-transcriptional fate of target mRNAs, which typically bear AU-rich and/or G-rich elements, nucleolin has been linked to cellular events that influence disease, notably cell proliferation and protection against apoptotic death. Through its diverse RNA functions, nucleolin is increasingly implicated in pathological processes, particularly cancer and viral infection. Here, we review the RNA-binding activities of nucleolin, its influence on gene expression patterns, and its impact upon diseases. We also discuss the rising interest in targeting nucleolin therapeutically.
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              The role of human ribosomal proteins in the maturation of rRNA and ribosome production.

              Rachel Idol, Warren P Mason, Jack H. Ladenson … (2008)
              Production of ribosomes is a fundamental process that occurs in all dividing cells. It is a complex process consisting of the coordinated synthesis and assembly of four ribosomal RNAs (rRNA) with about 80 ribosomal proteins (r-proteins) involving more than 150 nonribosomal proteins and other factors. Diamond Blackfan anemia (DBA) is an inherited red cell aplasia caused by mutations in one of several r-proteins. How defects in r-proteins, essential for proliferation in all cells, lead to a human disease with a specific defect in red cell development is unknown. Here, we investigated the role of r-proteins in ribosome biogenesis in order to find out whether those mutated in DBA have any similarities. We depleted HeLa cells using siRNA for several individual r-proteins of the small (RPS6, RPS7, RPS15, RPS16, RPS17, RPS19, RPS24, RPS25, RPS28) or large subunit (RPL5, RPL7, RPL11, RPL14, RPL26, RPL35a) and studied the effect on rRNA processing and ribosome production. Depleting r-proteins in one of the subunits caused, with a few exceptions, a decrease in all r-proteins of the same subunit and a decrease in the corresponding subunit, fully assembled ribosomes, and polysomes. R-protein depletion, with a few exceptions, led to the accumulation of specific rRNA precursors, highlighting their individual roles in rRNA processing. Depletion of r-proteins mutated in DBA always compromised ribosome biogenesis while affecting either subunit and disturbing rRNA processing at different levels, indicating that the rate of ribosome production rather than a specific step in ribosome biogenesis is critical in patients with DBA.
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                Author and article information

                Contributors
                Guangzhi Tong
                Guangqing Liu
                Journal
                Journal ID (nlm-ta): Virol Sin
                Journal ID (iso-abbrev): Virol Sin
                Title: Virologica Sinica
                Publisher: Wuhan Institute of Virology, Chinese Academy of Sciences
                ISSN (Print): 1674-0769
                ISSN (Electronic): 1995-820X
                Publication date PMC-release: 12 January 2022
                Publication date Collection: February 2022
                Publication date (Electronic): 12 January 2022
                Volume: 37
                Issue: 1
                Pages: 48-59
                Affiliations
                [a ]Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, 200241, China
                [b ]Laboratory of Virology, Wageningen University and Research, Wageningen, 6708 PB, the Netherlands
                [c ]Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China
                Author notes
                [∗ ]Corresponding author. Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, 200241, China. gztong@ 123456shvri.ac.cn liugq@ 123456shvri.ac.cn
                Article
                Publisher Item ID: S1995-820X(22)00004-9
                DOI: 10.1016/j.virs.2022.01.004
                PMC ID: 8922422
                PubMed ID: 35234629
                SO-VID: 4df4def9-cc5c-42b6-a261-a491e53578b4
                Copyright © © 2022 The Authors
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 23 June 2021
                Date accepted : 15 September 2021
                Categories
                Subject: Research Article

                Keywords: rabbit hemorrhagic disease virus (rhdv),nucleolin,virus replication,rna-dependent rna polymerase (rdrp)
                Data availability:
                Keywords: rabbit hemorrhagic disease virus (rhdv), nucleolin, virus replication, rna-dependent rna polymerase (rdrp)

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