Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus

Dong, De-Li; Zhu, Shi-Qiang; Miao, Qiuhong; Zhu, Jie; Tang, Aoxing; Qi, Ruibin; Li, Teng; Yin, Daqiang; Liu, Guangqing

doi:10.1099/jgv.0.001358

Cited by 10 publications

(12 citation statements)

References 47 publications

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“…By sequence comparison, we found that caMAVS shares conserved structural domains (CARD-PRR-NC-TM) with MAVS of other mammalian species and that caMAVS shares the highest identity with sheep MAVS (98.1%). Further analysis using transiently expressed MAVS mutants mapped individual domains of caMAVS responsible for its distribution in Vero-SLAM cells, which have been described as a useful cell model to study PPRV infection [ 22 ]. The full-length caMAVS protein was localized in mitochondria, while caMAVS lacking the TM domain lost the mitochondrial localization and was found in both cytoplasm and nucleus.…”

Section: Discussionmentioning

confidence: 99%

“…Vero-SLAM cells support efficient replication of PPRV and the downstream signaling from caMAVS is functional. In a previous study, we demonstrated that nucleolin could inhibit PPRV replication in Vero-SLAMs [ 22 ]. All cells were grown with 1% antibiotics of penicillin and streptomycin (P/S) at 37 °C and with a 5% atmospheric CO 2 concentration.…”

Section: Methodsmentioning

confidence: 99%

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Caprine MAVS Is a RIG-I Interacting Type I Interferon Inducer Downregulated by Peste des Petits Ruminants Virus Infection

Miao

Chen

et al. 2021

Viruses

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The mitochondrial antiviral-signaling protein (MAVS, also known as VISA, IPS-1, or CARDIF) plays an essential role in the type I interferon (IFN) response and in retinoic acid-inducible gene I (RIG-I) mediated antiviral innate immunity in mammals. In this study, the caprine MAVS gene (caMAVS, 1566 bp) was identified and cloned. The caMAVS shares the highest amino acid similarity (98.1%) with the predicted sheep MAVS. Confocal microscopy analysis of partial deletion mutants of caMAVS revealed that the transmembrane and the so-called Non-Characterized domains are indispensable for intracellular localization to mitochondria. Overexpression of caMAVS in caprine endometrial epithelial cells up-regulated the mRNA levels of caprine interferon-stimulated genes. We concluded that caprine MAVS mediates the activation of the type I IFN pathway. We further demonstrated that both the CARD-like domain and the transmembrane domain of caMAVS were essential for the activation of the IFN-β promotor. The interaction between caMAVS and caprine RIG-I and the vital role of the CARD and NC domain in this interaction was demonstrated by co-immunoprecipitation. Upon infection with the Peste des Petits Ruminants Virus (PPRV, genus Morbillivirus), the level of MAVS was greatly reduced. This reduction was prevented by the addition of the proteasome inhibitor MG132. Moreover, we found that viral protein V could interact and colocalize with MAVS. Together, we identified caMAVS as a RIG-I interactive protein involved in the activation of type I IFN pathways in caprine cells and as a target for PPRV immune evasion.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Caprine MAVS Is a RIG-I Interacting Type I Interferon Inducer Downregulated by Peste des Petits Ruminants Virus Infection

Miao

Chen

et al. 2021

Viruses

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“…The applications of nanobodies in diagnostics and therapeutics are exponentially growing in biomedical and veterinary fields [ 46 , 61 , 62 , 63 ]. A very limited number of and extremely expensive biological antiviral treatments are available to control PPRV infections in sheep and goats [ 64 , 65 , 66 ]. The PPR antivirals cost high from the perspective of animal production [ 64 , 65 , 66 , 67 ].…”

Section: Discussionmentioning

confidence: 99%

Development of Nanobodies Targeting Peste des Petits Ruminants Virus: The Prospect in Disease Diagnosis and Therapy

Kinimi

Vincke

Odongo

et al. 2021

Animals

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Peste des petits ruminants virus (PPRV) causes a highly devastating disease, peste des petits ruminants (PPR) of sheep and goats, that threatens food security, small ruminant production, and the conservation of wild small ruminants in many developing countries, especially in Africa. Robust serological and molecular diagnostic tools are available to detect PPRV infection, but they were mainly developed for domestic sheep and goats. The presence of a wide host range for PPRV does present serological diagnostic challenges. New innovative diagnostic tools are needed to detect PPRV in atypical hosts (e.g., Camelidae, Suidae, and Bovinae), in wildlife ecosystems and in complex field situations. Interestingly, single-domain antigen binding fragments (nanobodies) derived from heavy-chain-only camelid antibodies have emerged as a new hope in the development of accurate, rapid, and cost-effective diagnostic tools in veterinary and biomedical fields that are suitable for low-income countries. The main objective of this study was to construct an immune nanobody library to retrieve PPRV-reactive nanobodies that enable the development of diagnostic and therapeutic nanobodies in the future. Here, a strategy was developed whereby an alpaca (Vicugna pacos) was immunized with a live attenuated vaccine strain (PPRV/N/75/1) to raise an affinity-matured immune response in the heavy-chain-only antibody classes. The nanobody gene repertoire was engineered in pMECS-GG phagemid, whereby a ccdB gene (encoding a lethal protein) was substituted by the nanobody gene. An immune nanobody library with approximately sixty-four million independent transformants was constructed, of which 100% contained an insert with the proper size of nanobody gene. Following phage display and biopanning, nine nanobodies that specifically recognise completely inactivated PPRV were identified on enzyme-linked immunosorbent assay. They showed superb potency in rapidly identifying PPRV, which is likely to open a new perspective in the diagnosis and possible treatment of PPR infection.

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“…The localization of nucleolin is changed in the virus infected cells. NCL interacts with PPRV N protein and indirectly inhibits the growth of PPRV by stimulating the interferon (IFN) pathway [52]. By contrast, NCL facilitates the entry of influenza A viruses and enterovirus (EV)71 [53,54].…”

Section: Discussionmentioning

confidence: 99%

Quantitative Analysis of Lysine Acetylation in Vero Cells Infected With Peste Des Petits Ruminants Virus

Meng

Zhu

Zhang

et al. 2021

Preprint

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Background: Peste des petits ruminants virus (PPRV) is a negative-stranded RNA virus belonging to the Paramyxoviridae family and causes acute, highly contagious disease in small ruminants. Lysine acetylation plays central role in regulating gene expression. However, the extent and function of lysine acetylation in host cells during PPRV infection remains unknown. Methods: Lysine acetylation of PPRV-infected Vero cells was tested and differentially expressed lysine acetylation was found. The acetylated peptides were enriched using specific antibody and labeled with demethylation. Proteins with acetylation sites were identified. Subsequently, intensive bioinformatics analysis of succinylome of PPRV-infected Vero cells was were performed. In this study, intensive proteomic quantification analysis of the proteome and acetylome of PPRV-infected Vero cells was performed using dimethylation labeling-based quantitative proteomics. Results: We identified 4729 cellular proteins and 1068 proteins with 2641 modification sites quantifiable detected by mass spectrometry, of which 304 proteins with 410 acetylation sites were significantly acetylated in response to PPRV infection. Bioinformatics analyses revealed that the differentially acetylated proteins mainly participated in carbohydrate catabolic and DNA metabolic process, and were associated with multifarious functions, suggesting that intracellular activities were extensively changed after PPRV infection. Protein-protein interaction (PPI) network of the identified proteins further indicated that a variety of chaperone and ribosome processes were modulated by acetylation. Conclusions: To our knowledge, this is the first study on acetylome in host cell infected with PPRV. It provides an important baseline to future study the roles of acetylation in the host response to PPRV replication.

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Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus

Cited by 10 publications

References 47 publications

Caprine MAVS Is a RIG-I Interacting Type I Interferon Inducer Downregulated by Peste des Petits Ruminants Virus Infection

Caprine MAVS Is a RIG-I Interacting Type I Interferon Inducer Downregulated by Peste des Petits Ruminants Virus Infection

Development of Nanobodies Targeting Peste des Petits Ruminants Virus: The Prospect in Disease Diagnosis and Therapy

Quantitative Analysis of Lysine Acetylation in Vero Cells Infected With Peste Des Petits Ruminants Virus

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