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Article ; Online: Mapping of RNase P Ribozyme Regions in Proximity with a Human RNase P Subunit Protein Using Fe(II)-EDTA Cleavage and Nuclease Footprint Analyses.

Trang, Phong / Smith, Adam / Liu, Fenyong

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2666, Page(s) 55–67

Abstract: Ribonuclease P (RNase P), which may consist of both protein subunits and a catalytic RNA part, is responsible for 5' maturation of tRNA by cleaving the 5'-leader sequence. In Escherichia coli, RNase P contains a catalytic RNA subunit (M1 RNA) and a ... ...

Abstract	Ribonuclease P (RNase P), which may consist of both protein subunits and a catalytic RNA part, is responsible for 5' maturation of tRNA by cleaving the 5'-leader sequence. In Escherichia coli, RNase P contains a catalytic RNA subunit (M1 RNA) and a protein factor (C5 protein). In human cells, RNase P holoenzyme consists of an RNA subunit (H1 RNA) and multiple protein subunits that include human RPP29 protein. M1GS, a sequence specific targeting ribozyme derived from M1 RNA, can be constructed to target a specific mRNA to degrade it in vitro. Recent studies have shown that M1GS ribozymes are efficient in blocking the expression of viral mRNAs in cultured cells and in animals. These results suggest that RNase P ribozymes have the potential to be useful in basic research and in clinical applications. It has been shown that RNase P binding proteins, such as C5 protein and RPP29, can enhance the activities of M1GS RNA in processing a natural tRNA substrate and a target mRNA. Understanding how RPP29 binds to M1GS RNA and enhances the enzyme's catalytic activity will provide great insight into developing more robust gene-targeting ribozymes for in vivo application. In this chapter, we describe the methods of using Fe(II)-ethylenediaminetetraacetic acid (EDTA) cleavage and nuclease footprint analyses to determine the regions of a M1GS ribozyme that are in proximity to RPP29 protein.
MeSH term(s)	Animals ; Humans ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; RNA, Catalytic/metabolism ; Edetic Acid ; Protein Subunits/metabolism ; RNA/chemistry ; RNA, Messenger/genetics ; Escherichia coli/metabolism ; Endonucleases/metabolism
Chemical Substances	Ribonuclease P (EC 3.1.26.5) ; RNA, Catalytic ; Fe(II)-EDTA (15651-72-6) ; Edetic Acid (9G34HU7RV0) ; Protein Subunits ; RNA (63231-63-0) ; RNA, Messenger ; Endonucleases (EC 3.1.-)
Language	English
Publishing date	2023-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3191-1_4
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Potential Application of the CRISPR/Cas9 System against Herpesvirus Infections.

Chen, Yuan-Chuan / Sheng, Jingxue / Trang, Phong / Liu, Fenyong

Viruses

2018 Volume 10, Issue 6

Abstract: The CRISPR/Cas9 system has been applied in the genome editing and disruption of latent infections for herpesviruses such as the herpes simplex virus, Epstein⁻Barr virus, cytomegalovirus, and Kaposi's sarcoma-associated herpesvirus. CRISPR/Cas9-directed ... ...

Abstract	The CRISPR/Cas9 system has been applied in the genome editing and disruption of latent infections for herpesviruses such as the herpes simplex virus, Epstein⁻Barr virus, cytomegalovirus, and Kaposi's sarcoma-associated herpesvirus. CRISPR/Cas9-directed mutagenesis can introduce similar types of mutations to the viral genome as can bacterial artificial chromosome recombination engineering, which maintains and reconstitutes the viral genome successfully. The cleavage mediated by CRISPR/Cas9 enables the manipulation of disease-associated viral strains with unprecedented efficiency and precision. Additionally, current therapies for herpesvirus productive and latent infections are limited in efficacy and cannot eradicate viruses. CRISPR/Cas9 is potentially adapted for antiviral treatment by specifically targeting viral genomes during latent infections. This review, which focuses on recently published progress, suggests that the CRISPR/Cas9 system is not only a useful tool for basic virology research, but also a promising strategy for the control and prevention of herpesvirus latent infections.
MeSH term(s)	Animals ; CRISPR-Cas Systems ; Cytomegalovirus/genetics ; Gene Editing ; Genome, Viral ; Herpesviridae/genetics ; Herpesviridae Infections/prevention & control ; Herpesviridae Infections/therapy ; Herpesvirus 4, Human/genetics ; Herpesvirus 8, Human/genetics ; Humans ; Mice ; Mutagenesis ; Simplexvirus/genetics ; Virus Latency
Language	English
Publishing date	2018-05-29
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v10060291
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Article: Mapping the regions of RNase P catalytic RNA that are potentially in close contact with its protein cofactor.

Trang, Phong / Liu, Fenyong

Methods in molecular biology (Clifton, N.J.)

2008 Volume 488, Page(s) 267–277

Abstract: Ribonuclease P (RNase P) from Escherichia coli is a transfer RNA (tRNA)-processing enzyme and consists of a catalytic RNA subunit (M1 RNA) and a protein component (C5 protein). M1GS, a gene-targeting ribozyme derived from M1 RNA, can cleave a target ... ...

Abstract	Ribonuclease P (RNase P) from Escherichia coli is a transfer RNA (tRNA)-processing enzyme and consists of a catalytic RNA subunit (M1 RNA) and a protein component (C5 protein). M1GS, a gene-targeting ribozyme derived from M1 RNA, can cleave a target messenger RNA (mRNA) efficiently in vitro and inhibit its expression effectively in cultured cells. It has been shown that C5 protein can significantly increase the activities of M1 ribozyme and M1GS RNA in cleaving a natural tRNA substrate and a target mRNA, respectively. Understanding how C5 binds to M1GS RNA and affects the specific interactions between the ribozyme and its target mRNA substrates may facilitate the development of gene-targeting ribozymes that function effectively in vivo in the presence of cellular proteins. We describe the methods to determine the regions of a M1GS ribozyme that are potentially in close proximity to C5 protein. Specifically, methods are described in detail in using Fe(II)-ethylenediaminetetraacetic acid (EDTA) cleavage and nuclease footprint analyses to map the regions of the ribozyme in the absence and presence of C5 protein. These methods intend to provide experimental protocols for studying the regions of RNase P ribozyme that are in close contact with C5 protein.
MeSH term(s)	Edetic Acid/chemistry ; Ferrous Compounds/chemistry ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism ; RNA/chemistry ; RNA/metabolism ; RNA, Catalytic/chemistry ; RNA, Catalytic/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/metabolism
Chemical Substances	Ferrous Compounds ; Proteins ; RNA, Catalytic ; RNA (63231-63-0) ; Edetic Acid (9G34HU7RV0) ; Ribonuclease P (EC 3.1.26.5)
Language	English
Publishing date	2008
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1007/978-1-60327-475-3_19
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Article ; Online: Inhibition of human cytomegalovirus major capsid protein expression and replication by ribonuclease P-associated external guide sequences.

Deng, Qiudi / Liu, Yujun / Li, Xin / Yan, Bin / Sun, Xu / Tang, Wei / Trang, Phong / Yang, Zhu / Gong, Hao / Wang, Yu / Lu, Jie / Chen, Jun / Xia, Chuan / Xing, Xiwen / Lu, Sangwei / Liu, Fenyong

RNA (New York, N.Y.)

2019 Volume 25, Issue 5, Page(s) 645–655

Abstract: External guide sequences (EGSs) signify the short RNAs that induce ribonuclease P (RNase P), an enzyme responsible for processing the 5' termini of tRNA, to specifically cleave a target mRNA by forming a precursor tRNA-like complex. Hence, the EGS ... ...

Abstract	External guide sequences (EGSs) signify the short RNAs that induce ribonuclease P (RNase P), an enzyme responsible for processing the 5' termini of tRNA, to specifically cleave a target mRNA by forming a precursor tRNA-like complex. Hence, the EGS technology may serve as a potential strategy for gene-targeting therapy. Our previous studies have revealed that engineered EGS variants induced RNase P to efficiently hydrolyze target mRNAs. In the present research, an EGS variant was designed to be complementary to the mRNA coding for human cytomegalovirus (HCMV) major capsid protein (MCP), which is vital to form the viral capsid. In vitro, the EGS variant was about 80-fold more efficient in inducing human RNase P-mediated cleavage of the target mRNA than a natural tRNA-derived EGS. Moreover, the expressed variant and natural tRNA-originated EGSs led to a decrease of MCP expression by 98% and 73%-74% and a decrease of viral growth by about 10,000- and 200-fold in cells infected with HCMV, respectively. These results reveal direct evidence that the engineered EGS variant has higher efficiency in blocking the expression of HCMV genes and viral growth than the natural tRNA-originated EGS. Therefore, our findings imply that the EGS variant can be a potent candidate agent for the treatment of infections caused by HCMV.
MeSH term(s)	Base Pairing ; Capsid Proteins/biosynthesis ; Capsid Proteins/genetics ; Cell Line, Transformed ; Cell Line, Tumor ; Cytomegalovirus/genetics ; Cytomegalovirus/metabolism ; Fibroblasts/metabolism ; Fibroblasts/virology ; Gene Expression Regulation, Viral ; Gene Targeting/methods ; Genetic Engineering/methods ; Host-Pathogen Interactions/genetics ; Humans ; Molecular Targeted Therapy ; Neuroglia/metabolism ; Neuroglia/virology ; Nucleic Acid Conformation ; Primary Cell Culture ; RNA Cleavage ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Transfer, Ser/chemistry ; RNA, Transfer, Ser/genetics ; RNA, Transfer, Ser/metabolism ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; Virus Replication/physiology
Chemical Substances	Capsid Proteins ; RNA, Messenger ; RNA, Transfer, Ser ; RNA, Viral ; major capsid protein, Cytomegalovirus ; Ribonuclease P (EC 3.1.26.5)
Language	English
Publishing date	2019-02-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1241540-6
ISSN	1469-9001 ; 1355-8382
ISSN (online)	1469-9001
ISSN	1355-8382
DOI	10.1261/rna.069682.118
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Article ; Online: Atomic structures and deletion mutant reveal different capsid-binding patterns and functional significance of tegument protein pp150 in murine and human cytomegaloviruses with implications for therapeutic development.

Liu, Wei / Dai, Xinghong / Jih, Jonathan / Chan, Karen / Trang, Phong / Yu, Xuekui / Balogun, Rilwan / Mei, Ye / Liu, Fenyong / Zhou, Z Hong

PLoS pathogens

2019 Volume 15, Issue 2, Page(s) e1007615

Abstract: Cytomegalovirus (CMV) infection causes birth defects and life-threatening complications in immunosuppressed patients. Lack of vaccine and need for more effective drugs have driven widespread ongoing therapeutic development efforts against human CMV (HCMV) ...

Abstract	Cytomegalovirus (CMV) infection causes birth defects and life-threatening complications in immunosuppressed patients. Lack of vaccine and need for more effective drugs have driven widespread ongoing therapeutic development efforts against human CMV (HCMV), mostly using murine CMV (MCMV) as the model system for preclinical animal tests. The recent publication (Yu et al., 2017, DOI: 10.1126/science.aam6892) of an atomic model for HCMV capsid with associated tegument protein pp150 has infused impetus for rational design of novel vaccines and drugs, but the absence of high-resolution structural data on MCMV remains a significant knowledge gap in such development efforts. Here, by cryoEM with sub-particle reconstruction method, we have obtained the first atomic structure of MCMV capsid with associated pp150. Surprisingly, the capsid-binding patterns of pp150 differ between HCMV and MCMV despite their highly similar capsid structures. In MCMV, pp150 is absent on triplex Tc and exists as a "Λ"-shaped dimer on other triplexes, leading to only 260 groups of two pp150 subunits per capsid in contrast to 320 groups of three pp150 subunits each in a "Δ"-shaped fortifying configuration. Many more amino acids contribute to pp150-pp150 interactions in MCMV than in HCMV, making MCMV pp150 dimer inflexible thus incompatible to instigate triplex Tc-binding as observed in HCMV. While pp150 is essential in HCMV, our pp150-deletion mutant of MCMV remained viable though with attenuated infectivity and exhibiting defects in retaining viral genome. These results thus invalidate targeting pp150, but lend support to targeting capsid proteins, when using MCMV as a model for HCMV pathogenesis and therapeutic studies.
MeSH term(s)	Animals ; Capsid ; Capsid Proteins/metabolism ; Capsid Proteins/ultrastructure ; Cryoelectron Microscopy/methods ; Cytomegalovirus/genetics ; Cytomegalovirus/metabolism ; Cytomegalovirus/pathogenicity ; Cytomegalovirus Infections/metabolism ; Genome, Viral/genetics ; Humans ; Mice ; Muromegalovirus/metabolism ; Muromegalovirus/pathogenicity ; Phosphoproteins/metabolism ; Phosphoproteins/physiology ; Phosphoproteins/ultrastructure ; Sequence Deletion/genetics ; Viral Matrix Proteins/metabolism ; Viral Matrix Proteins/physiology ; Viral Matrix Proteins/ultrastructure ; Virion ; Virus Assembly
Chemical Substances	Capsid Proteins ; Phosphoproteins ; Viral Matrix Proteins ; pp150 protein, Cytomegalovirus
Language	English
Publishing date	2019-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1007615
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Article: RNase P ribozyme as an antiviral agent against human cytomegalovirus.

Trang, Phong / Liu, Fenyong

Methods in molecular biology (Clifton, N.J.)

2004 Volume 252, Page(s) 437–450

Abstract: Human cytomegalovirus (HCMV) represents one of the most medically important human viruses and causes a wide spectrum of human diseases, including birth defects and mental retardation in newborns, common opportunistic infections in acquired ... ...

Abstract	Human cytomegalovirus (HCMV) represents one of the most medically important human viruses and causes a wide spectrum of human diseases, including birth defects and mental retardation in newborns, common opportunistic infections in acquired immunodeficiency syndrome (AIDS) patients (e.g., CMV-associated retinitis and pneumonia), and possibly cardiovascular diseases such as atherosclerosis. This chapter describes the utilization of RNase P ribozyme-specifically, M1GS ribozyme, as a gene-targeting agent for blocking HCMV gene expression and growth. The target for the RNase P ribozyme is the overlapping region of the mRNAs that code for HCMV major transcription factors IE1 and IE2, which are essential for viral gene expression and replication. The methods described in this chapter focus primarily on i) construction of the retroviral vector for expression of M1GS ribozymes in cultured cells, ii) generation of stable cell lines expressing ribozymes, iii) determination of the expression of M1GS RNAs in human cells, and iv) evaluation of the efficacy of ribozymes in inhibiting HCMV IE1/IE2 expression and viral growth. Using these methods, we successfully constructed M1GS RNAs against the IE1/IE2 mRNA sequence and recently showed that a reduction of up to 150- to 3000-fold in HCMV growth is found in cells that express the ribozymes.
MeSH term(s)	Acquired Immunodeficiency Syndrome/drug therapy ; Antiviral Agents/pharmacology ; Base Sequence ; Blotting, Northern/methods ; Cytomegalovirus/drug effects ; Cytomegalovirus/growth & development ; DNA Primers ; Gene Targeting/methods ; Genetic Diseases, Inborn/drug therapy ; Genetic Diseases, Inborn/genetics ; HIV-1/drug effects ; Humans ; Infant, Newborn ; Molecular Sequence Data ; Polymerase Chain Reaction ; Promoter Regions, Genetic ; Ribonuclease P/genetics ; Ribonuclease P/pharmacology
Chemical Substances	Antiviral Agents ; DNA Primers ; Ribonuclease P (EC 3.1.26.5)
Language	English
Publishing date	2004
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1385/1-59259-746-7:437
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Article: Ribonuclease P-mediated inhibition of human cytomegalovirus gene expression and replication induced by engineered external guide sequences

Jiang, Xiaohong / Chen, Yuan-Chuan / Gong, Hao / Trang, Phong / Lu, Sangwei / Liu, Fenyong

RNA biology. 2012 Sept. 1, v. 9, no. 9

2012

Abstract: External guide sequences (EGSs) are RNA molecules that can bind to a target mRNA and direct ribonuclease P (RNase P), a tRNA processing enzyme, for specific cleavage of the target mRNA. Using an in vitro selection procedure, we have previously generated ... ...

Abstract	External guide sequences (EGSs) are RNA molecules that can bind to a target mRNA and direct ribonuclease P (RNase P), a tRNA processing enzyme, for specific cleavage of the target mRNA. Using an in vitro selection procedure, we have previously generated EGS variants that efficiently direct human RNase P to cleave a target mRNA in vitro. In this study, we constructed EGSs from a variant to target the overlapping region of the mRNAs coding for human cytomegalovirus (HCMV) capsid scaffolding protein (CSP) and assemblin, which are essential for viral capsid formation. The EGS variant was about 40-fold more active in directing human RNase P to cleave the mRNA in vitro than the EGS derived from a natural tRNA. Moreover, a reduction of about 98% and 75% in CSP/assemblin gene expression and a reduction of 7000- and 250-fold in viral growth were observed in HCMV-infected cells that expressed the variant and the tRNA-derived EGS, respectively. Our study shows that the EGS variant is more effective in blocking HCMV gene expression and growth than the tRNA-derived EGS. Moreover, these results demonstrate the utility of highly active EGS RNA variants in gene targeting applications including anti-HCMV therapy.
Keywords	Human betaherpesvirus 5 ; capsid ; gene expression ; genes ; humans ; ribonucleases ; therapeutics ; viral growth
Language	English
Dates of publication	2012-0901
Size	p. 1186-1195.
Publishing place	Taylor & Francis
Document type	Article
ISSN	1555-8584
DOI	10.4161/rna.21724
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Engineered RNase P Ribozymes Effectively Inhibit the Infection of Murine Cytomegalovirus in Animals.

Li, Wei / Liu, Yujun / Wang, Yuanyuan / Li, Ruilin / Trang, Phong / Tang, Wei / Yang, Zhu / Wang, Yu / Sun, Xu / Xing, Xiwen / Lu, Sangwei / Liu, Fenyong

Theranostics

2018 Volume 8, Issue 20, Page(s) 5634–5644

Abstract: Rationales: ...

Abstract	Rationales:
MeSH term(s)	Animals ; Cytomegalovirus/genetics ; Genetic Therapy/methods ; Mice ; Muromegalovirus/drug effects ; Muromegalovirus/pathogenicity ; RNA, Antisense/genetics ; RNA, Catalytic/genetics ; RNA, Messenger/genetics ; Ribonuclease P/metabolism
Chemical Substances	RNA, Antisense ; RNA, Catalytic ; RNA, Messenger ; Ribonuclease P (EC 3.1.26.5)
Language	English
Publishing date	2018-11-09
Publishing country	Australia
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2592097-2
ISSN	1838-7640 ; 1838-7640
ISSN (online)	1838-7640
ISSN	1838-7640
DOI	10.7150/thno.27776
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Article ; Online: Human cytomegalovirus reprogrammes haematopoietic progenitor cells into immunosuppressive monocytes to achieve latency.

Zhu, Dihan / Pan, Chaoyun / Sheng, Jingxue / Liang, Hongwei / Bian, Zhen / Liu, Yuan / Trang, Phong / Wu, Jianguo / Liu, Fenyong / Zhang, Chen-Yu / Zen, Ke

Nature microbiology

2018 Volume 3, Issue 4, Page(s) 503–513

Abstract: The precise cell type hosting latent human cytomegalovirus (HCMV) remains elusive. Here, we report that HCMV reprogrammes human haematopoietic progenitor cells (HPCs) into a unique monocyte subset to achieve latency. Unlike conventional monocytes, this ... ...

Abstract	The precise cell type hosting latent human cytomegalovirus (HCMV) remains elusive. Here, we report that HCMV reprogrammes human haematopoietic progenitor cells (HPCs) into a unique monocyte subset to achieve latency. Unlike conventional monocytes, this monocyte subset possesses higher levels of B7-H4, IL-10 and inducible nitric oxide synthase (iNOS), a longer lifespan and strong immunosuppressive capacity. Cell sorting of peripheral blood from latently infected human donors confirms that only this monocyte subset, representing less than 0.1% of peripheral mononuclear cells, is HCMV genome-positive but immediate-early-negative. Mechanistic studies demonstrate that HCMV promotes the differentiation of HPCs into this monocyte subset by activating cellular signal transducer and activator of transcription 3 (STAT3). In turn, this monocyte subset generates a high level of nitric oxide (NO) to silence HCMV immediate-early transcription and promote viral latency. By contrast, the US28-knockout HCMV mutant, which is incapable of activating STAT3, fails to reprogramme the HPCs and achieve latency. Our findings reveal that via activating the STAT3-iNOS-NO axis, HCMV differentiates human HPCs into a longevous, immunosuppressive monocyte subset for viral latency.
MeSH term(s)	Cell Differentiation/physiology ; Cellular Reprogramming/genetics ; Cytomegalovirus/genetics ; Cytomegalovirus/immunology ; Cytomegalovirus/pathogenicity ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/virology ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Humans ; Immune Tolerance/genetics ; Immune Tolerance/immunology ; Interleukin-10/metabolism ; Monocytes/virology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type II/metabolism ; STAT3 Transcription Factor/metabolism ; V-Set Domain-Containing T-Cell Activation Inhibitor 1/metabolism ; Virus Latency/genetics ; Virus Latency/immunology
Chemical Substances	IL10 protein, human ; STAT3 Transcription Factor ; STAT3 protein, human ; V-Set Domain-Containing T-Cell Activation Inhibitor 1 ; VTCN1 protein, human ; Interleukin-10 (130068-27-8) ; Nitric Oxide (31C4KY9ESH) ; NOS2 protein, human (EC 1.14.13.39) ; Nitric Oxide Synthase Type II (EC 1.14.13.39)
Language	English
Publishing date	2018-03-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2058-5276
ISSN (online)	2058-5276
DOI	10.1038/s41564-018-0131-9
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Article ; Online: RNase P Ribozymes Inhibit the Replication of Human Cytomegalovirus by Targeting Essential Viral Capsid Proteins.

Yang, Zhu / Reeves, Michael / Ye, Jun / Trang, Phong / Zhu, Li / Sheng, Jingxue / Wang, Yu / Zen, Ke / Wu, Jianguo / Liu, Fenyong

Viruses

2015 Volume 7, Issue 7, Page(s) 3345–3360

Abstract: An engineered RNase P-based ribozyme variant, which was generated using the in vitro selection procedure, was used to target the overlapping mRNA region of two proteins essential for human cytomegalovirus (HCMV) replication: capsid assembly protein (AP) ... ...

Abstract	An engineered RNase P-based ribozyme variant, which was generated using the in vitro selection procedure, was used to target the overlapping mRNA region of two proteins essential for human cytomegalovirus (HCMV) replication: capsid assembly protein (AP) and protease (PR). In vitro studies showed that the generated variant, V718-A, cleaved the target AP mRNA sequence efficiently and its activity was about 60-fold higher than that of wild type ribozyme M1-A. Furthermore, we observed a reduction of 98%-99% in AP/PR expression and an inhibition of 50,000 fold in viral growth in cells with V718-A, while a 75% reduction in AP/PR expression and a 500-fold inhibition in viral growth was found in cells with M1-A. Examination of the antiviral effects of the generated ribozyme on the HCMV replication cycle suggested that viral DNA encapsidation was inhibited and as a consequence, viral capsid assembly was blocked when the expression of AP and PR was inhibited by the ribozyme. Thus, our study indicates that the generated ribozyme variant is highly effective in inhibiting HCMV gene expression and blocking viral replication, and suggests that engineered RNase P ribozyme can be potentially developed as a promising gene-targeting agent for anti-HCMV therapy.
MeSH term(s)	Capsid Proteins/antagonists & inhibitors ; Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Cytomegalovirus/genetics ; Cytomegalovirus/physiology ; Cytomegalovirus Infections/genetics ; Cytomegalovirus Infections/therapy ; Cytomegalovirus Infections/virology ; Gene Expression Regulation, Viral ; Humans ; RNA, Catalytic/genetics ; RNA, Catalytic/metabolism ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; Virus Replication
Chemical Substances	Capsid Proteins ; RNA, Catalytic ; Ribonuclease P (EC 3.1.26.5)
Language	English
Publishing date	2015-06-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v7072775
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