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  1. Article ; Online: Deletion of gene OV132 attenuates Orf virus more effectively than gene OV112

    Yamada, Yumiko / Chuang, Shih-Te / Tseng, Ching-Yu / Liao, Guan-Ru / Liu, Shin-Wu / Tseng, Yeu-Yang / Lin, Fong-Yuan / Xu, Weili

    Appl Microbiol Biotechnol. 2023 Feb., v. 107, no. 2-3 p.835-851

    2023  

    Abstract: Orf virus (ORFV), a Parapoxvirus in Poxviridae, infects sheep and goats resulting in contagious pustular dermatitis. ORFV is regarded as a promising viral vector candidate for vaccine development and oncolytic virotherapy. Owing to their potential ... ...

    Abstract Orf virus (ORFV), a Parapoxvirus in Poxviridae, infects sheep and goats resulting in contagious pustular dermatitis. ORFV is regarded as a promising viral vector candidate for vaccine development and oncolytic virotherapy. Owing to their potential clinical application, safety concerns have become increasingly important. Deletion of either the OV132 (encoding vascular endothelial growth factor, VEGF) or OV112 (encoding the chemokine binding protein, CBP) genes reduced ORFV infectivity, which has been independently demonstrated in the NZ2 and NZ7 strains, respectively. This study revealed that the VEGF and CBP gene sequences of the local strain (TW/Hoping) shared a similarity of 47.01% with NZ2 and 90.56% with NZ7. Due to the high sequence divergence of these two immunoregulatory genes among orf viral strains, their contribution to the pathogenicity of Taiwanese ORFV isolates was comparatively characterized. Initially, two ORFV recombinants were generated, in which either the VEGF or CBP gene was deleted and replaced with the reporter gene EGFP. In vitro assays indicated that both the VEGF-deletion mutant ORFV-VEGFΔ-EGFP and the CBP deletion mutant ORFV-CBPΔ-EGFP were attenuated in cells. In particular, ORFV-VEGFΔ-EGFP significantly reduced plaque size and virus yield compared to ORFV-CBPΔ-EGFP and the wild-type control. Similarly, in vivo analysis revealed no virus yield in the goat skin biopsy infected by ORFV-VEGFΔ-EGFP, and significantly reduced the virus yield of ORFV-CBPΔ-EGFP relative to the wild-type control. These results confirmed the loss of virulence of both deletion mutants in the Hoping strain, whereas the VEGF-deletion mutant was more attenuated than the CBP deletion strain in both cell and goat models. KEY POINTS: • VEGF and CBP genes are crucial in ORFV pathogenesis in the TW/Hoping strain • The VEGF-deletion mutant virus was severely attenuated in both cell culture and animal models • Deletion mutant viruses are advantageous vectors for the development of vaccines and therapeutic regimens
    Keywords Orf virus ; biopsy ; cell culture ; chemokines ; contagious ecthyma ; goats ; immunomodulation ; mutants ; pathogenesis ; reporter genes ; sheep ; vaccine development ; vascular endothelial growth factors ; virulence ; viruses
    Language English
    Dates of publication 2023-02
    Size p. 835-851.
    Publishing place Springer Berlin Heidelberg
    Document type Article ; Online
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-022-12323-0
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    In stock of ZB MED Bonn / Germany

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  2. Article ; Online: Deletion of gene OV132 attenuates Orf virus more effectively than gene OV112.

    Yamada, Yumiko / Chuang, Shih-Te / Tseng, Ching-Yu / Liao, Guan-Ru / Liu, Shin-Wu / Tseng, Yeu-Yang / Lin, Fong-Yuan / Hsu, Wei-Li

    Applied microbiology and biotechnology

    2022  Volume 107, Issue 2-3, Page(s) 835–851

    Abstract: Orf virus (ORFV), a Parapoxvirus in Poxviridae, infects sheep and goats resulting in contagious pustular dermatitis. ORFV is regarded as a promising viral vector candidate for vaccine development and oncolytic virotherapy. Owing to their potential ... ...

    Abstract Orf virus (ORFV), a Parapoxvirus in Poxviridae, infects sheep and goats resulting in contagious pustular dermatitis. ORFV is regarded as a promising viral vector candidate for vaccine development and oncolytic virotherapy. Owing to their potential clinical application, safety concerns have become increasingly important. Deletion of either the OV132 (encoding vascular endothelial growth factor, VEGF) or OV112 (encoding the chemokine binding protein, CBP) genes reduced ORFV infectivity, which has been independently demonstrated in the NZ2 and NZ7 strains, respectively. This study revealed that the VEGF and CBP gene sequences of the local strain (TW/Hoping) shared a similarity of 47.01% with NZ2 and 90.56% with NZ7. Due to the high sequence divergence of these two immunoregulatory genes among orf viral strains, their contribution to the pathogenicity of Taiwanese ORFV isolates was comparatively characterized. Initially, two ORFV recombinants were generated, in which either the VEGF or CBP gene was deleted and replaced with the reporter gene EGFP. In vitro assays indicated that both the VEGF-deletion mutant ORFV-VEGFΔ-EGFP and the CBP deletion mutant ORFV-CBPΔ-EGFP were attenuated in cells. In particular, ORFV-VEGFΔ-EGFP significantly reduced plaque size and virus yield compared to ORFV-CBPΔ-EGFP and the wild-type control. Similarly, in vivo analysis revealed no virus yield in the goat skin biopsy infected by ORFV-VEGFΔ-EGFP, and significantly reduced the virus yield of ORFV-CBPΔ-EGFP relative to the wild-type control. These results confirmed the loss of virulence of both deletion mutants in the Hoping strain, whereas the VEGF-deletion mutant was more attenuated than the CBP deletion strain in both cell and goat models. KEY POINTS: • VEGF and CBP genes are crucial in ORFV pathogenesis in the TW/Hoping strain • The VEGF-deletion mutant virus was severely attenuated in both cell culture and animal models • Deletion mutant viruses are advantageous vectors for the development of vaccines and therapeutic regimens.
    MeSH term(s) Animals ; Ecthyma, Contagious/pathology ; Goats ; Orf virus/genetics ; Sheep ; Skin ; Vascular Endothelial Growth Factor A/genetics ; Genes, Viral
    Chemical Substances Vascular Endothelial Growth Factor A
    Language English
    Publishing date 2022-12-09
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-022-12323-0
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2229: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Epidemiology of Severe Fever with Thrombocytopenia Syndrome in Dogs and Cats in Taiwan.

    Kuan, Chih-Ying / Ou, Shan-Chia / Chang, Chao-Chin / Kao, Pei-Ling / Tsai, Ruei-Sheng / Rattanapanadda, Porjai / Lin, Tsai-Lu / Maeda, Ken / Cheng, Tsun-Li / Lee, Ya-Jane / Chuang, Shih-Te / Lin, Shiun-Long / Liu, Hsien-Yueh / Lin, Fong-Yuan / Lin, Jen-Wei / Hsu, Wei-Li / Chou, Chi-Chung

    Viruses

    2023  Volume 15, Issue 12

    Abstract: Severe Fever with Thrombocytopenia Syndrome (SFTS), caused by the SFTS Virus (SFTSV), is a global health threat. SFTSV in Taiwan has only been reported in ruminants and wild animals. Thus, we aimed to investigate the infection statuses of dogs and cats, ... ...

    Abstract Severe Fever with Thrombocytopenia Syndrome (SFTS), caused by the SFTS Virus (SFTSV), is a global health threat. SFTSV in Taiwan has only been reported in ruminants and wild animals. Thus, we aimed to investigate the infection statuses of dogs and cats, the animals with closer human interactions. Overall, the SFTSV RNA prevalence was 23% (170/735), with dogs showing a 25.9% (111/429) prevalence and cats at 19.3% (59/306) prevalence. Noticeably, the prevalence in stray animals (39.8% 77/193) was significantly higher than in domesticated ones (17.2%, 93/542). Among the four categories analyzed, the highest SFTSV prevalence was found in the stray dogs at 53.9% (120/193), significantly higher than the 24.2% prevalence noted in stray cats. In contrast, domesticated animals exhibited similar prevalence rates, with 17.1% for dogs and 17.2% for cats. It is noteworthy that in the domesticated animal groups, a significantly elevated prevalence (45%, 9/20) was observed among cats exhibiting thrombocytopenia compared to those platelet counts in the reference range (4.8%, 1/21). The high infection rate in stray animals, especially stray dogs, indicated that exposure to various outdoor environments influences the prevalence of infections. Given the higher human interaction with dogs and cats, there is a need for proactive measures to reduce the risk associated with the infection of SFTSV in both animals and humans.
    MeSH term(s) Animals ; Cats ; Humans ; Dogs ; Severe Fever with Thrombocytopenia Syndrome/epidemiology ; Severe Fever with Thrombocytopenia Syndrome/veterinary ; Bunyaviridae Infections/epidemiology ; Bunyaviridae Infections/veterinary ; Taiwan/epidemiology ; Cat Diseases/epidemiology ; Dog Diseases/epidemiology ; Phlebovirus/genetics ; Animals, Wild ; Animals, Domestic
    Language English
    Publishing date 2023-11-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v15122338
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: The pseudorabies virus vhs protein cleaves RNA containing an IRES sequence

    Liu, Ya‐Fen / Tsai, Pei‐Yun / Chulakasian, Songkhla / Lin, Fong‐Yuan / Hsu, Wei‐Li

    FEBS journal. 2016 Mar., v. 283, no. 5

    2016  

    Abstract: The virion host shutoff protein (vhs), encoded by the gene UL41, has RNase activity and is the key regulator of the early host shutoff response induced by type 1 herpes simplex virus. Despite low amino acid similarity, the vhs protein of the swine ... ...

    Abstract The virion host shutoff protein (vhs), encoded by the gene UL41, has RNase activity and is the key regulator of the early host shutoff response induced by type 1 herpes simplex virus. Despite low amino acid similarity, the vhs protein of the swine herpesvirus, pseudorabies virus (PrV), also exhibits RNase activity. However, the mechanism underlying the action of vhs remains undefined. Here, we report that the RNA degradation profile of PrV vhs is similar, but not identical, to that of type 1 herpes simplex virus vhs. Notably, the presence of a cap structure enhances both the degradation rate and the preferential targeting of the vhs protein towards the 3′‐end of the encephalomyocarditis virus internal ribosome entry site (IRES). Furthermore, type 1 herpes simplex virus vhs produces a simple degradation pattern, but PrV vhs gives rise to multiple intermediates. The results of northern blotting using probes recognizing various regions of the RNA substrate found that PrV vhs also cleaves downstream of the IRES region and this vhs protein overall shows 5′ to 3′ RNase activity. Moreover, addition of the translation initiation factors eIF4H and eIF4B significantly increased the RNase activity of recombinant PrV vhs against capped RNA. Nonetheless, these proteins did not fully reconstitute the IRES‐directed targeting pattern observed for vhs translated in a rabbit reticular lysate system. The interaction between PrV vhs and eIF4H/eIF4B implies that the translation initiation machinery within the cell is able to stimulate the nuclease activity of PrV vhs. However, this process remains inefficient in terms of the IRES‐targeting pattern.
    Keywords Encephalomyocarditis virus ; Human herpesvirus 1 ; Northern blotting ; RNA ; Suid herpesvirus 1 ; amino acids ; genes ; proteins ; rabbits ; ribonucleases ; ribosomes ; swine ; translation (genetics) ; virion
    Language English
    Dates of publication 2016-03
    Size p. 899-911.
    Publishing place Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
    Document type Article
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.13642
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    In stock of ZB MED Bonn / Germany

    Z 2006/704: Show issues

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  5. Article ; Online: Adenosine Deaminase Acting on RNA 1 Associates with Orf Virus OV20.0 and Enhances Viral Replication.

    Liao, Guan-Ru / Tseng, Yeu-Yang / Tseng, Ching-Yu / Lin, Fong-Yuan / Yamada, Yumiko / Liu, Hao-Ping / Kuan, Chih-Ying / Hsu, Wei-Li

    Journal of virology

    2019  Volume 93, Issue 7

    Abstract: Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by targeting the double-stranded RNA (dsRNA)-activated protein kinase (PKR) by multiple mechanisms. ... ...

    Abstract Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by targeting the double-stranded RNA (dsRNA)-activated protein kinase (PKR) by multiple mechanisms. These mechanisms include a direct interaction with PKR and binding with two PKR activators, dsRNA and the cellular PKR activator (PACT), which ultimately leads to the inhibition of PKR activation. In the present study, we identified a novel association between OV20.0 and adenosine deaminase acting on RNA 1 (ADAR1). OV20.0 bound directly to the dsRNA binding domains (RBDs) of ADAR1 in the absence of dsRNA. Additionally, OV20.0 preferentially interacted with RBD1 of ADAR1, which was essential for its dsRNA binding ability and for the homodimerization that is critical for intact adenosine-to-inosine (A-to-I)-editing activity. Finally, the association with OV20.0 suppressed the A-to-I-editing ability of ADAR1, while ADAR1 played a proviral role during ORFV infection by inhibiting PKR phosphorylation. These observations revealed a new strategy used by OV20.0 to evade antiviral responses via PKR.
    MeSH term(s) A549 Cells ; Adenosine/genetics ; Adenosine Deaminase/genetics ; Animals ; Cell Line ; Cell Line, Tumor ; Ecthyma, Contagious/genetics ; GTPase-Activating Proteins/genetics ; HEK293 Cells ; Humans ; Immunity, Innate/genetics ; Inosine/genetics ; Orf virus/genetics ; Phosphorylation/genetics ; RNA Editing/genetics ; RNA, Double-Stranded/genetics ; RNA, Viral/genetics ; RNA-Binding Proteins/genetics ; Sheep ; Viral Proteins/genetics ; Virus Replication/genetics
    Chemical Substances GTPase-Activating Proteins ; OV20.0L protein, Orf virus ; RNA, Double-Stranded ; RNA, Viral ; RNA-Binding Proteins ; Viral Proteins ; Inosine (5A614L51CT) ; ADAR protein, human (EC 3.5.4.37) ; Adenosine Deaminase (EC 3.5.4.4) ; Adenosine (K72T3FS567)
    Language English
    Publishing date 2019-03-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01912-18
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: The pseudorabies virus vhs protein cleaves RNA containing an IRES sequence.

    Liu, Ya-Fen / Tsai, Pei-Yun / Chulakasian, Songkhla / Lin, Fong-Yuan / Hsu, Wei-Li

    The FEBS journal

    2016  Volume 283, Issue 5, Page(s) 899–911

    Abstract: The virion host shutoff protein (vhs), encoded by the gene UL41, has RNase activity and is the key regulator of the early host shutoff response induced by type 1 herpes simplex virus. Despite low amino acid similarity, the vhs protein of the swine ... ...

    Abstract The virion host shutoff protein (vhs), encoded by the gene UL41, has RNase activity and is the key regulator of the early host shutoff response induced by type 1 herpes simplex virus. Despite low amino acid similarity, the vhs protein of the swine herpesvirus, pseudorabies virus (PrV), also exhibits RNase activity. However, the mechanism underlying the action of vhs remains undefined. Here, we report that the RNA degradation profile of PrV vhs is similar, but not identical, to that of type 1 herpes simplex virus vhs. Notably, the presence of a cap structure enhances both the degradation rate and the preferential targeting of the vhs protein towards the 3'-end of the encephalomyocarditis virus internal ribosome entry site (IRES). Furthermore, type 1 herpes simplex virus vhs produces a simple degradation pattern, but PrV vhs gives rise to multiple intermediates. The results of northern blotting using probes recognizing various regions of the RNA substrate found that PrV vhs also cleaves downstream of the IRES region and this vhs protein overall shows 5' to 3' RNase activity. Moreover, addition of the translation initiation factors eIF4H and eIF4B significantly increased the RNase activity of recombinant PrV vhs against capped RNA. Nonetheless, these proteins did not fully reconstitute the IRES-directed targeting pattern observed for vhs translated in a rabbit reticular lysate system. The interaction between PrV vhs and eIF4H/eIF4B implies that the translation initiation machinery within the cell is able to stimulate the nuclease activity of PrV vhs. However, this process remains inefficient in terms of the IRES-targeting pattern.
    MeSH term(s) Animals ; Base Sequence ; Eukaryotic Initiation Factors/metabolism ; Gene Deletion ; HEK293 Cells ; Herpesvirus 1, Suid/chemistry ; Humans ; Internal Ribosome Entry Sites ; Molecular Sequence Data ; Protein Biosynthesis ; RNA, Viral/chemistry ; Rabbits ; Recombinant Proteins/chemistry ; Ribonucleases/metabolism ; Transcription, Genetic ; Viral Proteins/metabolism ; Virion/chemistry
    Chemical Substances EIF4H protein, human ; Eukaryotic Initiation Factors ; Internal Ribosome Entry Sites ; RNA, Viral ; Recombinant Proteins ; Viral Proteins ; eIF-4B ; virion host shutoff protein, Simplexvirus (118367-50-3) ; Ribonucleases (EC 3.1.-)
    Language English
    Publishing date 2016-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.13642
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Regulation of PACT-Mediated Protein Kinase Activation by the OV20.0 Protein of Orf Virus.

    Tseng, Yeu-Yang / Liao, Guan-Ru / Sen, Ganes C / Lin, Fong-Yuan / Hsu, Wei-Li

    Journal of virology

    2015  Volume 89, Issue 22, Page(s) 11619–11629

    Abstract: Double-stranded RNA (dsRNA)-activated protein kinase (PKR), a major component of the cellular antiviral system, is activated by the binding of either dsRNA or the cellular PKR activator, the PACT protein. The suppression of PKR activation is one of the ... ...

    Abstract Double-stranded RNA (dsRNA)-activated protein kinase (PKR), a major component of the cellular antiviral system, is activated by the binding of either dsRNA or the cellular PKR activator, the PACT protein. The suppression of PKR activation is one of the main strategies that viruses employ to circumvent interferon signaling. Orf virus (ORFV), a parapoxvirus from the Poxviridae family, causes contagious pustular dermatitis in small ruminants. Previous studies have demonstrated that various OV20.0 isoforms, encoded by the OV20.0L gene, are able to inhibit PKR activation both by sequestering dsRNA and by physically interacting with PKR in vitro. Thus, this gene acts as a virulence factor of ORFV when tested using a mouse infection model. In the present study, the regions within OV20.0 that interact with dsRNA and with PKR have been mapped. Furthermore, this study demonstrates for the first time that OV20.0 is also able to interact with the dsRNA binding domain of PACT and that the presence of dsRNA strengthened the interaction of these two molecules. The presence of OV20.0 diminishes PKR phosphorylation when this is stimulated by PACT. Nevertheless, the association of OV20.0 with PKR, rather than with PACT, was found to be essential for reducing PACT-mediated PKR phosphorylation. These observations elucidate a new strategy whereby innate immunity can be evaded by ORFV.IMPORTANCE Our previous study indicated that ORFV's two OV20.0 isoforms act as a PKR antagonist via sequestering the PKR activator, dsRNA, and by interacting with PKR, leading to an inhibition of PKR activation (Y. Y. Tseng, F. Y. Lin, S. F. Cheng, D. Tscharke, S. Chulakasian, C. C. Chou, Y. F. Liu, W. S. Chang, M. L. Wong, and W. L. Hsu, J Virol 89:4966-4979, 2015, doi:10.1128/JVI.03714-14). In the current study, the possible mechanisms by which OV20.0 protein counteracts PKR activation were studied in depth. OV20.0 is able to bind PKR and its two activators, dsRNA and PACT. In addition, OV20.0 binds directly to the RNA binding domains (RBDs) of PKR, and this interaction does not require dsRNA. Moreover, OV20.0 interacts with or occupies the RBD2 and the kinase domain of PKR, which then prevents PACT binding to PKR. Finally, OV20.0 associates with PACT via the RBDs, which may reduce the ability of PACT to induce PKR activation. The findings in this study provide new concepts in relation to how ORFV modulates PKR activation.
    MeSH term(s) Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; Enzyme Activation/genetics ; Fibroblasts/virology ; Gene Expression Regulation, Viral/genetics ; Goats ; HEK293 Cells ; Humans ; Immune Evasion/genetics ; Immunity, Innate/immunology ; Molecular Sequence Data ; Orf virus/genetics ; Orf virus/immunology ; Orf virus/pathogenicity ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; RNA, Double-Stranded/metabolism ; RNA-Binding Proteins/metabolism ; Sequence Alignment ; Sequence Analysis, RNA ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virulence Factors/genetics ; eIF-2 Kinase/metabolism
    Chemical Substances OV20.0L protein, Orf virus ; PRKRA protein, human ; RNA, Double-Stranded ; RNA-Binding Proteins ; Viral Proteins ; Virulence Factors ; eIF-2 Kinase (EC 2.7.11.1)
    Language English
    Publishing date 2015-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01739-15
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  8. Article ; Online: The interplay of reovirus with autophagy.

    Chiu, Hung-Chuan / Richart, Sarah / Lin, Fong-Yuan / Hsu, Wei-Li / Liu, Hung-Jen

    BioMed research international

    2014  Volume 2014, Page(s) 483657

    Abstract: Autophagy participates in multiple fundamental physiological processes, including survival, differentiation, development, and cellular homeostasis. It eliminates cytoplasmic protein aggregates and damaged organelles by triggering a series of events: ... ...

    Abstract Autophagy participates in multiple fundamental physiological processes, including survival, differentiation, development, and cellular homeostasis. It eliminates cytoplasmic protein aggregates and damaged organelles by triggering a series of events: sequestering the protein substrates into double-membrane vesicles, fusing the vesicles with lysosomes, and then degrading the autophagic contents. This degradation pathway is also involved in various disorders, for instance, cancers and infectious diseases. This paper provides an overview of modulation of autophagy in the course of reovirus infection and also the interplay of autophagy and reovirus.
    MeSH term(s) Autophagy/genetics ; Humans ; Lysosomes/metabolism ; Lysosomes/virology ; Protein Aggregation, Pathological ; Reoviridae/genetics ; Reoviridae/pathogenicity ; Reoviridae Infections/genetics ; Reoviridae Infections/metabolism
    Language English
    Publishing date 2014-03-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2698540-8
    ISSN 2314-6141 ; 2314-6133
    ISSN (online) 2314-6141
    ISSN 2314-6133
    DOI 10.1155/2014/483657
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Roles of nucleic acid substrates and cofactors in the vhs protein activity of pseudorabies virus.

    Liu, Ya-Fen / Tsai, Pei-Yun / Lin, Fong-Yuan / Lin, Kuan-Hsun / Chang, Tien-Jye / Lin, Hui-Wen / Chulakasian, Songkhla / Hsu, Wei-Li

    Veterinary research

    2015  Volume 46, Page(s) 141

    Abstract: Pseudorabies virus (PrV) belongs to the α-herpesvirinae of which human simplex virus (HSV) is the prototype virus. One of the hallmarks of HSV infection is shutoff of protein synthesis that is mediated by various viral proteins including vhs (virion host ...

    Abstract Pseudorabies virus (PrV) belongs to the α-herpesvirinae of which human simplex virus (HSV) is the prototype virus. One of the hallmarks of HSV infection is shutoff of protein synthesis that is mediated by various viral proteins including vhs (virion host shutoff), which is encoded by the UL41 gene. However, the function of PrV vhs is poorly understood. Due to the low sequence similarity (39.3%) between the HSV and PrV UL41 proteins, vhs might not share the same biochemistry characteristics. The purpose of this study was to characterize the nuclease activity of the PrV vhs protein with respect to substrate specificity, its requirements in terms of cofactors, and the protein regions, as well as key amino acids, which contribute to vhs activity. Our results indicated that, similar to HSV vhs, PrV vhs is able to degrade ssRNA and mRNA. However, PrV vhs also targeted rRNA for degradation, which is novel compared to the HSV-1 vhs. Activity assays indicated that Mg(2+) alone enhances RNA degradation mediated by PrV vhs, while K(+) and ATP are not sufficient to induce activity. Finally, we demonstrated that each of the four highly conserved functional boxes of PrV vhs contributes to RNA degradation and that, in particular, residues 152, 169, 171, 172, 173 343, 345, 352 and 356, which are conserved among α-herpesviruses, are key amino acids needed for PrV vhs ribonuclease activity.
    MeSH term(s) Animals ; HEK293 Cells ; Herpesvirus 1, Suid/genetics ; Herpesvirus 1, Suid/metabolism ; Humans ; Pseudorabies/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Ribosomal/genetics ; RNA, Ribosomal/metabolism ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances RNA, Messenger ; RNA, Ribosomal ; RNA, Small Interfering ; Viral Proteins
    Language English
    Publishing date 2015-12-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1146298-x
    ISSN 1297-9716 ; 0928-4249
    ISSN (online) 1297-9716
    ISSN 0928-4249
    DOI 10.1186/s13567-015-0284-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: The different molecular forms of urine neutrophil gelatinase-associated lipocalin present in dogs with urinary diseases.

    Hsu, Wei-Li / Chiou, Hsiao-Chi / Tung, Kwong-Chung / Belot, Guillaume / Virilli, Anais / Wong, Min-Liang / Lin, Fong-Yuan / Lee, Ya-Jane

    BMC veterinary research

    2014  Volume 10, Page(s) 202

    Abstract: Background: Neutrophil gelatinase-associated lipocalin (NGAL) is a useful biomarker for the early prediction of renal diseases. NGAL may exist as monomer, dimer and/or NGAL/MMP-9 complex forms in humans. In this study, the existence of various forms of ... ...

    Abstract Background: Neutrophil gelatinase-associated lipocalin (NGAL) is a useful biomarker for the early prediction of renal diseases. NGAL may exist as monomer, dimer and/or NGAL/MMP-9 complex forms in humans. In this study, the existence of various forms of NGAL in urine (uNGAL) was determined and whether these forms are related to the different urinary diseases found in dogs is further discussed.
    Results: Eighty-one urine samples from dogs with different forms of renal disease (41), pyuria (19) and a number of non-renal related diseases (10), as well as healthy dogs (11), were collected. uNGAL concentrations and their molecular forms in dogs were measured by ELISA and Western blot analysis, respectively. The uNGAL concentrations of dogs with pyuria (median: 15.35 ng/mL) were significantly higher than those of the healthy control animals (median: 3.92 ng/mL) (p < 0.01), but lower than those of dogs with renal diseases (median: 23.77 ng/mL). Each NGAL molecular form could be detected in dog urine. In particular, monomer was detected more frequently in patients with renal disease than those with non-renal diseases; while the dimer form appeared in a significantly higher percentage of cases with pyuria compared to those without pyuria. The NGAL/MMP-9 complex was found to exist not only in the patients with cystitis, but also in the cases with renal injury.
    Conclusion: Different molecular forms of uNGAL can indicate different origins of the urinary abnormalities. Determining the molecular forms of uNGAL present in diseased dogs may provide clinical workers with a tool that will help the early and more precise detection of different urinary diseases.
    MeSH term(s) Acute-Phase Proteins/urine ; Animals ; Dog Diseases/metabolism ; Dog Diseases/urine ; Dogs ; Enzyme-Linked Immunosorbent Assay/veterinary ; Female ; Gene Expression Regulation/physiology ; Lipocalins/urine ; Mice ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Proto-Oncogene Proteins/urine ; Urologic Diseases/metabolism ; Urologic Diseases/veterinary
    Chemical Substances Acute-Phase Proteins ; Lipocalins ; Protein Isoforms ; Proto-Oncogene Proteins ; neutrophil gelatinase-associated lipocalin protein, dog
    Language English
    Publishing date 2014-08-27
    Publishing country England
    Document type Journal Article
    ISSN 1746-6148
    ISSN (online) 1746-6148
    DOI 10.1186/s12917-014-0202-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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