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Pesquisa : B04.280.210.950 [Categoria DeCS]
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  1 / 27 MEDLINE  
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[PMID]:28466296
[Au] Autor:Suryawanashi YR; Zhang T; Woyczesczyk HM; Christie J; Byers E; Kohler S; Eversole R; Mackenzie C; Essani K
[Ad] Endereço:Laboratory of Virology, Department of Biological Sciences, Western Michigan University, Kalamazoo, MI, 49008-5410, USA.
[Ti] Título:T-independent response mediated by oncolytic tanapoxvirus recombinants expressing interleukin-2 and monocyte chemoattractant protein-1 suppresses human triple negative breast tumors.
[So] Source:Med Oncol;34(6):112, 2017 Jun.
[Is] ISSN:1559-131X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human triple negative breast cancer (TNBC) is an aggressive disease, associated with a high rate of recurrence and metastasis. Current therapeutics for TNBC are limited, highly toxic and show inconsistent efficacy due to a high degree of intra-tumoral and inter-tumoral heterogeneity. Oncolytic viruses (OVs) are an emerging treatment option for cancers. Several OVs are currently under investigation in preclinical and clinical settings. Here, we examine the oncolytic potential of two tanapoxvirus (TPV) recombinants expressing mouse monocyte chemoattractant protein (mMCP)-1 [also known as mCCL2] and mouse interleukin (mIL)-2, in human TNBC, in vitro and in vivo. Both wild-type (wt) TPV and TPV recombinants demonstrated efficient replicability in human TNBC cells and killed cancer cell efficiently in a dose-dependent manner in vitro. TPV/∆66R/mCCL2 and TPV/∆66R/mIL-2 expressing mCCL2 and mIL-2, respectively, suppressed the growth of MDA-MB-231 tumor xenografts in nude mice significantly, as compared to the mock-injected tumors. Histological analysis of tumors showed areas of viable tumor cells, necrotic foci and immune cell accumulation in virus-treated tumors. Moreover, TPV/∆66R/mIL-2-treated tumors showed a deep infiltration of mononuclear immune cells into the tumor capsule and focal cell death in tumors. In conclusion, TPV recombinants expressing mCCL2 and mIL-2 showed a significant therapeutic effect in MDA-MB-231 tumor xenografts, in nude mice through induction of potent antitumor immune responses. Considering the oncolytic potency of armed oncolytic TPV recombinants expressing mCCL2 and mIL-2 in an experimental nude mouse model, these viruses merit further investigation as alternative treatment options for human breast cancer.
[Mh] Termos MeSH primário: Quimiocina CCL2/metabolismo
Imunoterapia/métodos
Interleucina-2/metabolismo
Vírus Oncolíticos/genética
Neoplasias de Mama Triplo Negativas/metabolismo
Yatapoxvirus/genética
[Mh] Termos MeSH secundário: Animais
Aotidae
Linhagem Celular
Quimiocina CCL2/genética
Quimiocina CCL2/imunologia
Seres Humanos
Interleucina-2/genética
Interleucina-2/imunologia
Masculino
Camundongos
Camundongos Nus
Vírus Oncolíticos/metabolismo
Neoplasias de Mama Triplo Negativas/genética
Neoplasias de Mama Triplo Negativas/imunologia
Ensaios Antitumorais Modelo de Xenoenxerto
Yatapoxvirus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokine CCL2); 0 (Interleukin-2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1007/s12032-017-0973-7


  2 / 27 MEDLINE  
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[PMID]:27738905
[Au] Autor:Zhang T; Suryawanshi YR; Kordish DH; Woyczesczyk HM; Jeng D; Essani K
[Ad] Endereço:Laboratory of Virology, Department of Biological Sciences, Western Michigan University, Kalamazoo, MI, 49008, USA.
[Ti] Título:Tanapoxvirus lacking a neuregulin-like gene regresses human melanoma tumors in nude mice.
[So] Source:Virus Genes;53(1):52-62, 2017 Feb.
[Is] ISSN:1572-994X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuregulin (NRG), an epidermal growth factor is known to promote the growth of various cell types, including human melanoma cells through ErbB family of tyrosine kinases receptors. Tanapoxvirus (TPV)-encoded protein TPV-15L, a functional mimic of NRG, also acts through ErbB receptors. Here, we show that the TPV-15L protein promotes melanoma proliferation. TPV recombinant generated by deleting the 15L gene (TPVΔ15L) showed replication ability similar to that of wild-type TPV (wtTPV) in owl monkey kidney cells, human lung fibroblast (WI-38) cells, and human melanoma (SK-MEL-3) cells. However, a TPV recombinant with both 15L and the thymidine kinase (TK) gene 66R ablated (TPVΔ15LΔ66R) replicated less efficiently compared to TPVΔ15L and the parental virus. TPVΔ15L exhibited more robust tumor regression in the melanoma-bearing nude mice compared to other TPV recombinants. Our results indicate that deletion of TPV-15L gene product which facilitates the growth of human melanoma cells can be an effective strategy to enhance the oncolytic potential of TPV for the treatment of melanoma.
[Mh] Termos MeSH primário: Melanoma/patologia
Neurregulinas/genética
Terapia Viral Oncolítica
Vírus Oncolíticos/genética
Deleção de Sequência
Proteínas Virais/genética
Yatapoxvirus/genética
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Linhagem Celular
Proliferação Celular
Modelos Animais de Doenças
Vetores Genéticos/genética
Seres Humanos
Masculino
Melanoma/metabolismo
Melanoma/terapia
Camundongos
Camundongos Nus
Terapia Viral Oncolítica/métodos
Carga Tumoral
Replicação Viral
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neuregulins); 0 (Viral Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161015
[St] Status:MEDLINE
[do] DOI:10.1007/s11262-016-1402-2


  3 / 27 MEDLINE  
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[PMID]:25887490
[Au] Autor:Conrad SJ; El-Aswad M; Kurban E; Jeng D; Tripp BC; Nutting C; Eversole R; Mackenzie C; Essani K
[Ad] Endereço:Laboratory of Virology, Department of Biological Sciences, Western Michigan University, Kalamazoo, MI, 49008, USA. steven.j.conrad@wmich.edu.
[Ti] Título:Oncolytic tanapoxvirus expressing FliC causes regression of human colorectal cancer xenografts in nude mice.
[So] Source:J Exp Clin Cancer Res;34:19, 2015 Feb 19.
[Is] ISSN:1756-9966
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Colorectal cancers are significant causes of morbidity and mortality and existing therapies often perform poorly for individuals afflicted with advanced disease. Oncolytic virotherapy is an emerging therapeutic modality with great promise for addressing this medical need. Herein we describe the in vivo testing of recombinant variants of the tanapoxvirus (TPV). Recombinant viruses were made ablated for either the 66R gene (encoding a thymidine kinase), the 2L gene (encoding a TNF-binding protein), or both. Some of the recombinants were armed to express mouse chemotactic protein 1 (mCCL2/mMCP-1), mouse granulocyte-monocyte colony stimulating factor (mGM-CSF), or bacterial flagellin (FliC). Tumors were induced in athymic nude mice by implantation of HCT 116 cells and subsequently treated by a single intratumoral injection of one of the recombinant TPVs. Histological examination showed a common neoplastic cell type and a range of immune cell infiltration, necrosis, and tumor cell organization. Significant regression was seen in tumors treated with virus TPV/Δ2L/Δ66R/fliC, and to a lesser extent the recombinants TPV/Δ2L and TPV/Δ66R. Our results suggest that oncolytic recombinants of the TPV armed with activators of the innate immune response may be effective virotherapeutic agents for colorectal cancers in humans and should be explored further to fully realize their potential.
[Mh] Termos MeSH primário: Neoplasias Colorretais/patologia
Flagelina/genética
Expressão Gênica
Vetores Genéticos/genética
Terapia Viral Oncolítica
Vírus Oncolíticos/genética
Yatapoxvirus/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Neoplasias Colorretais/terapia
Modelos Animais de Doenças
Terapia Genética
Vetores Genéticos/administração & dosagem
Seres Humanos
Masculino
Camundongos
Transdução Genética
Transgenes
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
12777-81-0 (Flagellin)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150419
[St] Status:MEDLINE
[do] DOI:10.1186/s13046-015-0131-z


  4 / 27 MEDLINE  
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[PMID]:25255815
[Au] Autor:Monroe BP; Nakazawa YJ; Reynolds MG; Carroll DS
[Ad] Endereço:Division of High-Consequence Pathogens and Pathology, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Mailstop A-30, Atlanta, GA 30333, USA. ihd2@cdc.gov.
[Ti] Título:Estimating the geographic distribution of human Tanapox and potential reservoirs using ecological niche modeling.
[So] Source:Int J Health Geogr;13:34, 2014 Sep 25.
[Is] ISSN:1476-072X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Tanapox virus is a zoonotic infection that causes mild febrile illness and one to several nodular skin lesions. The disease is endemic in parts of Africa. The principal reservoir for the virus that causes Tanapox is unknown, but has been hypothesized to be a non-human primate. This study employs ecological niche modeling (ENM) to determine areas of tropical Africa suitable for the occurrence of human Tanapox and a list of hypothetical reservoirs. The resultant niche model will be a useful tool to guide medical surveillance activities in the region. METHODS: This study uses the Desktop GARP software to predict regions where human Tanapox might be expected to occur based on historical human case locations and environmental data. Additional modeling of primate species, using occurrence data from museum records was performed to determine suitable disease reservoirs. RESULTS: The final ENM predicts a potential distribution of Tanapox over much of equatorial Africa, exceeding the borders of Kenya and Democratic Republic of Congo (DRC) where it has been historically reported. Five genera of non-human primates were found to be potential reservoir taxa. CONCLUSIONS: Validity testing suggests the model created here is robust (p < 0.04). Several genera of primates were identified as having ENMs overlapping with that of Tanapox and are suggested as potential reservoirs, mainly members of the Genus Cercopithecus. The ENM modeling technique has several limitations and results should be interpreted with caution. This study may increase knowledge and engage further research in this neglected disease.
[Mh] Termos MeSH primário: Reservatórios de Doenças/virologia
Ecossistema
Mapeamento Geográfico
Modelos Teóricos
Infecções por Poxviridae/epidemiologia
Infecções Tumorais por Vírus/epidemiologia
Yatapoxvirus/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
República Democrática do Congo/epidemiologia
Haplorrinos
Seres Humanos
Quênia/epidemiologia
Pan troglodytes
Papio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1504
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140927
[St] Status:MEDLINE
[do] DOI:10.1186/1476-072X-13-34


  5 / 27 MEDLINE  
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[PMID]:23269801
[Au] Autor:Jeng D; Ma Z; Barrett JW; McFadden G; Loeb JA; Essani K
[Ad] Endereço:Department of Biological Sciences, Western Michigan University, Kalamazoo, MI, USA.
[Ti] Título:The tanapoxvirus 15L protein is a virus-encoded neuregulin that promotes viral replication in human endothelial cells.
[So] Source:J Virol;87(6):3018-26, 2013 Mar.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Studies on large double-stranded DNA (dsDNA) viruses such as poxviruses have been helpful in identifying a number of viral and cellular growth factors that contribute to our broad understanding of virus-host interaction. Orthopoxviruses and leporipoxviruses are among the most studied viruses in this aspect. However, tanapoxvirus (TPV), a member of the genus Yatapoxvirus, still remains largely unexplored, as the only known hosts for this virus are humans and monkeys. Here, we describe the initial characterization of an epidermal growth factor (EGF)-like growth factor mimicking human neuregulin from TPV, expressed by the TPV-15L gene. Assays using a baculovirus-expressed and tagged TPV-15L protein demonstrated the ability to phosphorylate neuregulin receptors. Neuregulins represent a large family of EGF-like growth factors that play important roles in embryonic endocardium development, Schwann and oligodendrocyte survival and differentiation, localized acetylcholine receptor expression at the neuromuscular junction, and epithelial morphogenesis. Interestingly, certain neuregulin molecules are able to target specific tissues through interactions with heparin sulfate proteoglycans via an immunoglobulin (Ig)-like domain. Analyses of TPV-15L revealed no Ig-like domain, but it retains the ability to bind heparin and phosphorylate neuregulin receptors, providing compelling evidence that TPV-15L is a functional mimetic of neuregulin. TPV-15L knockout virus experiments demonstrate that the virus replicates in human umbilical vein endothelial cells less efficiently than wild-type TPV-Kenya, indicating that this is a nonessential protein for virus viability but can serve a stimulatory role for replication in some cultured cells. However, the precise role of this protein in host-virus interaction still remains to be deduced.
[Mh] Termos MeSH primário: Células Endoteliais/virologia
Neurregulinas/metabolismo
Proteínas Virais/metabolismo
Fatores de Virulência/metabolismo
Replicação Viral
Yatapoxvirus/patogenicidade
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Técnicas de Inativação de Genes
Seres Humanos
Dados de Sequência Molecular
Neurregulinas/genética
Alinhamento de Sequência
Proteínas Virais/genética
Fatores de Virulência/genética
Yatapoxvirus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Neuregulins); 0 (Viral Proteins); 0 (Virulence Factors)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121228
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.02112-12


  6 / 27 MEDLINE  
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[PMID]:22927815
[Au] Autor:Krumm B; Meng X; Wang Z; Xiang Y; Deng J
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma, United States of America.
[Ti] Título:A unique bivalent binding and inhibition mechanism by the yatapoxvirus interleukin 18 binding protein.
[So] Source:PLoS Pathog;8(8):e1002876, 2012.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interleukin 18 (IL18) is a cytokine that plays an important role in inflammation as well as host defense against microbes. Mammals encode a soluble inhibitor of IL18 termed IL18 binding protein (IL18BP) that modulates IL18 activity through a negative feedback mechanism. Many poxviruses encode homologous IL18BPs, which contribute to virulence. Previous structural and functional studies on IL18 and IL18BPs revealed an essential binding hot spot involving a lysine on IL18 and two aromatic residues on IL18BPs. The aromatic residues are conserved among the very diverse mammalian and poxviruses IL18BPs with the notable exception of yatapoxvirus IL18BPs, which lack a critical phenylalanine residue. To understand the mechanism by which yatapoxvirus IL18BPs neutralize IL18, we solved the crystal structure of the Yaba-Like Disease Virus (YLDV) IL18BP and IL18 complex at 1.75 Šresolution. YLDV-IL18BP forms a disulfide bonded homo-dimer engaging IL18 in a 2∶2 stoichiometry, in contrast to the 1∶1 complex of ectromelia virus (ECTV) IL18BP and IL18. Disruption of the dimer interface resulted in a functional monomer, however with a 3-fold decrease in binding affinity. The overall architecture of the YLDV-IL18BP:IL18 complex is similar to that observed in the ECTV-IL18BP:IL18 complex, despite lacking the critical lysine-phenylalanine interaction. Through structural and mutagenesis studies, contact residues that are unique to the YLDV-IL18BP:IL18 binding interface were identified, including Q67, P116 of YLDV-IL18BP and Y1, S105 and D110 of IL18. Overall, our studies show that YLDV-IL18BP is unique among the diverse family of mammalian and poxvirus IL-18BPs in that it uses a bivalent binding mode and a unique set of interacting residues for binding IL18. However, despite this extensive divergence, YLDV-IL18BP binds to the same surface of IL18 used by other IL18BPs, suggesting that all IL18BPs use a conserved inhibitory mechanism by blocking a putative receptor-binding site on IL18.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intercelular/química
Interleucina-18/química
Multimerização Proteica
Proteínas Virais/química
Yatapoxvirus/química
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Linhagem Celular
Cristalografia por Raios X
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/genética
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Interleucina-18/genética
Interleucina-18/metabolismo
Mutagênese
Mutação de Sentido Incorreto
Infecções por Poxviridae/genética
Infecções por Poxviridae/metabolismo
Estrutura Quaternária de Proteína
Estrutura Terciária de Proteína
Proteínas Virais/genética
Proteínas Virais/metabolismo
Yatapoxvirus/genética
Yatapoxvirus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intercellular Signaling Peptides and Proteins); 0 (Interleukin-18); 0 (Viral Proteins); 0 (interleukin-18 binding protein)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120829
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1002876


  7 / 27 MEDLINE  
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[PMID]:21529335
[Au] Autor:Jeng D; Rahman MM; McFadden G; Essani K
[Ad] Endereço:Department of Molecular Genetics and Microbiology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
[Ti] Título:Tumor necrosis factor inhibitors from poxviruses with an emphasis on tanapoxvirus-2L protein.
[So] Source:Recent Pat DNA Gene Seq;5(2):97-103, 2011 Aug.
[Is] ISSN:2212-3431
[Cp] País de publicação:United Arab Emirates
[La] Idioma:eng
[Ab] Resumo:Viruses have evolved strategies to counteract host defenses. Some tactics employ viral proteins to neutralize host immune effector proteins such as cytokines, chemokines and their receptors, which help coordinate the host responses against the virus. Tumor necrosis factor (TNF) is one of the crucial pro-inflammatory/anti-viral cytokines involved in inflammatory and autoimmune diseases. Poxvirus anti-immune proteins represent some of the most complex and efficient mechanisms of regulating TNF and its pathological effects. These proteins have considerable potential for treating TNF-related diseases. Here we discuss two major classes of poxvirus-TNF inhibitors focusing on the tanapoxvirus (TPV)-2L protein, previously called TPV-gp38. TPV-2L has been shown to interact and biologically neutralize human (h)TNF, and has been indirectly associated with the inhibition of other cytokines (hIFN-γ, hIL-2 and hIL-5). The TPV-2L protein alone has been expressed, purified and shown to bind with high affinity to hTNF, but lacked binding to the other cytokines. Further studies identified sequential binding of hß2-microglobulin and hα2-macroglobulin to TPV-2L. The ability of a single viral protein to form multi-protein complexes suggests that TPV might also possess other novel strategies of evading the immune system. Reviewed here are patented poxvirus TNF-binding proteins and their genes to evaluate their potential therapeutic value.
[Mh] Termos MeSH primário: Poxviridae/metabolismo
Fator de Necrose Tumoral alfa/antagonistas & inibidores
Proteínas Virais/química
[Mh] Termos MeSH secundário: Seres Humanos
Evasão da Resposta Imune
Complexos Multiproteicos/imunologia
Complexos Multiproteicos/metabolismo
Poxviridae/imunologia
Ligação Proteica
Fator de Necrose Tumoral alfa/metabolismo
Proteínas Virais/imunologia
Proteínas Virais/metabolismo
Yatapoxvirus/imunologia
Yatapoxvirus/metabolismo
alfa-Macroglobulinas/metabolismo
Microglobulina-2 beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Multiprotein Complexes); 0 (Tumor Necrosis Factor-alpha); 0 (Viral Proteins); 0 (alpha-Macroglobulins); 0 (beta 2-Microglobulin)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:110718
[Lr] Data última revisão:
110718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110503
[St] Status:MEDLINE


  8 / 27 MEDLINE  
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[PMID]:20937275
[Au] Autor:Lee EH; Seo YJ; Ahn HC; Kang YM; Kim HE; Lee YM; Choi BS; Lee JH
[Ad] Endereço:Department of Chemistry, Gyeongsang National University, Jinju, Gyengnam, Republic of Korea.
[Ti] Título:NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L.
[So] Source:FEBS Lett;584(21):4453-7, 2010 Nov 05.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZα(E3L)) bound to Z-DNA revealed that the overall structure of yabZα(E3L) and its interaction with Z-DNA are very similar to those of hZα(ADAR1). Here we have performed NMR hydrogen exchange experiments on the complexes between yabZα(E3L) and d(CGCGCG)(2) with a variety of protein-to-DNA molar ratios. This study revealed that yabZα(E3L) could efficiently change the B-form helix of the d(CGCGCG)(2) to left-handed Z-DNA via the active-mono B-Z transition pathway like hZα(ADAR1).
[Mh] Termos MeSH primário: DNA/química
Hidrogênio
Espectroscopia de Ressonância Magnética/métodos
Conformação de Ácido Nucleico
Proteínas Virais/química
Proteínas Virais/metabolismo
Yatapoxvirus
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
DNA/genética
DNA/metabolismo
Seres Humanos
Camundongos
Modelos Moleculares
Dados de Sequência Molecular
Estrutura Terciária de Proteína
Prótons
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protons); 0 (Viral Proteins); 7YNJ3PO35Z (Hydrogen); 9007-49-2 (DNA)
[Em] Mês de entrada:1011
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101013
[St] Status:MEDLINE
[do] DOI:10.1016/j.febslet.2010.10.003


  9 / 27 MEDLINE  
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[PMID]:19232662
[Au] Autor:Rahman MM; Jeng D; Singh R; Coughlin J; Essani K; McFadden G
[Ad] Endereço:Department of Molecular Genetics and Microbiology, College of Medicine, University of Florida, 1600 SW Archer Road, Gainesville, FL 32610, USA.
[Ti] Título:Interaction of human TNF and beta2-microglobulin with Tanapox virus-encoded TNF inhibitor, TPV-2L.
[So] Source:Virology;386(2):462-8, 2009 Apr 10.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tanapox virus (TPV) encodes and expresses a secreted TNF-binding protein, TPV-2L or gp38, that displays inhibitory properties against TNF from diverse mammalian species, including human, monkey, canine and rabbit. TPV-2L also has sequence similarity with the MHC-class I heavy chain and interacts differently with human TNF as compared to the known cellular TNF receptors or any of the known virus-encoded TNF receptor homologs derived from many poxviruses. In order to determine the TNF binding region in TPV-2L, various TPV-2L C-terminal truncations and internal deletions were created and the muteins were expressed using recombinant baculovirus vectors. C-terminal deletions from TPV-2L resulted in reduced binding affinity for human TNF and specific mutants of TNF that discriminate between TNF-R1 and TNF-R2. However, deletion of C-terminal 42 amino acid residues totally abolished the binding of human TNF and its mutants. Removal of any of the predicted internal domains resulted in a mutant TPV-2L protein incapable of binding to human TNF. Deletion of C-terminal residues also affected the ability of TPV-2L to block TNF-induced cellular cytotoxicity. In addition to TNF, TPV-2L can also form complexes with human beta2-microglobulin to form a novel macromolecular complex. In summary, the TPV-2L protein is a bona fide MHC-1 heavy chain family member that binds and inhibits human TNF in a fashion very distinct from other known poxvirus-encoded TNF inhibitors, and also can form a novel complex with the human MHC-1 light chain, beta2-microglobulin.
[Mh] Termos MeSH primário: Fator de Necrose Tumoral alfa/metabolismo
Proteínas Virais/metabolismo
Yatapoxvirus/metabolismo
Microglobulina-2 beta/metabolismo
[Mh] Termos MeSH secundário: Animais
Baculoviridae/genética
Sítios de Ligação
Linhagem Celular
Seres Humanos
Camundongos
Ligação Proteica
Receptores do Fator de Necrose Tumoral/metabolismo
Deleção de Sequência
Proteínas Virais/genética
Yatapoxvirus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Receptors, Tumor Necrosis Factor); 0 (TNF protein, human); 0 (Tumor Necrosis Factor-alpha); 0 (Viral Proteins); 0 (beta 2-Microglobulin)
[Em] Mês de entrada:0904
[Cu] Atualização por classe:090330
[Lr] Data última revisão:
090330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090224
[St] Status:MEDLINE
[do] DOI:10.1016/j.virol.2009.01.026


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[PMID]:18971273
[Au] Autor:Bartee E; Mohamed MR; Lopez MC; Baker HV; McFadden G
[Ad] Endereço:Department of Molecular Genetics and Microbiology, College of Medicine, University of Florida, Gainesville, Florida 32610, USA.
[Ti] Título:The addition of tumor necrosis factor plus beta interferon induces a novel synergistic antiviral state against poxviruses in primary human fibroblasts.
[So] Source:J Virol;83(2):498-511, 2009 Jan.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumor necrosis factor (TNF) and members of the interferon (IFN) family have been shown to independently inhibit the replication of a variety of viruses. In addition, previous reports have shown that treatment with various combinations of these antiviral cytokines induces a synergistic antiviral state that can be significantly more potent than addition of any of these cytokines alone. The mechanism of this cytokine synergy and its effects on global gene expression, however, are not well characterized. Here, we use DNA microarray analysis to demonstrate that treatment of uninfected primary human fibroblasts with TNF plus IFN-beta induces a distinct synergistic state characterized by significant perturbations of several hundred genes which are coinduced by the individual cytokines alone, as well as the induction of more than 850 novel host cell genes. This synergy is mediated directly by the two ligands, not by intermediate secreted factors, and is necessary and sufficient to completely block the productive replication and spread of myxoma virus in human fibroblasts. In contrast, the replication of two other poxviruses, vaccinia virus and tanapox virus, are only partially inhibited in these cells by the synergistic antiviral state, whereas the spread of both of these viruses to neighboring cells was efficiently blocked. Taken together, our data indicate that the combination of TNF and IFN-beta induces a novel synergistic antiviral state that is highly distinct from that induced by either cytokine alone.
[Mh] Termos MeSH primário: Fibroblastos/imunologia
Fibroblastos/virologia
Fatores Imunológicos/imunologia
Interferon beta/imunologia
Myxoma virus/imunologia
Fator de Necrose Tumoral alfa/imunologia
[Mh] Termos MeSH secundário: Células Cultivadas
Sinergismo Farmacológico
Perfilação da Expressão Gênica
Seres Humanos
Fatores Imunológicos/farmacologia
Interferon beta/farmacologia
Myxoma virus/fisiologia
Análise de Sequência com Séries de Oligonucleotídeos
Fator de Necrose Tumoral alfa/farmacologia
Vírus Vaccinia/imunologia
Ensaio de Placa Viral
Replicação Viral/imunologia
Yatapoxvirus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunologic Factors); 0 (Tumor Necrosis Factor-alpha); 77238-31-4 (Interferon-beta)
[Em] Mês de entrada:0901
[Cu] Atualização por classe:140902
[Lr] Data última revisão:
140902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:081031
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.01376-08



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