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  1 / 374 MEDLINE  
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[PMID]:28695289
[Au] Autor:Silver ZA; Watkins DI
[Ad] Endereço:Medical Scientist Training Program, University of Miami Miller School of Medicine, Miami, FL, USA. zas11@med.miami.edu.
[Ti] Título:The role of MHC class I gene products in SIV infection of macaques.
[So] Source:Immunogenetics;69(8-9):511-519, 2017 Aug.
[Is] ISSN:1432-1211
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human immunodeficiency virus (HIV) remains among the most significant public health threats worldwide. Despite three decades of research following the discovery of HIV, a preventive vaccine remains elusive. The study of HIV elite controllers has been crucial to elaborate the genetic and immunologic determinants that underlie control of HIV replication. Coordinated studies of elite control in humans have, however, been limited by variability among infecting viral strains, host genotype, and the uncertainty of the timing and route of infection. In this review, we discuss the role of nonhuman primate (NHP) models for the elucidation of the immunologic correlates that underlie control of AIDS virus replication. We discuss the importance of major histocompatibility complex class I (MHC-I) alleles in activating CD8+ T-cell populations that promote control of both HIV and simian immunodeficiency virus (SIV) replication. Provocatively, we make the argument that T-cell subsets recognizing the HIV/SIV viral infectivity factor (Vif) protein may be crucial for control of viral replication. We hope that this review demonstrates how an in-depth understanding of the MHC-I gene products associated with elite control of HIV/SIV, and the epitopes that they present, can provide researchers with a glimpse into the protective immune responses that underlie AIDS nonprogression.
[Mh] Termos MeSH primário: Genes MHC Classe I/fisiologia
Macaca
Síndrome de Imunodeficiência Adquirida dos Símios/genética
[Mh] Termos MeSH secundário: Animais
Epitopos
Produtos do Gene vif/imunologia
Seres Humanos
Vacinas contra a SAIDS/imunologia
Síndrome de Imunodeficiência Adquirida dos Símios/imunologia
Linfócitos T/imunologia
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Epitopes); 0 (Gene Products, vif); 0 (SAIDS Vaccines)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1007/s00251-017-0997-3


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[PMID]:28516844
[Au] Autor:Ai Y; Ma J; Wang X
[Ad] Endereço:†â€‹Present address: National Institute of Biological Sciences, Beijing, PR China. 1​College of Wildlife Resources, Northeast Forestry University, Hexing Road, Harbin 150040, PR China.
[Ti] Título:Clues for two-step virion infectivity factor regulation by core binding factor beta.
[So] Source:J Gen Virol;98(5):1113-1121, 2017 May.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lentiviruses threaten human and animal health. Virion infectivity factor (Vif) is essential for the infectivity of most lentiviruses, except for the equine infectious anaemia virus (EIAV). Vif promotes viral infectivity by recruiting a Cullin-based E3 ligase to induce the degradation of a class of host restriction factors, named APOBEC3. Core binding factor beta (CBF-ß) is necessary for several primate lentiviral Vif functions, including HIV-1 Vif. Although much progress has been made in understanding the contribution of CBF-ß to Vif function, the precise mechanism has not yet been fully elucidated. In this study, we found that an interaction with CBF-ß altered the oligomerization and subcellular distribution pattern and increased the stability of two primate lentiviral Vifs, HIV-1 Vif and Macaca simian immunodeficiency virus (SIVmac) Vif. Moreover, using a CBF-ß loss-of-function mutant, we demonstrated that the interaction between CBF-ß and Vif was not sufficient for Vif assistance; a region including F68 in CBF-ß was also required for the stability and function of Vif. For the first time, this study separates the binding and regulating processes of CBF-ß when it is promoting Vif function, which further extends our understanding of the biochemical regulation of Vif by CBF-ß.
[Mh] Termos MeSH primário: Subunidade beta de Fator de Ligação ao Core/metabolismo
Produtos do Gene vif/metabolismo
HIV-1/fisiologia
Interações Hospedeiro-Patógeno
Vírus da Imunodeficiência Símia/fisiologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Subunidade beta de Fator de Ligação ao Core/genética
Análise Mutacional de DNA
Técnicas de Inativação de Genes
Seres Humanos
Macaca
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Core Binding Factor beta Subunit); 0 (Gene Products, vif)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000749


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[PMID]:28331087
[Au] Autor:Yoshikawa R; Takeuchi JS; Yamada E; Nakano Y; Misawa N; Kimura Y; Ren F; Miyazawa T; Koyanagi Y; Sato K
[Ad] Endereço:Laboratory of Viral Pathogenesis, Institute for Virus Research, Kyoto University, Kyoto, Japan.
[Ti] Título:Feline Immunodeficiency Virus Evolutionarily Acquires Two Proteins, Vif and Protease, Capable of Antagonizing Feline APOBEC3.
[So] Source:J Virol;91(11), 2017 Jun 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interplay between viral and host proteins has been well studied to elucidate virus-host interactions and their relevance to virulence. Mammalian genes encode apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3) proteins, which act as intrinsic restriction factors against lentiviruses. To overcome APOBEC3-mediated antiviral actions, lentiviruses have evolutionarily acquired an accessory protein, viral infectivity factor (Vif), and Vif degrades host APOBEC3 proteins via a ubiquitin/proteasome-dependent pathway. Although the Vif-APOBEC3 interaction and its evolutionary significance, particularly those of primate lentiviruses (including HIV) and primates (including humans), have been well investigated, those of nonprimate lentiviruses and nonprimates are poorly understood. Moreover, the factors that determine lentiviral pathogenicity remain unclear. Here, we focus on feline immunodeficiency virus (FIV), a pathogenic lentivirus in domestic cats, and the interaction between FIV Vif and feline APOBEC3 in terms of viral virulence and evolution. We reveal the significantly reduced diversity of FIV subtype B compared to that of other subtypes, which may associate with the low pathogenicity of this subtype. We also demonstrate that FIV subtype B Vif is less active with regard to feline APOBEC3 degradation. More intriguingly, we further reveal that FIV protease cleaves feline APOBEC3 in released virions. Taken together, our findings provide evidence that a lentivirus encodes two types of anti-APOBEC3 factors, Vif and viral protease. During the history of mammalian evolution, mammals coevolved with retroviruses, including lentiviruses. All pathogenic lentiviruses, excluding equine infectious anemia virus, have acquired the gene via evolution to combat APOBEC3 proteins, which are intrinsic restriction factors against exogenous lentiviruses. Here we demonstrate that FIV, a pathogenic lentivirus in domestic cats, antagonizes feline APOBEC3 proteins by both Vif and a viral protease. Furthermore, the Vif proteins of an FIV subtype (subtype B) have attenuated their anti-APOBEC3 activity through evolution. Our findings can be a clue to elucidate the complicated evolutionary processes by which lentiviruses adapt to mammals.
[Mh] Termos MeSH primário: Desaminases APOBEC/antagonistas & inibidores
Ácido Aspártico Endopeptidases/metabolismo
Produtos do Gene vif/metabolismo
Vírus da Imunodeficiência Felina/genética
[Mh] Termos MeSH secundário: Desaminases APOBEC/metabolismo
Animais
Ácido Aspártico Endopeptidases/genética
Gatos
Evolução Molecular
Produtos do Gene vif/genética
Interações Hospedeiro-Patógeno
Vírus da Imunodeficiência Felina/metabolismo
Vírus da Imunodeficiência Felina/patogenicidade
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, vif); EC 3.4.23.- (Aspartic Acid Endopeptidases); EC 3.4.23.- (FIV protease); EC 3.5.4.5 (APOBEC Deaminases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


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[PMID]:27630243
[Au] Autor:Gu Q; Zhang Z; Cano Ortiz L; Franco AC; Häussinger D; Münk C
[Ad] Endereço:Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
[Ti] Título:Feline Immunodeficiency Virus Vif N-Terminal Residues Selectively Counteract Feline APOBEC3s.
[So] Source:J Virol;90(23):10545-10557, 2016 Dec 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Feline immunodeficiency virus (FIV) Vif protein counteracts feline APOBEC3s (FcaA3s) restriction factors by inducing their proteasomal degradation. The functional domains in FIV Vif for interaction with FcaA3s are poorly understood. Here, we have identified several motifs in FIV Vif that are important for selective degradation of different FcaA3s. Cats (Felis catus) express three types of A3s: single-domain A3Z2, single-domain A3Z3, and double-domain A3Z2Z3. We proposed that FIV Vif would selectively interact with the Z2 and the Z3 A3s. Indeed, we identified two N-terminal Vif motifs (12LF13 and 18GG19) that specifically interacted with the FcaA3Z2 protein but not with A3Z3. In contrast, the exclusive degradation of FcaA3Z3 was regulated by a region of three residues (M24, L25, and I27). Only a FIV Vif carrying a combination of mutations from both interaction sites lost the capacity to degrade and counteract FcaA3Z2Z3. However, alterations in the specific A3s interaction sites did not affect the cellular localization of the FIV Vif protein and binding to feline A3s. Pulldown experiments demonstrated that the A3 binding region localized to FIV Vif residues 50 to 80, outside the specific A3 interaction domain. Finally, we found that the Vif sites specific to individual A3s are conserved in several FIV lineages of domestic cat and nondomestic cats, while being absent in the FIV Vif of pumas. Our data support a complex model of multiple Vif-A3 interactions in which the specific region for selective A3 counteraction is discrete from a general A3 binding domain. IMPORTANCE: Both human immunodeficiency virus (HIV) and feline immunodeficiency virus (FIV) Vif proteins counteract their host's APOBEC3 restriction factors. However, these two Vif proteins have limited sequence homology. The molecular interaction between FIV Vif and feline APOBEC3s are not well understood. Here, we identified N-terminal FIV Vif sites that regulate the selective interaction of Vif with either feline APOBEC3Z2 or APOBEC3Z3. These specific Vif sites are conserved in several FIV lineages of domestic cat and nondomestic cats, while being absent in FIV Vif from puma. Our findings provide important insights for future experiments describing the FIV Vif interaction with feline APOBEC3s and also indicate that the conserved feline APOBEC3s interaction sites of FIV Vif allow FIV transmissions in Felidae.
[Mh] Termos MeSH primário: Citidina Desaminase/metabolismo
Produtos do Gene vif/metabolismo
Vírus da Imunodeficiência Felina/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Gatos/virologia
Linhagem Celular
Citidina Desaminase/química
Citidina Desaminase/genética
Produtos do Gene vif/química
Produtos do Gene vif/genética
Genes Virais
Células HEK293
Interações Hospedeiro-Patógeno
Seres Humanos
Vírus da Imunodeficiência Felina/classificação
Vírus da Imunodeficiência Felina/genética
Leões/virologia
Mutação
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteólise
Homologia de Sequência de Aminoácidos
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, vif); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE


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[PMID]:27581978
[Au] Autor:Zhang Z; Gu Q; Jaguva Vasudevan AA; Jeyaraj M; Schmidt S; Zielonka J; Perkovic M; Heckel JO; Cichutek K; Häussinger D; Smits SH; Münk C
[Ad] Endereço:Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
[Ti] Título:Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C.
[So] Source:J Virol;90(22):10193-10208, 2016 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lentiviruses have evolved the Vif protein to counteract APOBEC3 (A3) restriction factors by targeting them for proteasomal degradation. Previous studies have identified important residues in the interface of human immunodeficiency virus type 1 (HIV-1) Vif and human APOBEC3C (hA3C) or human APOBEC3F (hA3F). However, the interaction between primate A3C proteins and HIV-1 Vif or natural HIV-1 Vif variants is still poorly understood. Here, we report that HIV-1 Vif is inactive against A3Cs of rhesus macaques (rhA3C), sooty mangabey monkeys (smmA3C), and African green monkeys (agmA3C), while HIV-2, African green monkey simian immunodeficiency virus (SIVagm), and SIVmac Vif proteins efficiently mediate the depletion of all tested A3Cs. We identified that residues N/H130 and Q133 in rhA3C and smmA3C are determinants for this HIV-1 Vif-triggered counteraction. We also found that the HIV-1 Vif interaction sites in helix 4 of hA3C and hA3F differ. Vif alleles from diverse HIV-1 subtypes were tested for degradation activities related to hA3C. The subtype F-1 Vif was identified to be inactive for degradation of hA3C and hA3F. The residues that determined F-1 Vif inactivity in the degradation of A3C/A3F were located in the C-terminal region (K167 and D182). Structural analysis of F-1 Vif revealed that impairing the internal salt bridge of E171-K167 restored reduction capacities to A3C/A3F. Furthermore, we found that D101 could also form an internal interaction with K167. Replacing D101 with glycine and R167 with lysine in NL4-3 Vif impaired its counteractivity to A3F and A3C. This finding indicates that internal interactions outside the A3 binding region in HIV-1 Vif influence the capacity to induce degradation of A3C/A3F. IMPORTANCE: The APOBEC3 restriction factors can serve as potential barriers to lentiviral cross-species transmissions. Vif proteins from lentiviruses counteract APOBEC3 by proteasomal degradation. In this study, we found that monkey-derived A3C, rhA3C and smmA3C, were resistant to HIV-1 Vif. This was determined by A3C residues N/H130 and Q133. However, HIV-2, SIVagm, and SIVmac Vif proteins were found to be able to mediate the depletion of all tested primate A3C proteins. In addition, we identified a natural HIV-1 Vif (F-1 Vif) that was inactive in the degradation of hA3C/hA3F. Here, we provide for the first time a model that explains how an internal salt bridge of E171-K167-D101 influences Vif-mediated degradation of hA3C/hA3F. This finding provides a novel way to develop HIV-1 inhibitors by targeting the internal interactions of the Vif protein.
[Mh] Termos MeSH primário: Citidina Desaminase/metabolismo
Produtos do Gene vif/metabolismo
HIV-1/metabolismo
Vírus da Imunodeficiência Símia/metabolismo
Produtos do Gene vif do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Linhagem Celular
Células HEK293
Infecções por HIV/virologia
HIV-2/metabolismo
Seres Humanos
Lentivirus/metabolismo
Macaca mulatta
Ligação Proteica/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, vif); 0 (vif Gene Products, Human Immunodeficiency Virus); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE


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[PMID]:27368163
[Au] Autor:Zhang Z; Gu Q; Jaguva Vasudevan AA; Hain A; Kloke BP; Hasheminasab S; Mulnaes D; Sato K; Cichutek K; Häussinger D; Bravo IG; Smits SH; Gohlke H; Münk C
[Ad] Endereço:Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-University Düsseldorf, Building 23.12.U1.82, Moorenstr. 5, 40225, Düsseldorf, Germany.
[Ti] Título:Determinants of FIV and HIV Vif sensitivity of feline APOBEC3 restriction factors.
[So] Source:Retrovirology;13(1):46, 2016 Jul 01.
[Is] ISSN:1742-4690
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Feline immunodeficiency virus (FIV) is a global pathogen of Felidae species and a model system for Human immunodeficiency virus (HIV)-induced AIDS. In felids such as the domestic cat (Felis catus), APOBEC3 (A3) genes encode for single-domain A3Z2s, A3Z3 and double-domain A3Z2Z3 anti-viral cytidine deaminases. The feline A3Z2Z3 is expressed following read-through transcription and alternative splicing, introducing a previously untranslated exon in frame, encoding a domain insertion called linker. Only A3Z3 and A3Z2Z3 inhibit Vif-deficient FIV. Feline A3s also are restriction factors for HIV and Simian immunodeficiency viruses (SIV). Surprisingly, HIV-2/SIV Vifs can counteract feline A3Z2Z3. RESULTS: To identify residues in feline A3s that Vifs need for interaction and degradation, chimeric human-feline A3s were tested. Here we describe the molecular direct interaction of feline A3s with Vif proteins from cat FIV and present the first structural A3 model locating these interaction regions. In the Z3 domain we have identified residues involved in binding of FIV Vif, and their mutation blocked Vif-induced A3Z3 degradation. We further identified additional essential residues for FIV Vif interaction in the A3Z2 domain, allowing the generation of FIV Vif resistant A3Z2Z3. Mutated feline A3s also showed resistance to the Vif of a lion-specific FIV, indicating an evolutionary conserved Vif-A3 binding. Comparative modelling of feline A3Z2Z3 suggests that the residues interacting with FIV Vif have, unlike Vif-interacting residues in human A3s, a unique location at the domain interface of Z2 and Z3 and that the linker forms a homeobox-like domain protruding of the Z2Z3 core. HIV-2/SIV Vifs efficiently degrade feline A3Z2Z3 by possible targeting the linker stretch connecting both Z-domains. CONCLUSIONS: Here we identified in feline A3s residues important for binding of FIV Vif and a unique protein domain insertion (linker). To understand Vif evolution, a structural model of the feline A3 was developed. Our results show that HIV Vif binds human A3s differently than FIV Vif feline A3s. The linker insertion is suggested to form a homeo-box domain, which is unique to A3s of cats and related species, and not found in human and mouse A3s. Together, these findings indicate a specific and different A3 evolution in cats and human.
[Mh] Termos MeSH primário: Citidina Desaminase/química
Citidina Desaminase/metabolismo
Produtos do Gene vif/metabolismo
HIV-1/metabolismo
Vírus da Imunodeficiência Felina/metabolismo
[Mh] Termos MeSH secundário: Animais
Gatos
Linhagem Celular
Citidina Desaminase/genética
Evolução Molecular
Produtos do Gene vif/genética
Genes Homeobox
HIV-1/genética
Seres Humanos
Vírus da Imunodeficiência Felina/genética
Modelos Moleculares
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, vif); 0 (Recombinant Fusion Proteins); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160703
[St] Status:MEDLINE
[do] DOI:10.1186/s12977-016-0274-9


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[PMID]:27193350
[Au] Autor:Yoshikawa R; Izumi T; Nakano Y; Yamada E; Moriwaki M; Misawa N; Ren F; Kobayashi T; Koyanagi Y; Sato K
[Ad] Endereço:Laboratory of Viral Pathogenesis, Institute for Virus Research, Kyoto University, Kyoto 6068507.
[Ti] Título:Small ruminant lentiviral Vif proteins commonly utilize cyclophilin A, an evolutionarily and structurally conserved protein, to degrade ovine and caprine APOBEC3 proteins.
[So] Source:Microbiol Immunol;60(6):427-36, 2016 Jun.
[Is] ISSN:1348-0421
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:Mammals have co-evolved with retroviruses, including lentiviruses, over a long period. Evidence supporting this contention is that viral infectivity factor (Vif) encoded by lentiviruses antagonizes the anti-viral action of cellular apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3 (APOBEC3) of the host. To orchestrate E3 ubiquitin ligase complex for APOBEC3 degradation, Vifs utilize mammalian proteins such as core-binding factor beta (CBFB; for primate lentiviruses) or cyclophilin A (CYPA; for Maedi-Visna virus [MVV]). However, the co-evolutionary relationship between lentiviral Vif and the mammalian proteins associated with Vif-mediated APOBEC3 degradation is poorly understood. Moreover, it is unclear whether Vif proteins of small ruminant lentiviruses (SRLVs), including MVV and caprine arthritis encephalitis virus (CAEV), commonly utilize CYPA to degrade the APOBEC3 of their hosts. In this study, molecular phylogenetic and protein homology modeling revealed that Vif co-factors are evolutionarily and structurally conserved. It was also found that not only MVV but also CAEV Vifs degrade APOBEC3 of both sheep and goats and that CAEV Vifs interact with CYPA. These findings suggest that lentiviral Vifs chose evolutionarily and structurally stable proteins as their partners (e.g., CBFB or CYPA) for APOBEC3 degradation and, particularly, that SRLV Vifs evolved to utilize CYPA as their co-factor in degradation of ovine and caprine APOBEC3.
[Mh] Termos MeSH primário: Vírus da Artrite-Encefalite Caprina/genética
Ciclofilina A/genética
Ciclofilina A/metabolismo
Citidina Desaminase/metabolismo
Produtos do Gene vif/genética
Produtos do Gene vif/metabolismo
[Mh] Termos MeSH secundário: Animais
Vírus da Artrite-Encefalite Caprina/metabolismo
Células Cultivadas
Subunidade beta de Fator de Ligação ao Core/genética
Subunidade beta de Fator de Ligação ao Core/metabolismo
Ciclofilinas/genética
Ciclofilinas/metabolismo
Citidina Desaminase/genética
Evolução Molecular
Cabras
Células HEK293
Interações Hospedeiro-Patógeno
Seres Humanos
Interleucina-2/genética
Filogenia
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Core Binding Factor beta Subunit); 0 (Gene Products, vif); 0 (Interleukin-2); 137497-17-7 (cyclophilin B); EC 3.5.4.5 (Cytidine Deaminase); EC 5.2.1.- (Cyclophilin A); EC 5.2.1.- (Cyclophilins)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160520
[St] Status:MEDLINE
[do] DOI:10.1111/1348-0421.12387


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[PMID]:26935128
[Au] Autor:Yoshikawa R; Nakano Y; Yamada E; Izumi T; Misawa N; Koyanagi Y; Sato K
[Ad] Endereço:Laboratory of Viral Pathogenesis, Institute for Virus Research, Kyoto University, Kyoto, 6068507.
[Ti] Título:Species-specific differences in the ability of feline lentiviral Vif to degrade feline APOBEC3 proteins.
[So] Source:Microbiol Immunol;60(4):272-9, 2016 Apr.
[Is] ISSN:1348-0421
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:How host-virus co-evolutionary relationships manifest is one of the most intriguing issues in virology. To address this topic, the mammal-lentivirus relationship can be considered as an interplay of cellular and viral proteins, particularly apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3 (APOBEC3) and viral infectivity factor (Vif). APOBEC3s enzymatically restrict lentivirus replication, whereas Vif antagonizes the host anti-viral action mediated by APOBEC3. In this study, the focus was on the interplay between feline APOBEC3 proteins and two feline immunodeficiency viruses in cats and pumas. To our knowledge, this study provides the first evidence of non-primate lentiviral Vif being incapable of counteracting a natural host's anti-viral activity mediated via APOBEC3 protein.
[Mh] Termos MeSH primário: Citosina Desaminase/metabolismo
Produtos do Gene vif/metabolismo
Vírus da Imunodeficiência Felina/metabolismo
[Mh] Termos MeSH secundário: Animais
Gatos
Citosina Desaminase/genética
Evolução Molecular
Produtos do Gene vif/genética
Produtos do Gene vif/imunologia
Interações Hospedeiro-Patógeno
Imunidade Inata
Vírus da Imunodeficiência Felina/genética
Vírus da Imunodeficiência Felina/imunologia
Puma
Especificidade da Espécie
Viroses/veterinária
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gene Products, vif); EC 3.5.4.1 (APOBEC3 protein, human); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160304
[St] Status:MEDLINE
[do] DOI:10.1111/1348-0421.12371


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[PMID]:26590796
[Au] Autor:Franzdóttir SR; Ólafsdóttir K; Jónsson SR; Strobel H; Andrésson ÓS; Andrésdóttir V
[Ad] Endereço:Institute for Experimental Pathology, Keldur, University of Iceland, Reykjavik, Iceland.
[Ti] Título:Two mutations in the vif gene of maedi-visna virus have different phenotypes, indicating more than one function of Vif.
[So] Source:Virology;488:37-42, 2016 Jan 15.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Like most other lentiviruses, maedi-visna virus (MVV) requires Vif for replication in natural target cells and in vivo. Here, we show that Vif-deficient MVV accumulates G-A mutations in the sequence context characteristic of ovine APOBEC3, consistent with a role of MVV Vif in neutralizing APOBEC3. We studied two point mutations in the vif gene of MVV. One was a tryptophan to arginine mutation that affects the interaction with APOBEC3 and caused G-A hypermutation. The other mutation was a proline to serine mutation that together with a mutation in the capsid protein caused attenuated replication in fetal ovine synovial (FOS) cells but not in sheep choroid plexus (SCP) cells. There was no hypermutation associated with this mutation. These results suggest that MVV Vif exerts more than one function and that there may be interaction between Vif and the capsid. The results also suggest the involvement of an unknown host factor in MVV Vif function.
[Mh] Termos MeSH primário: Produtos do Gene vif/genética
Mutação de Sentido Incorreto
Mutação Puntual
Replicação Viral
Vírus Visna-Maedi/fisiologia
[Mh] Termos MeSH secundário: Proteínas do Capsídeo/genética
Fenótipo
Vírus Visna-Maedi/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Gene Products, vif)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160206
[Lr] Data última revisão:
160206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151123
[St] Status:MEDLINE


  10 / 374 MEDLINE  
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[PMID]:26544511
[Au] Autor:Land AM; Wang J; Law EK; Aberle R; Kirmaier A; Krupp A; Johnson WE; Harris RS
[Ad] Endereço:Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Masonic Cancer Center, and Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota, USA.
[Ti] Título:Degradation of the cancer genomic DNA deaminase APOBEC3B by SIV Vif.
[So] Source:Oncotarget;6(37):39969-79, 2015 Nov 24.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:APOBEC3B is a newly identified source of mutation in many cancers, including breast, head/neck, lung, bladder, cervical, and ovarian. APOBEC3B is a member of the APOBEC3 family of enzymes that deaminate DNA cytosine to produce the pro-mutagenic lesion, uracil. Several APOBEC3 family members function to restrict virus replication. For instance, APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H combine to restrict HIV-1 in human lymphocytes. HIV-1 counteracts these APOBEC3s with the viral protein Vif, which targets the relevant APOBEC3s for proteasomal degradation. While APOBEC3B does not restrict HIV-1 and is not targeted by HIV-1 Vif in CD4-positive T cells, we asked whether related lentiviral Vif proteins could degrade APOBEC3B. Interestingly, several SIV Vif proteins are capable of promoting APOBEC3B degradation, with SIVmac239 Vif proving the most potent. This likely occurs through the canonical polyubiquitination mechanism as APOBEC3B protein levels are restored by MG132 treatment and by altering a conserved E3 ligase-binding motif. We further show that SIVmac239 Vif can prevent APOBEC3B mediated geno/cytotoxicity and degrade endogenous APOBEC3B in several cancer cell lines. Our data indicate that the APOBEC3B degradation potential of SIV Vif is an effective tool for neutralizing the cancer genomic DNA deaminase APOBEC3B. Further optimization of this natural APOBEC3 antagonist may benefit cancer therapy.
[Mh] Termos MeSH primário: Citidina Desaminase/metabolismo
Produtos do Gene vif/metabolismo
Vírus da Imunodeficiência Símia/metabolismo
[Mh] Termos MeSH secundário: Desaminase APOBEC-3G
Animais
Linhagem Celular Tumoral
Sobrevivência Celular/genética
Citidina Desaminase/genética
Dano ao DNA
Produtos do Gene vif/genética
Células HEK293
Seres Humanos
Immunoblotting
Macaca mulatta/virologia
Antígenos de Histocompatibilidade Menor
Neoplasias/genética
Neoplasias/metabolismo
Neoplasias/patologia
Complexo de Endopeptidases do Proteassoma/metabolismo
Proteólise
Vírus da Imunodeficiência Símia/genética
Produtos do Gene vif do Vírus da Imunodeficiência Humana/genética
Produtos do Gene vif do Vírus da Imunodeficiência Humana/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Gene Products, vif); 0 (Minor Histocompatibility Antigens); 0 (vif Gene Products, Human Immunodeficiency Virus); 0 (vif protein, Human immunodeficiency virus 1); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.5.4.5 (APOBEC-3G Deaminase); EC 3.5.4.5 (APOBEC3B protein, human); EC 3.5.4.5 (APOBEC3G protein, human); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151107
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.5483



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