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Referências encontradas : 138 [refinar]
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[PMID]:28878069
[Au] Autor:Andrade ACDSP; Rodrigues RAL; Oliveira GP; Andrade KR; Bonjardim CA; La Scola B; Kroon EG; Abrahão JS
[Ad] Endereço:Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, Minas Gerais, Brazil.
[Ti] Título:Filling Knowledge Gaps for Mimivirus Entry, Uncoating, and Morphogenesis.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Since the discovery of mimivirus, its unusual structural and genomic features have raised great interest in the study of its biology; however, many aspects concerning its replication cycle remain uncertain. In this study, extensive analyses of electron microscope images, as well as biological assay results, shed light on unclear points concerning the mimivirus replication cycle. We found that treatment with cytochalasin, a phagocytosis inhibitor, negatively impacted the incorporation of mimivirus particles by , causing a negative effect on viral growth in amoeba monolayers. Treatment of amoebas with bafilomicin significantly impacted mimivirus uncoating and replication. In conjunction with microscopic analyses, these data suggest that mimiviruses indeed depend on phagocytosis for entry into amoebas, and particle uncoating (and stargate opening) appears to be dependent on phagosome acidification. In-depth analyses of particle morphogenesis suggest that the mimivirus capsids are assembled from growing lamellar structures. Despite proposals from previous studies that genome acquisition occurs before the acquisition of fibrils, our results clearly demonstrate that the genome and fibrils can be acquired simultaneously. Our data suggest the existence of a specific area surrounding the core of the viral factory where particles acquire the surface fibrils. Furthermore, we reinforce the concept that defective particles can be formed even in the absence of virophages. Our work provides new information about unexplored steps in the life cycle of mimivirus. Investigating the viral life cycle is essential to a better understanding of virus biology. The combination of biological assays and microscopic images allows a clear view of the biological features of viruses. Since the discovery of mimivirus, many studies have been conducted to characterize its replication cycle, but many knowledge gaps remain to be filled. In this study, we conducted a new examination of the replication cycle of mimivirus and provide new evidence concerning some stages of the cycle which were previously unclear, mainly entry, uncoating, and morphogenesis. Furthermore, we demonstrate that atypical virion morphologies can occur even in the absence of virophages. Our results, along with previous data, allow us to present an ultimate model for the mimivirus replication cycle.
[Mh] Termos MeSH primário: Acanthamoeba castellanii/virologia
Mimiviridae/fisiologia
Internalização do Vírus
Replicação Viral/fisiologia
Desenvelopamento do Vírus/fisiologia
[Mh] Termos MeSH secundário: Acanthamoeba castellanii/metabolismo
Fagocitose
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE


  2 / 138 MEDLINE  
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[PMID]:28840939
[Au] Autor:Arroyo Mühr LS; Bzhalava Z; Hortlund M; Lagheden C; Nordqvist Kleppe S; Bzhalava D; Hultin E; Dillner J
[Ad] Endereço:Karolinska Institutet, Department of Laboratory Medicine, Division of Pathology, Karolinska University Hospital, Huddinge, Stockholm, 141 86, Sweden.
[Ti] Título:Viruses in cancers among the immunosuppressed.
[So] Source:Int J Cancer;141(12):2498-2504, 2017 Dec 15.
[Is] ISSN:1097-0215
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most cancer forms known to be caused by viruses are increased among the immunosuppressed, but several cancer forms without established viral etiology are also increased, notably nonmelanoma skin carcinoma (NMSC). We followed all 13,429 solid organ transplantation patients in Sweden for cancer occurrence after transplantation. We requested these tumor specimens and sequenced the first 89 specimens received (62 NMSCs, 27 other cancers). The sequences were analyzed for viruses based on two bioinformatics algorithms (paracel-blast (sensitive for detection of known viruses) and hidden Markov model (HMM; sensitive for distantly related viruses)). Among the 62 NMSCs, the virus family detected in the largest proportion of specimens was Mimiviridae (9/62 NMSCs). The majority of the virus-related reads belonged to Papillomaviridae. The HMM analysis identified 86 additional previously not described viral contigs related to 11 virus families, with reads related to Mimiviridae being the most common (detected in 28/62 NMSCs) with the most prevalent contig (Mimivirus SE906, 1937 bp) detected in 17/62 NMSCs. Among the 27 other cancers, viral sequences were detected in only 5 specimens by blast analysis, compared to in all 27 specimens by HMM (Mimiviridae, Poxviridae, Phycodnaviridae and virus-related sequences yet unclassified to any family). 99% of the virus reads belonged to a single previously not described sequence (Mimivirus SE996, 911 bp). A multitude of viruses is readily detectable in specimens with cancers occurring among the immunosuppressed, with sequences related to Mimiviridae being the most prevalent. Further research would be needed to elucidate the biological significance of the viruses.
[Mh] Termos MeSH primário: Neoplasias/imunologia
Transplante de Órgãos/efeitos adversos
Análise de Sequência de DNA/métodos
Viroses/epidemiologia
Vírus/classificação
[Mh] Termos MeSH secundário: Algoritmos
Biologia Computacional/métodos
Seres Humanos
Hospedeiro Imunocomprometido
Cadeias de Markov
Mimiviridae/genética
Mimiviridae/isolamento & purificação
Neoplasias/virologia
Papillomaviridae/genética
Papillomaviridae/isolamento & purificação
Suécia
Vírus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170826
[St] Status:MEDLINE
[do] DOI:10.1002/ijc.31017


  3 / 138 MEDLINE  
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[PMID]:28779233
[Au] Autor:Ku B; You JA; Oh KJ; Yun HY; Lee HS; Shin HC; Jung J; Shin YB; Kim SJ
[Ad] Endereço:Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Republic of Korea. bku@kribb.re.kr.
[Ti] Título:Crystal structures of two forms of the Acanthamoeba polyphaga mimivirus Rab GTPase.
[So] Source:Arch Virol;162(11):3407-3416, 2017 Nov.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Acanthamoeba polyphaga mimivirus (APMV) is a member of the family of giant viruses, harboring a 1,200 kbp genome within its 700 nm-diameter viral particle. The R214 gene of the APMV genome was recently shown to encode a homologue of the Rab GTPases, molecular switch proteins known to play a pivotal role in the regulation of membrane trafficking that were considered to exist only in eukaryotes. Herein, we report the first crystal structures of GDP- and GTP-bound forms of APMV Rab GTPase, both of which were determined at high resolution. An in-depth structural comparison of APMV Rab with each other and with mammalian Rab homologues led to an atomic-level elucidation of the inactive-active conformational change upon GDP/GTP exchange. APMV Rab GTPase exhibited considerable structural similarity to human Rab5, as previously predicted based on its amino acid sequence. However, it also contains unique structural features differentiating it from mammalian homologues, such as the functional substitution of a phenylalanine residue for the stabilization of the nucleotide's guanine base.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica/fisiologia
Regulação Viral da Expressão Gênica/fisiologia
Mimiviridae/metabolismo
Proteínas Virais/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Cristalização
Mimiviridae/genética
Modelos Moleculares
Conformação Proteica
Proteínas Virais/química
Proteínas Virais/genética
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Proteins); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3510-2


  4 / 138 MEDLINE  
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[PMID]:28763516
[Au] Autor:Kwon E; Pathak D; Chang HW; Kim DY
[Ad] Endereço:College of Pharmacy, Yeungnam University, Gyeongsan, Gyeongbuk, South Korea.
[Ti] Título:Crystal structure of mimivirus uracil-DNA glycosylase.
[So] Source:PLoS One;12(8):e0182382, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytosine deamination induced by stresses or enzymatic catalysis converts deoxycytidine into deoxyuridine, thereby introducing a G to A mutation after DNA replication. Base-excision repair to correct uracil to cytosine is initiated by uracil-DNA glycosylase (UDG), which recognizes and eliminates uracil from DNA. Mimivirus, one of the largest known viruses, also encodes a distinctive UDG gene containing a long N-terminal domain (N-domain; residues 1-130) and a motif-I (residues 327-343), in addition to the canonical catalytic domain of family I UDGs (also called UNGs). To understand the structural and functional features of the additional segments, we have determined the crystal structure of UNG from Acanthamoeba polyphaga mimivirus (mvUNG). In the crystal structure of mvUNG, residues 95-130 in the N-domain bind to a hydrophobic groove in the catalytic domain, and motif-I forms a short ß-sheet with a positively charged surface near the active site. Circular dichroism spectra showed that residues 1-94 are in a random coil conformation. Deletion of the three additional fragments reduced the activity and thermal stability, compared to full-length mvUNG. The results suggested that the mvUNG N-domain and motif-I are required for its structural and functional integrity.
[Mh] Termos MeSH primário: Mimiviridae/enzimologia
Uracila-DNA Glicosidase/química
[Mh] Termos MeSH secundário: Acanthamoeba/virologia
Motivos de Aminoácidos
Domínio Catalítico
Dicroísmo Circular
Cristalografia por Raios X
DNA/química
Reparo do DNA
Deleção de Genes
Mimiviridae/genética
N-Glicosil Hidrolases/química
Estrutura Secundária de Proteína
Coloração pela Prata
Especificidade por Substrato
Uracila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
56HH86ZVCT (Uracil); 9007-49-2 (DNA); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.- (Uracil-DNA Glycosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182382


  5 / 138 MEDLINE  
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[PMID]:28759330
[Au] Autor:Colson P; La Scola B; Raoult D
[Ad] Endereço:Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), Aix Marseille Université, UM63, CNRS 7278, IRD 198, INSERM 1095, Institut Hospitalo-Universitaire (IHU) Méditerranée Infection, Assistance Publique-Hôpitaux de Marseille (AP-HM), 13005 Marseille, France; email: didier.raoult@gmail.com.
[Ti] Título:Giant Viruses of Amoebae: A Journey Through Innovative Research and Paradigm Changes.
[So] Source:Annu Rev Virol;4(1):61-85, 2017 Sep 29.
[Is] ISSN:2327-0578
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Giant viruses of amoebae were discovered serendipitously in 2003; they are visible via optical microscopy, making them bona fide microbes. Their lifestyle, structure, and genomes break the mold of classical viruses. Giant viruses of amoebae are complex microorganisms. Their genomes harbor between 444 and 2,544 genes, including many that are unique to viruses, and encode translation components; their virions contain >100 proteins as well as mRNAs. Mimiviruses have a specific mobilome, including virophages, provirophages, and transpovirons, and can resist virophages through a system known as MIMIVIRE (mimivirus virophage resistance element). Giant viruses of amoebae bring upheaval to the definition of viruses and tend to separate the current virosphere into two categories: very simple viruses and viruses with complexity similar to that of other microbes. This new paradigm is propitious for enhanced detection and characterization of giant viruses of amoebae, and a particular focus on their role in humans is warranted.
[Mh] Termos MeSH primário: Amoeba/virologia
Genoma Viral
Vírus Gigantes/genética
Vírus Gigantes/fisiologia
[Mh] Termos MeSH secundário: DNA Viral
Vírus Gigantes/classificação
Vírus Gigantes/isolamento & purificação
Interações Hospedeiro-Patógeno
Mimiviridae/genética
Filogenia
Vírion/genética
Virófagos/genética
Virófagos/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DNA, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-virology-101416-041816


  6 / 138 MEDLINE  
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[PMID]:28518044
[Au] Autor:Raoult D; Levasseur A; La Scola B
[Ti] Título:PCR Detection of Mimivirus.
[So] Source:Emerg Infect Dis;23(6):1044-1045, 2017 06.
[Is] ISSN:1080-6059
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Mimiviridae/imunologia
Reação em Cadeia da Polimerase
[Mh] Termos MeSH secundário: Anticorpos Antivirais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Antibodies, Viral)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.3201/eid2306.161896


  7 / 138 MEDLINE  
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[PMID]:28446675
[Au] Autor:Gallot-Lavallée L; Blanc G; Claverie JM
[Ad] Endereço:Information Génomique et Structurale, UMR 7256 (IMM FR 3479) Centre National de la Recherche Scientifique & Aix-Marseille University, Marseille, France Lucie.Gallot-Lavallee@igs.cnrs-mrs.fr Jean-Michel.Claverie@univ-amu.fr.
[Ti] Título:Comparative Genomics of Chrysochromulina Ericina Virus and Other Microalga-Infecting Large DNA Viruses Highlights Their Intricate Evolutionary Relationship with the Established Mimiviridae Family.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chrysochromulina ericina virus CeV-01B (CeV) was isolated from Norwegian coastal waters in 1998. Its icosahedral particle is 160 nm in diameter and encloses a 474-kb double-stranded DNA (dsDNA) genome. This virus, although infecting a microalga (the haptophyceae , formerly ), is phylogenetically related to members of the family, initially established with the acanthamoeba-infecting mimivirus and megavirus as prototypes. This family was later split into two genera ( and ) following the characterization of a virus infecting the heterotrophic stramenopile (CroV). CeV, as well as two of its close relatives, which infect the unicellular photosynthetic eukaryotes (Phaeocystis globosa virus [PgV]) and (Aureococcus anophagefferens virus [AaV]), are currently unclassified by the International Committee on Viral Taxonomy (ICTV). The detailed comparative analysis of the CeV genome presented here confirms the phylogenetic affinity of this emerging group of microalga-infecting viruses with the but argues in favor of their classification inside a distinct clade within the family. Although CeV, PgV, and AaV share more common features among them than with the larger , they also exhibit a large complement of unique genes, attesting to their complex evolutionary history. We identified several gene fusion events and cases of convergent evolution involving independent lateral gene acquisitions. Finally, CeV possesses an unusual number of inteins, some of which are closely related despite being inserted in nonhomologous genes. This appears to contradict the paradigm of allele-specific inteins and suggests that the are especially efficient in spreading inteins while enlarging their repertoire of homing genes. Although it infects the microalga , CeV is more closely related to acanthamoeba-infecting viruses of the family than to any member of the , the ICTV-approved family historically including all alga-infecting large dsDNA viruses. CeV, as well as its relatives that infect the microalgae (PgV) and (AaV), remains officially unclassified and a source of confusion in the literature. Our comparative analysis of the CeV genome in the context of this emerging group of alga-infecting viruses suggests that they belong to a distinct clade within the established family. The presence of a large number of unique genes as well as specific gene fusion events, evolutionary convergences, and inteins integrated at unusual locations document the complex evolutionary history of the CeV lineage.
[Mh] Termos MeSH primário: Evolução Molecular
Genoma Viral
Mimiviridae/classificação
Mimiviridae/genética
Phycodnaviridae/classificação
Phycodnaviridae/genética
Filogenia
[Mh] Termos MeSH secundário: Análise por Conglomerados
Análise de Sequência de DNA
Homologia de Sequência
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE


  8 / 138 MEDLINE  
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[PMID]:28314774
[Au] Autor:Piacente F; De Castro C; Jeudy S; Gaglianone M; Laugieri ME; Notaro A; Salis A; Damonte G; Abergel C; Tonetti MG
[Ad] Endereço:From the Department of Experimental Medicine and Center of Excellence for Biomedical Research, University of Genova, 16126 Genova, Italy.
[Ti] Título:The rare sugar -acetylated viosamine is a major component of Mimivirus fibers.
[So] Source:J Biol Chem;292(18):7385-7394, 2017 May 05.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The giant virus Mimivirus encodes an autonomous glycosylation system that is thought to be responsible for the formation of complex and unusual glycans composing the fibers surrounding its icosahedral capsid, including the dideoxyhexose viosamine. Previous studies have identified a gene cluster in the virus genome, encoding enzymes involved in nucleotide-sugar production and glycan formation, but the functional characterization of these enzymes and the full identification of the glycans found in viral fibers remain incomplete. Because viosamine is typically found in acylated forms, we suspected that one of the genes might encode an acyltransferase, providing directions to our functional annotations. Bioinformatic analyses indicated that the L142 protein contains an N-terminal acyltransferase domain and a predicted C-terminal glycosyltransferase. Sequence analysis of the structural model of the L142 N-terminal domain indicated significant homology with some characterized sugar acetyltransferases that modify the C-4 amino group in the bacillosamine or perosamine biosynthetic pathways. Using mass spectrometry and NMR analyses, we confirmed that the L142 N-terminal domain is a sugar acetyltransferase, catalyzing the transfer of an acetyl moiety from acetyl-CoA to the C-4 amino group of UDP-d-viosamine. The presence of acetylated viosamine has also been confirmed on the glycosylated viral fibers, using GC-MS and NMR. This study represents the first report of a virally encoded sugar acetyltransferase.
[Mh] Termos MeSH primário: Aciltransferases/química
Proteínas do Capsídeo/química
Mimiviridae/enzimologia
[Mh] Termos MeSH secundário: Aciltransferases/metabolismo
Proteínas do Capsídeo/metabolismo
Glicosilação
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); EC 2.3.- (Acyltransferases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.783217


  9 / 138 MEDLINE  
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[PMID]:28247094
[Au] Autor:Kerepesi C; Grolmusz V
[Ad] Endereço:PIT Bioinformatics Group, Eötvös University, Pázmány Péter stny. 1/C, Budapest, 1117, Hungary.
[Ti] Título:The "Giant Virus Finder" discovers an abundance of giant viruses in the Antarctic dry valleys.
[So] Source:Arch Virol;162(6):1671-1676, 2017 Jun.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Mimivirus was identified in 2003 from a biofilm of an industrial water-cooling tower in England. Later, numerous new giant viruses were found in oceans and freshwater habitats, some of them having 2,500 genes. We have demonstrated their likely presence in four soil samples taken from the Kutch Desert (Gujarat, India). Here we describe a bioinformatics work-flow, called the "Giant Virus Finder" that is capable of discovering the likely presence of the genomes of giant viruses in metagenomic shotgun-sequenced datasets. The new workflow is applied to numerous hot and cold desert soil samples as well as some tundra- and forest soils. We show that most of these samples contain giant viruses, especially in the Antarctic dry valleys. The results imply that giant viruses could be frequent not only in aqueous habitats, but in a wide spectrum of soils on our planet.
[Mh] Termos MeSH primário: Vírus Gigantes/isolamento & purificação
Mimiviridae/isolamento & purificação
Microbiologia do Solo
[Mh] Termos MeSH secundário: Regiões Antárticas
Vírus Gigantes/classificação
Vírus Gigantes/genética
Mimiviridae/classificação
Mimiviridae/genética
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3286-4


  10 / 138 MEDLINE  
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[PMID]:28239153
[Au] Autor:Colson P; La Scola B; Levasseur A; Caetano-Anollés G; Raoult D
[Ad] Endereço:Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), Aix-Marseille University, UM63, CNRS 7278, IRD 198, INSERM 1095, Institut Hospitalo-Universitaire (IHU) - Méditerranée Infection, AP-HM, 19-21 Boulevard Jean Moulin, 13385 Marseille, France.
[Ti] Título:Mimivirus: leading the way in the discovery of giant viruses of amoebae.
[So] Source:Nat Rev Microbiol;15(4):243-254, 2017 Apr.
[Is] ISSN:1740-1534
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The accidental discovery of the giant virus of amoeba - Acanthamoeba polyphaga mimivirus (APMV; more commonly known as mimivirus) - in 2003 changed the field of virology. Viruses were previously defined by their submicroscopic size, which probably prevented the search for giant viruses, which are visible by light microscopy. Extended studies of giant viruses of amoebae revealed that they have genetic, proteomic and structural complexities that were not thought to exist among viruses and that are comparable to those of bacteria, archaea and small eukaryotes. The giant virus particles contain mRNA and more than 100 proteins, they have gene repertoires that are broader than those of other viruses and, notably, some encode translation components. The infection cycles of giant viruses of amoebae involve virus entry by amoebal phagocytosis and replication in viral factories. In addition, mimiviruses are infected by virophages, defend against them through the mimivirus virophage resistance element (MIMIVIRE) system and have a unique mobilome. Overall, giant viruses of amoebae, including mimiviruses, marseilleviruses, pandoraviruses, pithoviruses, faustoviruses and molliviruses, challenge the definition and classification of viruses, and have increasingly been detected in humans.
[Mh] Termos MeSH primário: Acanthamoeba/virologia
Amoeba/virologia
Vírus Gigantes/ultraestrutura
Mimiviridae/ultraestrutura
[Mh] Termos MeSH secundário: Genoma Viral/genética
Vírus Gigantes/genética
Vírus Gigantes/metabolismo
Mimiviridae/genética
Mimiviridae/metabolismo
Virófagos/genética
Internalização do Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE
[do] DOI:10.1038/nrmicro.2016.197



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