Base de dados : MEDLINE
Pesquisa : B04.820.057 [Categoria DeCS]
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[PMID]:28736175
[Au] Autor:Shimon A; Shani O; Diskin R
[Ad] Endereço:Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
[Ti] Título:Structural Basis for Receptor Selectivity by the Whitewater Arroyo Mammarenavirus.
[So] Source:J Mol Biol;429(18):2825-2839, 2017 Sep 01.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Whitewater Arroyo virus belongs to the "New World" group of mammarenaviruses that reside in rodent reservoirs and are prevalent in North and South Americas. Clades B and A/B of New World mammarenaviruses use transferrin receptor 1 (TfR1) for entry. While all of these viruses use rodent-derived TfR1 orthologs, some can also use the human-TfR1 and thereby infect humans. Although we have structural information for TfR1 recognition by pathogenic virus, we do not know what the structural differences are between the receptor-binding domains of pathogenic and non-pathogenic viruses that allow some but not all viruses to utilize the human receptor for entry. The poor understanding of the molecular determinants of mammarenavirus host range, and thus pathogenicity, is partly due to the low sequence similarity between the receptor-binding domains from these viruses and the limited available structural information that preclude the use of modeling approaches. Here we present the first crystal structure of a receptor-binding domain of a non-pathogenic clade A/B mammarenavirus. This structure reveals the magnitude of structural differences within the receptor-binding domains of TfR1-tropic viruses. Our structural and sequence analyses indicate that the same structural incompatibilities with the human receptor equally affect both pathogenic and non-pathogenic mammarenaviruses. Non-pathogenic viruses do not have specific structural elements that prevent them from using the human receptor. Instead, the ability to utilize the human receptor directly depends on the extent of weak interactions throughout the receptor-binding site that in some viruses are sufficiently strong to overcome the structural incompatibilities.
[Mh] Termos MeSH primário: Arenaviridae/fisiologia
Especificidade de Hospedeiro
Receptores da Transferrina/metabolismo
Receptores Virais/metabolismo
Proteínas do Envelope Viral/química
Ligação Viral
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Conformação Proteica
Homologia de Sequência
Proteínas do Envelope Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptors, Transferrin); 0 (Receptors, Virus); 0 (Viral Envelope Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


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[PMID]:28515291
[Au] Autor:Stenglein MD; Sanchez-Migallon Guzman D; Garcia VE; Layton ML; Hoon-Hanks LL; Boback SM; Keel MK; Drazenovich T; Hawkins MG; DeRisi JL
[Ad] Endereço:Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado, USA.
[Ti] Título:Differential Disease Susceptibilities in Experimentally Reptarenavirus-Infected Boa Constrictors and Ball Pythons.
[So] Source:J Virol;91(15), 2017 Aug 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inclusion body disease (IBD) is an infectious disease originally described in captive snakes. It has traditionally been diagnosed by the presence of large eosinophilic cytoplasmic inclusions and is associated with neurological, gastrointestinal, and lymphoproliferative disorders. Previously, we identified and established a culture system for a novel lineage of arenaviruses isolated from boa constrictors diagnosed with IBD. Although ample circumstantial evidence suggested that these viruses, now known as reptarenaviruses, cause IBD, there has been no formal demonstration of disease causality since their discovery. We therefore conducted a long-term challenge experiment to test the hypothesis that reptarenaviruses cause IBD. We infected boa constrictors and ball pythons by cardiac injection of purified virus. We monitored the progression of viral growth in tissues, blood, and environmental samples. Infection produced dramatically different disease outcomes in snakes of the two species. Ball pythons infected with Golden Gate virus (GoGV) and with another reptarenavirus displayed severe neurological signs within 2 months, and viral replication was detected only in central nervous system tissues. In contrast, GoGV-infected boa constrictors remained free of clinical signs for 2 years, despite high viral loads and the accumulation of large intracellular inclusions in multiple tissues, including the brain. Inflammation was associated with infection in ball pythons but not in boa constrictors. Thus, reptarenavirus infection produces inclusions and inclusion body disease, although inclusions are neither necessarily associated with nor required for disease. Although the natural distribution of reptarenaviruses has yet to be described, the different outcomes of infection may reflect differences in geographical origin. New DNA sequencing technologies have made it easier than ever to identify the sequences of microorganisms in diseased tissues, i.e., to identify organisms that appear to cause disease, but to be certain that a candidate pathogen actually causes disease, it is necessary to provide additional evidence of causality. We have done this to demonstrate that reptarenaviruses cause inclusion body disease (IBD), a serious transmissible disease of snakes. We infected boa constrictors and ball pythons with purified reptarenavirus. Ball pythons fell ill within 2 months of infection and displayed signs of neurological disease typical of IBD. In contrast, boa constrictors remained healthy over 2 years, despite high levels of virus throughout their bodies. This difference matches previous reports that pythons are more susceptible to IBD than boas and could reflect the possibility that boas are natural hosts of these viruses in the wild.
[Mh] Termos MeSH primário: Infecções por Arenaviridae/veterinária
Arenaviridae/crescimento & desenvolvimento
Arenaviridae/imunologia
Boidae/virologia
Suscetibilidade a Doenças
[Mh] Termos MeSH secundário: Estruturas Animais/patologia
Estruturas Animais/virologia
Animais
Infecções por Arenaviridae/imunologia
Infecções por Arenaviridae/patologia
Inflamação/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE


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[PMID]:28505175
[Au] Autor:Rosenthal M; Gogrefe N; Vogel D; Reguera J; Rauschenberger B; Cusack S; Günther S; Reindl S
[Ad] Endereço:Department of Virology, Bernhard-Nocht-Institute for Tropical Medicine, Hamburg, Germany.
[Ti] Título:Structural insights into reptarenavirus cap-snatching machinery.
[So] Source:PLoS Pathog;13(5):e1006400, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cap-snatching was first discovered in influenza virus. Structures of the involved domains of the influenza virus polymerase, namely the endonuclease in the PA subunit and the cap-binding domain in the PB2 subunit, have been solved. Cap-snatching endonucleases have also been demonstrated at the very N-terminus of the L proteins of mammarena-, orthobunya-, and hantaviruses. However, a cap-binding domain has not been identified in an arena- or bunyavirus L protein so far. We solved the structure of the 326 C-terminal residues of the L protein of California Academy of Sciences virus (CASV), a reptarenavirus, by X-ray crystallography. The individual domains of this 37-kDa fragment (L-Cterm) as well as the domain arrangement are structurally similar to the cap-binding and adjacent domains of influenza virus polymerase PB2 subunit, despite the absence of sequence homology, suggesting a common evolutionary origin. This enabled identification of a region in CASV L-Cterm with similarity to a cap-binding site; however, the typical sandwich of two aromatic residues was missing. Consistent with this, cap-binding to CASV L-Cterm could not be detected biochemically. In addition, we solved the crystal structure of the corresponding endonuclease in the N-terminus of CASV L protein. It shows a typical endonuclease fold with an active site configuration that is essentially identical to that of known mammarenavirus endonuclease structures. In conclusion, we provide evidence for a presumably functional cap-snatching endonuclease in the N-terminus and a degenerate cap-binding domain in the C-terminus of a reptarenavirus L protein. Implications of these findings for the cap-snatching mechanism in arenaviruses are discussed.
[Mh] Termos MeSH primário: Infecções por Arenaviridae/virologia
Arenaviridae/enzimologia
Endonucleases/metabolismo
Modelos Moleculares
[Mh] Termos MeSH secundário: Arenaviridae/química
Arenaviridae/genética
Cristalografia por Raios X
Endonucleases/química
Endonucleases/genética
Conformação Proteica
Domínios Proteicos
Capuzes de RNA
Proteínas Virais/química
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA Caps); 0 (Viral Proteins); EC 3.1.- (Endonucleases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006400


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[PMID]:28062291
[Au] Autor:Abba Y; Hassim H; Hamzah H; Ibrahim OE; Mohd Lila MA; Noordin MM
[Ad] Endereço:Department of Veterinary Pathology and Microbiology, Faculty of Veterinary Medicine, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia; Department of Veterinary Pathology, Faculty of Veterinary Medicine, University of Maiduguri, PMB 1069, Maiduguri 600233, Borno State, Nigeria.
[Ti] Título:Pathological vicissitudes and oxidative stress enzyme responses in mice experimentally infected with reptarenavirus (isolate UPM/MY01).
[So] Source:Microb Pathog;104:17-27, 2017 Mar.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Boid inclusion body disease (BIBD) is a viral disease of boid snakes believed to be caused by reptarenavirus belonging to the family Arenaviridae. Unlike most mammalian arenaviruses, the reservoir host for reptarenavirus is still unknown. In this study, the pathological responses were evaluated in a mouse model for a period of 28 days. Blood and tissue samples (lung, liver, spleen, heart, kidney and brain) were collected for evaluation of hematology, biochemistry, histopathology and oxidative enzyme levels at six time points (1, 3, 7, 14, 21 and 28 days), after viral infection (2.0 × 10 pfu/mL) in the infected and normal saline in the control groups. An initial increase (p < 0.05) in white blood cell (WBC), neutrophil and lymphocyte counts were observed in the infected group at day 3 post infection, and a decline (p < 0.05) on day 7 and 4 post infection. Significant (p < 0.05) increases in alanine transaminase (ALT), aspartate transaminase (AST), creatinine, total protein and globulin levels were also observed in the infected group. An increased (p < 0.05) level of hydrogen peroxide, total antioxidant capacity (TAC), superoxide dismutase (SOD) activity and catalase activity (CAT) were frequently observed on different days in the infected group. The MDA activity was increased (p < 0.05) in the infected group on day 7 and 14. Histopathological changes observed in the liver, kidney, spleen, brain and lungs were mainly associated with degeneration, necrosis and infiltration of lymphocytes. Viral counts were low on days 7 and 14 but surged in both the liver and spleen on day 21 and 28. This study has shown that reptarenavirus replicates in mammalian host and induces oxidative stress. Furthermore, the resultant hematobiochemical and histopathological changes observed in infected mice were similar to what has been reported in mammarenavirus infections. This suggests that rodents may serve as potential reservoir hosts for reptarenavirus.
[Mh] Termos MeSH primário: Infecções por Arenaviridae/metabolismo
Arenaviridae
Estresse Oxidativo
[Mh] Termos MeSH secundário: Alanina Transaminase
Doenças dos Animais/genética
Doenças dos Animais/metabolismo
Doenças dos Animais/patologia
Doenças dos Animais/virologia
Animais
Antioxidantes/metabolismo
Infecções por Arenaviridae/genética
Infecções por Arenaviridae/patologia
Infecções por Arenaviridae/virologia
Biomarcadores
Catalase
Modelos Animais de Doenças
Regulação Enzimológica da Expressão Gênica
Peróxido de Hidrogênio/metabolismo
Peroxidação de Lipídeos
Fígado/patologia
Fígado/virologia
Pulmão/patologia
Pulmão/virologia
Masculino
Camundongos
Espécies Reativas de Oxigênio
Baço/patologia
Baço/virologia
Superóxido Dismutase/metabolismo
Células Vero
Carga Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biomarkers); 0 (Reactive Oxygen Species); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase); EC 2.6.1.2 (Alanine Transaminase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170406
[Lr] Data última revisão:
170406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE


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[PMID]:27938703
[Au] Autor:Chang L; Fu D; Stenglein MD; Hernandez JA; DeRisi JL; Jacobson ER
[Ad] Endereço:Department of Small Animal Clinical Sciences, College of Veterinary Medicine, University of Florida, 2015 SW 16th Avenue, Gainesville, FL 32608, USA.
[Ti] Título:Detection and prevalence of boid inclusion body disease in collections of boas and pythons using immunological assays.
[So] Source:Vet J;218:13-18, 2016 Dec.
[Is] ISSN:1532-2971
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Inclusion body disease (IBD) of boas and pythons is characterized by the intracytoplasmic accumulation of an antigenic 68 kDa viral protein IBDP, more recently known as the nucleoprotein (NP) of the reptarenaviruses. Blood samples of 131 captive boas and pythons (53 boa constrictors, Boa constrictor; 35 rainbow boas, Epicrates cenchria; 22 ball pythons, Python regius; 5 carpet pythons, Morelia spilota; 6 Burmese pythons, Python bivittatus; 4 Jamaican boas, Epicrates subflavus; 5 anacondas, Eunectes spp.; and 1 green tree python, Morelia viridis) were obtained from 28 collections in the USA. Diagnosis of IBD was initially made by the identification of eosinophilic intracytoplasmic inclusion bodies in hematoxylin and eosin (HE) stained blood films and isolated peripheral white blood cells (PWBC). The overall prevalence of IBD in study snakes was 25/131 or 19% (95% CI = 12.4%, 25.8%) with boa constrictors being more commonly infected (22/53 or 41.5%; 95% CI = 28.2%, 54.8%) than other species in this study. Of the 22 IBD positive boa constrictors, 87% were clinically healthy, 13% had various signs of chronic illness, and none showed signs of central nervous system disease. Using a validated monoclonal anti-NP antibody, NP was confirmed within the isolated PWBC by immunohistochemical staining and Western blots. The presence of reptarenaviruses within blood samples of 27 boa constrictors and three rainbow boas was also assessed by PCR. Among boa constrictors, very good agreements were shown between the observation of inclusion bodies (by HE stain) and the presence of NP (by immunohistochemistry, kappa = 0.92; and Western blots, kappa = 0.89), or the presence of reptarenaviruses (by PCR; kappa = 0.92).
[Mh] Termos MeSH primário: Animais de Zoológico
Infecções por Arenaviridae/veterinária
Arenaviridae/isolamento & purificação
Boidae
[Mh] Termos MeSH secundário: Animais
Infecções por Arenaviridae/epidemiologia
Infecções por Arenaviridae/virologia
Western Blotting/veterinária
Amarelo de Eosina-(YS)
Nível de Saúde
Hematoxilina
Imuno-Histoquímica/veterinária
Nucleoproteínas/isolamento & purificação
Prevalência
Especificidade da Espécie
Proteínas Virais/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (Viral Proteins); TDQ283MPCW (Eosine Yellowish-(YS)); YKM8PY2Z55 (Hematoxylin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


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[PMID]:27562602
[Au] Autor:Wang W; Zhou Z; Zhang L; Wang S; Xiao G
[Ad] Endereço:State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China. wangwei@wh.iov.cn.
[Ti] Título:Structure-function relationship of the mammarenavirus envelope glycoprotein.
[So] Source:Virol Sin;31(5):380-394, 2016 Oct.
[Is] ISSN:1995-820X
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Mammarenaviruses, including lethal pathogens such as Lassa virus and Junín virus, can cause severe hemorrhagic fever in humans. Entry is a key step for virus infection, which starts with binding of the envelope glycoprotein (GP) to receptors on target cells and subsequent fusion of the virus with target cell membranes. The GP precursor is synthesized as a polypeptide, and maturation occurs by two cleavage events, yielding a tripartite GP complex (GPC) formed by a stable signal peptide (SSP), GP1 and GP2. The unique retained SSP interacts with GP2 and plays essential roles in virion maturation and infectivity. GP1 is responsible for binding to the cell receptor, and GP2 is a class I fusion protein. The native structure of the tripartite GPC is unknown. GPC is critical for the receptor binding, membrane fusion and neutralization antibody recognition. Elucidating the molecular mechanisms underlining the structure-function relationship of the three subunits is the key for understanding their function and can facilitate novel avenues for combating virus infections. This review summarizes the basic aspects and recent research of the structure-function relationship of the three subunits. We discuss the structural basis of the receptor-binding domain in GP1, the interaction between SSP and GP2 and its role in virion maturation and membrane fusion, as well as the mechanism by which glycosylation stabilizes the GPC structure and facilitates immune evasion. Understanding the molecular mechanisms involved in these aspects will contribute to the development of novel vaccines and treatment strategies against mammarenaviruses infection.
[Mh] Termos MeSH primário: Infecções por Arenaviridae/virologia
Arenaviridae/metabolismo
Proteínas do Envelope Viral/química
Proteínas do Envelope Viral/metabolismo
[Mh] Termos MeSH secundário: Animais
Arenaviridae/química
Arenaviridae/genética
Seres Humanos
Proteínas do Envelope Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Viral Envelope Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160827
[St] Status:MEDLINE


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[PMID]:27314481
[Au] Autor:Sabino-Santos G; Maia FG; Jonsson CB; Goodin DG; Salazar-Bravo J; Figueiredo LT
[Ad] Endereço:1 Center for Virology Research, School of Medicine in Ribeirão Preto, University of São Paulo, Avenida Bandeirantes 3900, Ribeirão Preto, São Paulo, 14049-900, Brazil;
[Ti] Título:Serologic Evidence of Mammarenaviruses among Wild Rodents in Brazil.
[So] Source:J Wildl Dis;52(3):766-9, 2016 Jul.
[Is] ISSN:1943-3700
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We screened blood samples from 560 wild rodents collected in southeastern Brazil for antibodies to a recombinant nucleoprotein (rN) of Junín virus. Six rodents were antibody positive (1.1%), demonstrating evidence of infection with mammarenaviruses in several species of Brazilian rodents.
[Mh] Termos MeSH primário: Infecções por Arenaviridae/veterinária
Arenaviridae/classificação
Roedores/virologia
[Mh] Termos MeSH secundário: Animais
Animais Selvagens
Infecções por Arenaviridae/epidemiologia
Infecções por Arenaviridae/virologia
Brasil/epidemiologia
Estudos Soroepidemiológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160618
[St] Status:MEDLINE
[do] DOI:10.7589/2015-09-252


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PubMed Central Texto completo
Texto completo
[PMID]:26657729
[Au] Autor:Meyer B; Ly H
[Ad] Endereço:Department of Veterinary and Biomedical Sciences, University of Minnesota, Twin Cities, MN, USA.
[Ti] Título:Immunosuppression by hemorrhagic fever-causing viruses.
[So] Source:Oncotarget;6(42):44057-8, 2015 Dec 29.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Arenaviridae/imunologia
Filoviridae/imunologia
Flaviviridae/imunologia
Febres Hemorrágicas Virais/imunologia
Febres Hemorrágicas Virais/virologia
Tolerância Imunológica
Imunidade Inata
Orthobunyavirus/imunologia
[Mh] Termos MeSH secundário: Animais
Arenaviridae/metabolismo
Filoviridae/metabolismo
Flaviviridae/metabolismo
Febres Hemorrágicas Virais/metabolismo
Interações Hospedeiro-Patógeno
Seres Humanos
Orthobunyavirus/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:EDITORIAL
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.6509


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[PMID]:26401045
[Au] Autor:Iwasaki M; Ngo N; Cubitt B; Teijaro JR; de la Torre JC
[Ad] Endereço:Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
[Ti] Título:General Molecular Strategy for Development of Arenavirus Live-Attenuated Vaccines.
[So] Source:J Virol;89(23):12166-77, 2015 Dec.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Hemorrhagic fever arenaviruses (HFA) pose important public health problems in regions where they are endemic. Thus, Lassa virus (LASV) infects several hundred thousand individuals yearly in West Africa, causing a large number of Lassa fever cases associated with high morbidity and mortality. Concerns about human-pathogenic arenaviruses are exacerbated because of the lack of FDA-licensed arenavirus vaccines and because current antiarenaviral therapy is limited to an off-label use of ribavirin that is only partially effective. The Mopeia virus (MOPV)/LASV reassortant (ML29) is a LASV candidate live-attenuated vaccine (LAV) that has shown promising results in animal models. Nevertheless, the mechanism of ML29 attenuation remains unknown, which raises concerns about the phenotypic stability of ML29 in response to additional mutations. Development of LAVs based on well-defined molecular mechanisms of attenuation will represent a major step in combatting HFA. We used the prototypic arenavirus lymphocytic choriomeningitis virus (LCMV) to develop a general molecular strategy for arenavirus attenuation. Our approach involved replacement of the noncoding intergenic region (IGR) of the L genome segment with the IGR of the S genome segment to generate a recombinant LCMV, rLCMV(IGR/S-S), that was highly attenuated in vivo but induced protection against a lethal challenge with wild-type LCMV. Attenuation of rLCMV(IGR/S-S) was associated with a stable reorganization of the control of viral gene expression. This strategy can facilitate the rapid development of LAVs with the antigenic composition of the parental HFA and a mechanism of attenuation that minimizes concerns about increased virulence that could be caused by genetic changes in the LAV. IMPORTANCE: Hemorrhagic fever arenaviruses (HFA) cause high morbidity and mortality, and pose important public health problems in the regions where they are endemic. Implementation of live-attenuated vaccines (LAV) will represent a major step in combatting HFA. Here we have used the prototypic arenavirus LCMV to document a general molecular strategy for arenavirus attenuation that can facilitate the rapid development of safe and effective, as well as stable, LAV to combat HFA.
[Mh] Termos MeSH primário: Arenaviridae/imunologia
Febre Lassa/prevenção & controle
Vacinas Atenuadas/biossíntese
Vacinas Virais/biossíntese
[Mh] Termos MeSH secundário: Animais
Arenaviridae/genética
Northern Blotting
Cercopithecus aethiops
Primers do DNA/genética
Seres Humanos
Vírus da Coriomeningite Linfocítica/genética
Plasmídeos/genética
Vacinas Atenuadas/imunologia
Vacinas Sintéticas/genética
Células Vero
Vacinas Virais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Vaccines, Attenuated); 0 (Vaccines, Synthetic); 0 (Viral Vaccines)
[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:150925
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.02075-15


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[PMID]:26050472
[Au] Autor:Zhirnov IV; Ryabinin VA; Sinyakov AN; Ternovoy VA; Shikov AN
[Ti] Título:[A prototype of oligonucleotide microarray for detection of pathogens relating to arena- and Filoviridae families].
[So] Source:Bioorg Khim;41(1):54-66, 2015 Jan-Feb.
[Is] ISSN:0132-3423
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:A prototype of oligonucleotide microarray for detection of Lassa, Junin, Machupo, Guanarito viruses (Arenaviridae family), Ebola and Marburg viruses (Filoviridae family) was presented. An original approach founded on virus proteins (nucleocapsid protein for Junin, Guanarito, Machupo viruses and RNA-dependent RNA-polymerase for Lassa, Ebola and Marburg viruses) amino acid sequences analysis with subsequent transform of revealed unique peptides into due sets of oligonucleotides was used to design probes for hybridization and primers.
[Mh] Termos MeSH primário: Arenaviridae/genética
Primers do DNA/química
Ebolavirus/genética
Marburgvirus/genética
Análise de Sequência com Séries de Oligonucleotídeos/métodos
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Primers do DNA/genética
Análise de Sequência com Séries de Oligonucleotídeos/instrumentação
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Viral Proteins)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:150608
[Lr] Data última revisão:
150608
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150609
[St] Status:MEDLINE



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