scholarly journals Phylogenetics Based on Partial ORF2 of Triatoma Virus in Triatomines Collected Over a Decade From Domiciliary Habitats

2015 ◽  
Vol 15 (1) ◽  
pp. 17-17 ◽  
Author(s):  
M. L. Susevich ◽  
G. A. Marti ◽  
A. Balsalobre ◽  
M. G. Echeverria
Keyword(s):  
Triatoma Virus

First Study of Different Insect Cells to Triatoma Virus Infection

2014 ◽  
Vol 70 (4) ◽  
pp. 470-475
Author(s):  
María Laura Susevich ◽  
Gerardo Aníbal Marti ◽  
Germán Ernesto Metz ◽  
María Gabriela Echeverría
Keyword(s):  
Virus Infection ◽  
Insect Cells ◽  
Triatoma Virus

scholarly journals Capsid protein identification and analysis of mature Triatoma virus (TrV) virions and naturally occurring empty particles

Virology ◽  
2011 ◽  
Vol 409 (1) ◽  
pp. 91-101 ◽  
Author(s):  
Jon Agirre ◽  
Kerman Aloria ◽  
Jesus M. Arizmendi ◽  
Ibón Iloro ◽  
Félix Elortza ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Protein Identification ◽  
Naturally Occurring ◽  
Triatoma Virus

scholarly journals Phasing of the Triatoma virus diffraction data using a cryo-electron microscopy reconstruction

Virology ◽  
2008 ◽  
Vol 375 (1) ◽  
pp. 85-93 ◽  
Author(s):  
L.F. Estrozi ◽  
E. Neumann ◽  
G. Squires ◽  
G. Rozas-Dennis ◽  
M. Costabel ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Diffraction Data ◽  
Cryo Electron Microscopy ◽  
Triatoma Virus

scholarly journals Seroprevalence of Triatoma virus (Dicistroviridae: Cripaviridae) antibodies in Chagas disease patients

2015 ◽  
Vol 8 (1) ◽  
pp. 29 ◽  
Author(s):  
Jailson Querido ◽  
María G Echeverría ◽  
Gerardo A Marti ◽  
Rita Costa ◽  
María L Susevich ◽  
...  
Keyword(s):  
Chagas Disease ◽  
Triatoma Virus

scholarly journals X-ray structure of Triatoma virus empty capsid: insights into the mechanism of uncoating and RNA release in dicistroviruses

2016 ◽  
Vol 97 (10) ◽  
pp. 2769-2779 ◽  
Author(s):  
Rubén Sánchez-Eugenia ◽  
Aritz Durana ◽  
Ibai López-Marijuan ◽  
Gerardo A. Marti ◽  
Diego M. A. Guérin
Keyword(s):  
X Ray ◽  
Triatoma Virus ◽  
Empty Capsid

scholarly journals Triatoma patagonica (Hemiptera, Reduviidae), a New Host for Triatoma virus

2002 ◽  
Vol 97 (3) ◽  
pp. 427-429 ◽  
Author(s):  
Gabriela S Rozas-Dennis ◽  
Néstor J Cazzaniga ◽  
Diego MA Guérin
Keyword(s):  
New Host ◽  
Triatoma Virus

scholarly journals Triatoma Virus Recombinant VP4 Protein Induces Membrane Permeability through Dynamic Pores

2015 ◽  
Vol 89 (8) ◽  
pp. 4645-4654 ◽  
Author(s):  
Rubén Sánchez-Eugenia ◽  
Julen Goikolea ◽  
David Gil-Cartón ◽  
Lissete Sánchez-Magraner ◽  
Diego M. A. Guérin
Keyword(s):  
Viral Infection ◽  
Membrane Permeabilization ◽  
Model Membranes ◽  
Cell Entry ◽  
Target Cells ◽  
Dependent Manner ◽  
Microscopy Imaging ◽  
Small Protein ◽  
Content Type ◽  
Triatoma Virus

ABSTRACTIn naked viruses, membrane breaching is a key step that must be performed for genome transfer into the target cells. Despite its importance, the mechanisms behind this process remain poorly understood. The small protein VP4, encoded by the genomes of most viruses of the orderPicornavirales, has been shown to be involved in membrane alterations. Here we analyzed the permeabilization activity of the natively nonmyristoylated VP4 protein from triatoma virus (TrV), a virus belonging to theDicistroviridaefamily within thePicornaviralesorder. The VP4 protein was produced as a C-terminal maltose binding protein (MBP) fusion to achieve its successful expression. This recombinant VP4 protein is able to produce membrane permeabilization in model membranes in a membrane composition-dependent manner. The induced permeability was also influenced by the pH, being greater at higher pH values. We demonstrate that the permeabilization activity elicited by the protein occurs through discrete pores that are inserted on the membrane. Sizing experiments using fluorescent dextrans, cryo-electron microscopy imaging, and other, additional techniques showed that recombinant VP4 forms heterogeneous proteolipidic pores rather than common proteinaceous channels. These results suggest that the VP4 protein may be involved in the membrane alterations required for genome transfer or cell entry steps during dicistrovirus infection.IMPORTANCEDuring viral infection, viruses need to overcome the membrane barrier in order to enter the cell and replicate their genome. In nonenveloped viruses membrane fusion is not possible, and hence, other mechanisms are implemented. Among other proteins, like the capsid-forming proteins and the proteins required for viral replication, several viruses of the orderPicornaviridaecontain a small protein called VP4 that has been shown to be involved in membrane alterations. Here we show that the triatoma virus VP4 protein is able to produce membrane permeabilization in model membranes by the formation of heterogeneous dynamic pores. These pores formed by VP4 may be involved in the genome transfer or cell entry steps during viral infection.

AC-ELISA and RT-PCR assays for the diagnosis of triatoma virus (TrV) in triatomines (Hemiptera: Reduviidae) species

2008 ◽  
Vol 153 (8) ◽  
pp. 1427-1432 ◽  
Author(s):  
Gerardo A. Marti ◽  
Ester T. González ◽  
Juan J. García ◽  
Ana R. Viguera ◽  
Diego M. A. Guérin ◽  
...  
Keyword(s):  
Rt Pcr ◽  
Triatoma Virus ◽  
Pcr Assays

scholarly journals Inoculation of Triatoma Virus (Dicistroviridae: Cripavirus) elicits a non-infective immune response in mice

2013 ◽  
Vol 6 (1) ◽  
pp. 66 ◽  
Author(s):  
Jailson F B Querido ◽  
Jon Agirre ◽  
Gerardo A Marti ◽  
Diego M A Guérin ◽  
Marcelo Silva
Keyword(s):  
Immune Response ◽  
Triatoma Virus
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