scholarly journals Maedi-Visna virus: current perspectives

2018 ◽  
Vol Volume 9 ◽  
pp. 11-21 ◽  
Author(s):  
Esperanza Gomez-Lucia ◽  
Nuria Barquero ◽  
Ana Domenech
Keyword(s):  
Visna Virus ◽  
Maedi Visna Virus

scholarly journals Implication of caspases during maedi–visna virus-induced apoptosis

2002 ◽  
Vol 83 (12) ◽  
pp. 3153-3161 ◽  
Author(s):  
R. Duval ◽  
V. Bellet ◽  
S. Delebassée ◽  
C. Bosgiraud
Keyword(s):  
Cell Death ◽  
Caspase 3 ◽  
Specific Cell ◽  
Caspase 9 ◽  
Virus Growth ◽  
Caspase Inhibitors ◽  
Visna Virus ◽  
Maedi Visna Virus ◽  
Cellular Lysis

Maedi–visna virus (MVV) causes encephalitis, pneumonia and arthritis in sheep. In vitro, MVV infection and replication lead to strong cytopathic effects characterized by syncytia formation and subsequent cellular lysis. It was demonstrated previously that MVV infection in vitro induces cell death of sheep choroid plexus cells (SCPC) by a mechanism that can be associated with apoptotic cell death. Here, the relative implication of several caspases during acute infection with MVV is investigated by employing diverse in vitro and in situ strategies. It was demonstrated using specific pairs of caspase substrates and inhibitors that, during in vitro infection of SCPC by MVV, the two major pathways of caspase activation (i.e. intrinsic and extrinsic pathways) were stimulated: significant caspase-9 and -8 activities, as well as caspase-3 activity, were detected. To study the role of caspases during MVV infection in vitro, specific, cell-permeable, caspase inhibitors were used. First, these results showed that both z-DEVD-FMK (a potent inhibitor of caspase-3-like activities) and z-VAD-FMK (a broad spectrum caspase inhibitor) inhibit caspase-9, -8 and -3 activities. Second, both irreversible caspase inhibitors, z-DEVD-FMK and z-VAD-FMK, delayed MVV-induced cellular lysis as well as virus growth. Third, during SCPC in vitro infection by MVV, cells were positively stained with FITC-VAD-FMK, a probe that specifically stains cells containing active caspases. In conclusion, these data suggest that MVV infection in vitro induces SCPC cell death by a mechanism that is strongly dependent on active caspases.

Development of a candidate DNA vaccine against Maedi-Visna virus

2007 ◽  
Vol 119 (3-4) ◽  
pp. 222-232 ◽  
Author(s):  
Ana M. Henriques ◽  
Miguel Fevereiro ◽  
Duarte M.F. Prazeres ◽  
Gabriel A. Monteiro
Keyword(s):  
Dna Vaccine ◽  
Visna Virus ◽  
Maedi Visna Virus

Maedi-visna virus persistence: Antigenic variation and latency

2017 ◽  
Vol 55 ◽  
pp. 6-12 ◽  
Author(s):  
Hallgrímur Arnarson ◽  
Arnar Pálsson ◽  
Margrét Gudnadóttir ◽  
Valgerdur Andrésdóttir
Keyword(s):  
Antigenic Variation ◽  
Virus Persistence ◽  
Visna Virus ◽  
Maedi Visna Virus

Expression of maedi-visna virus major core protein, p25: development of a sensitive p25 antigen detection assay

1992 ◽  
Vol 37 (3) ◽  
pp. 305-320 ◽  
Author(s):  
H.T. Reyburn ◽  
D.J. Roy ◽  
B.A. Blacklaws ◽  
D.R. Sargan ◽  
I. McConnell
Keyword(s):  
Core Protein ◽  
Antigen Detection ◽  
Visna Virus ◽  
Detection Assay ◽  
Maedi Visna Virus ◽  
Major Core Protein

scholarly journals Maedi-visna virus Vif protein uses motifs distinct from HIV-1 Vif to bind zinc and cofactor required for A3 degradation

2020 ◽  
pp. jbc.RA120.015828
Author(s):  
Kirsten M. Knecht ◽  
Yingxia Hu ◽  
Diana Rubene ◽  
Matthew Cook ◽  
Samantha J Ziegler ◽  
...  
Keyword(s):  
Viral Infections ◽  
Zinc Ion ◽  
Binding Motif ◽  
Cytidine Deaminases ◽  
Visna Virus ◽  
Primate Lentiviruses ◽  
Maedi Visna Virus ◽  
Hiv 1

The mammalian apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3 or A3) family of cytidine deaminases restrict viral infections by mutating viral DNA and impeding reverse transcription. To overcome this antiviral activity, most lentiviruses express a viral accessory protein called Vif, which recruits A3 proteins to Cullin-RING E3 ubiquitin ligases such as Cul5 for ubiquitylation and subsequent proteasomal degradation. While Vif proteins from primate lentiviruses like HIV-1 utilize the transcription factor CBFβ as a non-canonical cofactor to stabilize the complex, maedi-visna virus (MVV) Vif hijacks cyclophilin A (CypA) instead. Since CBFβ and CypA are both highly conserved among mammals, the requirement for two different cellular cofactors suggests that these two A3-targeting Vif proteins have different biochemical and structural properties. To investigate this topic, we used a combination of in vitro biochemical assays and in vivo A3 degradation assays to study motifs required for MVV Vif to bind zinc ion, Cul5, and the cofactor CypA. Our results demonstrate that while some common motifs between HIV-1 Vif and MVV Vif are involved in recruiting Cul5, different determinants in MVV Vif are required for cofactor binding and stabilization of the E3 ligase complex, such as the zinc-binding motif and N- and C-terminal regions of the protein. Results from this study advance our understanding of the mechanism of MVV Vif recruitment of cellular factors and the evolution of lentiviral Vif proteins.

Relative contribution of colostrum from Maedi-Visna virus (MVV) infected ewes to MVV-seroprevalence in lambs

2005 ◽  
Vol 78 (3) ◽  
pp. 237-243 ◽  
Author(s):  
V. Álvarez ◽  
J. Arranz ◽  
M. Daltabuit-Test ◽  
I. Leginagoikoa ◽  
R.A. Juste ◽  
...  
Keyword(s):  
Relative Contribution ◽  
Visna Virus ◽  
Maedi Visna Virus

Maedi visna virus infection: where are we now?

Livestock ◽  
2015 ◽  
Vol 20 (1) ◽  
pp. 40-44
Author(s):  
Lynn Gibson
Keyword(s):  
Virus Infection ◽  
Visna Virus ◽  
Maedi Visna Virus
Sign in / Sign up

Export Citation Format

Share Document