scholarly journals Inhibition of viral replication by small interfering RNA targeting of the foot-and-mouth disease virus receptor integrin β6

2017 ◽  
Vol 14 (1) ◽  
pp. 735-742
Author(s):  
Na-Na Hu ◽  
Wenzhi Zhang ◽  
Lina Wang ◽  
Yuan-Zhi Wang ◽  
Chuang-Fu Chen
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
Small Interfering Rna ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Receptor ◽  
Mouth Disease Virus ◽  
Rna Targeting ◽  
Foot And Mouth ◽  
Interfering Rna

scholarly journals The DDX23 Negatively Regulates Translation and Replication of Foot-and-Mouth Disease Virus and Is Degraded by 3C Proteinase

Viruses ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 1348
Author(s):  
Sahibzada Waheed Abdullah ◽  
Shichong Han ◽  
Jin’en Wu ◽  
Yun Zhang ◽  
Manyuan Bai ◽  
...  
Keyword(s):  
Disease Virus ◽  
Small Interfering Rna ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Dependent Manner ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Rna Knockdown ◽  
Interfering Rna ◽  
Fmdv Replication

DEAD-box helicase 23 (DDX23) is a host nuclear helicase, which is a part of the spliceosomal complex and involved in pre-mRNA splicing. To investigate whether DDX23, an internal ribosomal entry sites transacting factor (ITAF) affects foot-and-mouth disease virus (FMDV) replication and translation through internal ribosome entry site (IRES)-dependent manner. For this, we utilized a pull-down assay, Western blotting, quantitative real-time PCR, confocal microscopy, overexpression and small interfering RNA knockdown, as well as the median tissue culture infective dose. Our findings showed that FMDV infection inhibited DDX23 expression and the overexpression of DDX23 reduced viral replication, however, CRISPR Cas9 knockout/small interfering RNA knockdown increased FMDV replication. FMDV IRES domain III and IV interacted with DDX23, whereas DDX23 interacted with FMDV 3C proteinase and significantly degraded. The enzymatic activity of FMDV 3C proteinase degraded DDX23, whereas FMDV degraded DDX23 via the lysosomal pathway. Additionally, IRES-driven translation was suppressed in DDX23-overexpressing cells, and was enhanced in DDX23 knocked down. Collectively, our results demonstrated that DDX23 negatively affects FMDV IRES-dependent translation, which could be a useful target for the design of antiviral drugs.

scholarly journals Foot-and-mouth disease virus utilizes an autophagic pathway during viral replication

Virology ◽  
2011 ◽  
Vol 410 (1) ◽  
pp. 142-150 ◽  
Author(s):  
Vivian O'Donnell ◽  
Juan M. Pacheco ◽  
Michael LaRocco ◽  
Tom Burrage ◽  
William Jackson ◽  
...  
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals The Ability of Integrin αvβ3 To Function as a Receptor for Foot-and-Mouth Disease Virus Is Not Dependent on the Presence of Complete Subunit Cytoplasmic Domains

2001 ◽  
Vol 75 (1) ◽  
pp. 527-532 ◽  
Author(s):  
Sherry Neff ◽  
Barry Baxt
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
High Efficiency ◽  
Cultured Cells ◽  
Foot And Mouth Disease ◽  
Integrin Αvβ3 ◽  
Mouth Disease ◽  
Cytoplasmic Domains ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT The integrin αvβ3 has been shown to function as one of the integrin receptors on cultured cells for foot-and-mouth disease virus (FMDV), and high-efficiency utilization of the bovine homolog of this integrin is dependent on the cysteine-rich repeat region of the bovine β3 subunit. In this study we have examined the role of the cytoplasmic domains of the αv and β3 subunits in FMDV infection. We have found that truncations or extensions of these domains of either subunit, including deletions removing almost all of the cytoplasmic domains, had little or no effect on the ability of the integrin to function as a receptor for FMDV. The lysosomotropic agent monensin inhibited viral replication in cells transfected with either intact or cytoplasmic domain-truncated αvβ3. In addition, viral replication in transfected cells was inhibited by an αvβ3 function-blocking antibody but not by function-blocking antibodies to three other RGD-directed integrins, suggesting that these integrins are not involved in the infectious process. These results indicate that alterations to the cytoplasmic domains of either subunit, which lead to the inability of the integrin receptor to function normally, do not abolish the ability of the integrin to bind and internalize this viral ligand.

scholarly journals Identification of Short Hairpin RNA Targeting Foot-And-Mouth Disease Virus with Transgenic Bovine Fetal Epithelium Cells

PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e42356 ◽  
Author(s):  
Hongmei Wang ◽  
Jianming Wu ◽  
Xiao Liu ◽  
Hongbin He ◽  
Fangrong Ding ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Short Hairpin Rna ◽  
Mouth Disease ◽  
Hairpin Rna ◽  
Mouth Disease Virus ◽  
Rna Targeting ◽  
Foot And Mouth ◽  
Short Hairpin ◽  
Epithelium Cells

scholarly journals Foot-and-mouth disease virus virulence in cattle is co-determined by viral replication dynamics and route of infection

Virology ◽  
2014 ◽  
Vol 452-453 ◽  
pp. 12-22 ◽  
Author(s):  
Jonathan Arzt ◽  
Juan M. Pacheco ◽  
George R. Smoliga ◽  
Meghan T. Tucker ◽  
Elizabeth Bishop ◽  
...  
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Route Of Infection ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Use of Confocal Immunofluorescence Microscopy To Localize Viral Nonstructural Proteins and Potential Sites of Replication in Pigs Experimentally Infected with Foot-and-Mouth Disease Virus

2005 ◽  
Vol 79 (10) ◽  
pp. 6410-6418 ◽  
Author(s):  
P. Monaghan ◽  
J. Simpson ◽  
C. Murphy ◽  
S. Durand ◽  
M. Quan ◽  
...  
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Rt Pcr ◽  
Tissue Samples ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Immunofluorescence Labeling

ABSTRACT Replication of foot-and-mouth disease virus in infected pig epithelium has been studied by immunofluorescence labeling of the viral nonstructural protein 3ABC and confocal microscopy. The results were correlated with viral RNA copy numbers in tissue samples from adjacent sites determined by reverse transcription-PCR (RT-PCR). Lesion formation was seen in the tongues and coronary band epithelia of infected pigs 2 days after infection. Viral replication was observed in cells of the epithelium of the tongue and coronary band but not in the associated stromal cells. Infected epithelial cells were present in the stratum spinosum, away from the lesion, with small lesions formed above the basement membrane. Viral replication was markedly reduced in tongue epithelium by day 3 postinfection but remained apparent in the coronary band tissue up to 5 days postinfection. These results were confirmed by the RNA copy number determined by RT-PCR.

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