Identification of novel interactions between host and non-structural protein 2C of foot-and-mouth disease virus

2021 ◽  
Author(s):  
Sonalika Mahajan ◽  
Gaurav Kumar Sharma ◽  
Kavita Bora ◽  
Bramhadev Pattnaik
Keyword(s):  
Disease Virus ◽  
Critical Role ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Structural Protein ◽  
Host Proteins ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Novel Interactions ◽  
Two Hybrid

The 2C protein of foot-and-mouth disease virus (FMDV) is reported to play a critical role in the virus replication complex and modulating the host’s immune response. However, the underlying molecular intricacies of subversion of cellular machinery remains poorly understood, thus emphasizing the need to study 2C-host interactions. In this study, we identified the host proteins interacting with the 2C using yeast-two hybrid (Y2H) approach, which is one of the most recognized, high-throughput tools to study protein-protein interactions. The FMDV-2C bait was characterized for auto-activation, toxicity, and expression and was found to be suitable for mating with cDNA library. On preliminary screening a total of 32 interacting host proteins were identified which were reduced to 22 on subsequent confirmation with alternative yeast based assays. Amongst these, NMI/2C interaction has been reported earlier by Wang et al. (2012) and remaining 21 are novel interactions. The Reactome analysis has revealed the role of the identified host proteins in cellular pathways exploited by 2C during FMDV replication. We also confirmed interaction of MARCH7, an E3 ubiquitin ligase with 2C using mammalian two-hybrid system and co-immunoprecipitation. This study leads to the identification of novel 2C interacting host proteins which enhance our understanding of 2C-host interface and may provide checkpoints for development of potential therapeutics against FMDV.

scholarly journals Foot-and-mouth disease virus non-structural protein 3A modulates cellular innate immune responses to influence host tropism

2020 ◽  
Vol 2 (7A) ◽  
Author(s):  
Soumendu Chakravarti ◽  
Caroline Wright ◽  
Emma Howes ◽  
Richard Kock ◽  
Terry Jackson ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Economic Losses ◽  
Structural Protein ◽  
Host Tropism ◽  
C Terminus ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Species Specific

The picornavirus foot-and-mouth disease virus (FMDV) is responsible for one of the most significant diseases of livestock, leading to large economic losses due to reduced productivity and trade embargoes for areas not certified as disease-free. The picornavirus non-structural protein 3A is involved in replication of the viral RNA genome and is implicated in host tropism of several picornaviruses. Deletions in the C-terminus of 3A have been observed in FMDV outbreaks specific for swine and such viruses are non-pathogenic in cattle. The mechanism for species specific attenuation of FMDV is unknown. We have shown that FMDV containing a C-terminal deletion in 3A is attenuated in bovine cell culture and that the attenuated phenotype can be reversed by the JAK1/2 inhibitor Ruxolitinib (Rux), identifying a role for the induction of interferon stimulated genes (ISGs) in the restricted bovine tropism of the 3A-deleted virus.

scholarly journals Early origin and global colonisation of foot-and-mouth disease virus

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Pakorn Aiewsakun ◽  
Nakarin Pamornchainavakul ◽  
Chaidate Inchaisri
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Epidemiological Data ◽  
Mouth Disease ◽  
Recent Common Ancestor ◽  
Structural Protein ◽  
Most Recent Common Ancestor ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Early Origin

Abstract In this study, we compiled 84-year worth (1934–2017) of genomic and epidemiological data of foot-and-mouth disease virus (FMDV), and performed comprehensive analyses to determine its early origin and transmission route. We found that recombination is a key feature of FMDV, and that the genomic regions coding for structural and non-structural proteins have markedly different evolutionary histories, and evolve at different rates. Despite all of these differences, analyses of both structural and non-structural protein coding regions consistently suggested that the most recent common ancestor of FMDV could be dated back to the Middle Age, ~ 200 to 300 years earlier than previously thought. The ancestors of the Euro-Asiatic and SAT strains could be dated back to the mid-seventeenth century, and to the mid-fifteenth to mid-sixteenth century, respectively. Our results implicated Mediterranean counties as an early geographical origin of FMDV before spreading to Europe and subsequently to Asia and South America.

scholarly journals Generation of monoclonal antibodies against non-structural protein 3AB of foot-and-mouth disease virus

2012 ◽  
Vol 27 (5) ◽  
pp. 316-319 ◽  
Author(s):  
Tong Lin ◽  
Junjun Shao ◽  
Huiyun Chang ◽  
Shandian Gao ◽  
Guozheng Cong ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Structural Protein ◽  
Mouth Disease Virus ◽  
Foot And Mouth

High expression of foot-and-mouth disease virus structural protein VP1 in tobacco chloroplasts

2005 ◽  
Vol 25 (4) ◽  
pp. 329-333 ◽  
Author(s):  
Yinü Li ◽  
Meng Sun ◽  
Jixing Liu ◽  
Zongqi Yang ◽  
Zhifang Zhang ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
High Expression ◽  
Structural Protein ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals The Kinase STK3 Interacts with the Viral Structural Protein VP1 and Inhibits Foot-and-Mouth Disease Virus Replication

2017 ◽  
Vol 2017 ◽  
pp. 1-8
Author(s):  
Huisheng Liu ◽  
Qiao Xue ◽  
Qiaoying Zeng ◽  
Zixiang Zhu ◽  
Haixue Zheng
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Host Cells ◽  
Cell Protein ◽  
Structural Protein ◽  
New Information ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Fmdv Replication

Foot-and-mouth disease virus (FMDV) is the etiological agent of FMD, which affects domestic and wild cloven-hoofed animals. The structural protein VP1 plays an important role in FMDV pathogenesis. However, the interacting partners of VP1 in host cells and the effects of these interactions in FMDV replication remain incompletely elucidated. Here, we identified a porcine cell protein, serine/threonine kinase 3 (STK3), which interacts with FMDV VP1 using the yeast two-hybrid system. The VP1-STK3 interaction was further confirmed by coimmunoprecipitation experiments in human embryonic kidney 293T and porcine kidney 15 (PK-15) cells. The carboxyl-terminal region (amino acids 180–214) of VP1 was essential for its interaction with STK3. The effects of overexpression and underexpressing of STK3 in PK-15 cells were assessed, and the results indicated that STK3 significantly inhibited FMDV replication. Our data expand the role of STK3 during viral infection, provide new information regarding the host cell kinases that are involved in viral replication, and identify potential targets for future antiviral strategies.

Sign in / Sign up

Export Citation Format

Share Document