scholarly journals Foot‐and‐mouth disease virus nonstructural protein 2B interacts with cyclophilin A, modulating virus replication

2018 ◽  
Vol 32 (12) ◽  
pp. 6706-6723 ◽  
Author(s):  
Huisheng Liu ◽  
Qiao Xue ◽  
Weijun Cao ◽  
Fan Yang ◽  
Linna Ma ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Cyclophilin A ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Foot-and-Mouth Disease Virus Nonstructural Protein 2C Interacts with Beclin1, Modulating Virus Replication

2012 ◽  
Vol 86 (22) ◽  
pp. 12080-12090 ◽  
Author(s):  
D. P. Gladue ◽  
V. O'Donnell ◽  
R. Baker-Branstetter ◽  
L. G. Holinka ◽  
J. M. Pacheco ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Erratum to: The carboxy-terminal half of nonstructural protein 3A is not essential for foot-and-mouth disease virus replication in cultured cell lines

2016 ◽  
Vol 161 (5) ◽  
pp. 1307-1307
Author(s):  
Mrutyunjay Behura ◽  
Jajati K. Mohapatra ◽  
Laxmi K. Pandey ◽  
Biswajit Das ◽  
Mukesh Bhatt ◽  
...  
Keyword(s):  
Disease Virus ◽  
Cell Lines ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Cultured Cell ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Carboxy Terminal

The carboxy-terminal half of nonstructural protein 3A is not essential for foot-and-mouth disease virus replication in cultured cell lines

2016 ◽  
Vol 161 (5) ◽  
pp. 1295-1305 ◽  
Author(s):  
Mrutyunjay Behura ◽  
Jajati K. Mohapatra ◽  
Laxmi K. Pandey ◽  
Biswajit Das ◽  
Mukesh Bhatt ◽  
...  
Keyword(s):  
Disease Virus ◽  
Cell Lines ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Cultured Cell ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Carboxy Terminal

T135I substitution in the nonstructural protein 2C enhances foot-and-mouth disease virus replication

Virus Genes ◽  
2017 ◽  
Vol 53 (6) ◽  
pp. 840-847 ◽  
Author(s):  
Tiangang Yuan ◽  
Haiwei Wang ◽  
Chen Li ◽  
Decheng Yang ◽  
Guohui Zhou ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Cellular Vimentin Interacts with Foot-and-Mouth Disease Virus Nonstructural Protein 3A and Negatively Modulates Viral Replication

2020 ◽  
Vol 94 (16) ◽  
Author(s):  
Xueqing Ma ◽  
Ying Ling ◽  
Pinghua Li ◽  
Pu Sun ◽  
Yimei Cao ◽  
...  
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Amino Acid Residues ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Fmdv Replication

ABSTRACT Nonstructural protein 3A of foot-and-mouth disease virus (FMDV) is a partially conserved protein of 153 amino acids that is in most FMDVs examined to date, and it plays important roles in virus replication, virulence, and host range. To better understand the role of 3A during FMDV infection, we used coimmunoprecipitation followed by mass spectrometry to identify host proteins that interact with 3A in FMDV-infected cells. Here, we report that cellular vimentin is a host binding partner for 3A. The 3A-vimentin interaction was further confirmed by coimmunoprecipitation, glutathione S-transferase (GST) pull down, and immunofluorescence assays. Alanine-scanning mutagenesis indicated that amino acid residues 15 to 21 at the N-terminal region of the FMDV 3A are responsible for the interaction between 3A and vimentin. Using reverse genetics, we demonstrate that mutations in 3A that disrupt the interaction between 3A and vimentin are also critical for virus growth. Overexpression of vimentin significantly suppressed the replication of FMDV, whereas knockdown of vimentin significantly enhanced FMDV replication. However, chemical disruption of the vimentin network by acrylamide resulted in a significant decrease in viral yield, suggesting that an intact vimentin network is needed for FMDV replication. These results indicate that vimentin interacts with FMDV 3A and negatively regulates FMDV replication and that the vimentin-3A interaction is essential for FMDV replication. This study provides information that should be helpful for understanding the molecular mechanism of FMDV replication. IMPORTANCE Foot-and-mouth disease virus (FMDV) nonstructural protein 3A plays important roles in virus replication, host range, and virulence. To further understand the role of 3A during FMDV infection, identification of host cell factors that interact with FMDV 3A is needed. Here, we found that vimentin is a direct binding partner of FMDV 3A, and manipulation of vimentin has a negative effect on virus replication. We also demonstrated that amino acid residues 15 to 21 at the N-terminal region of the FMDV 3A are responsible for the interaction between 3A and vimentin and that the 3A-vimentin interaction is critical for viral replication since the full-length cDNA clone harboring mutations in 3A, which were disrupt 3A-vimentin reactivity, could not produce viable virus progeny. This study provides information that not only provides us a better understanding of the mechanism of FMDV replication but also helps in the development of novel antiviral strategies in the future.

Gold Nanoparticles Impair Foot-and-Mouth Disease Virus Replication

2016 ◽  
Vol 15 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Solmaz Rafiei ◽  
Seyedeh Elham Rezatofighi ◽  
Mohammad Roayaei Ardakani ◽  
Saadat Rastegarzadeh
Keyword(s):  
Gold Nanoparticles ◽  
Disease Virus ◽  
Virus Replication ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Delivery of a foot-and-mouth disease virus empty capsid subunit antigen with nonstructural protein 2B improves protection of swine

Vaccine ◽  
2008 ◽  
Vol 26 (45) ◽  
pp. 5689-5699 ◽  
Author(s):  
Lindomar Pena ◽  
Mauro Pires Moraes ◽  
Marla Koster ◽  
Thomas Burrage ◽  
Juan M. Pacheco ◽  
...  
Keyword(s):  
Disease Virus ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Modifications to the Foot-and-Mouth Disease Virus 2A Peptide: Influence on Polyprotein Processing and Virus Replication

2018 ◽  
Vol 92 (8) ◽  
Author(s):  
Jonas Kjær ◽  
Graham J. Belsham
Keyword(s):  
Amino Acid ◽  
Disease Virus ◽  
Virus Replication ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Amino Acid Substitutions ◽  
2A Peptide ◽  
Polyprotein Processing ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACTFoot-and-mouth disease virus (FMDV) has a positive-sense single-stranded RNA (ssRNA) genome that includes a single, large open reading frame encoding a polyprotein. The cotranslational “cleavage” of this polyprotein at the 2A/2B junction is mediated by the 2A peptide (18 residues in length) using a nonproteolytic mechanism termed “ribosome skipping” or “StopGo.” Multiple variants of the 2A polypeptide with this property among the picornaviruses share a conserved C-terminal motif [D(V/I)E(S/T)NPG↓P]. The impact of 2A modifications within this motif on FMDV protein synthesis, polyprotein processing, and virus viability were investigated. Amino acid substitutions are tolerated at residues E14, S15, and N16within the 2A sequences of infectious FMDVs despite their reported “cleavage” efficiencies at the 2A/2B junction of only ca. 30 to 50% compared to that of the wild type (wt). In contrast, no viruses containing substitutions at residue P17, G18, or P19, which displayed little or no “cleavage” activityin vitro, were rescued, but wt revertants were obtained. The 2A substitutions impaired the replication of an FMDV replicon. Using transient-expression assays, it was shown that certain amino acid substitutions at residues E14, S15, N16, and P19resulted in partial “cleavage” of a protease-free polyprotein, indicating that these specific residues are not essential for cotranslational “cleavage.” Immunofluorescence studies, using full-length FMDV RNA transcripts encoding mutant 2A peptides, indicated that the 2A peptide remained attached to adjacent proteins, presumably 2B. These results show that efficient “cleavage” at the 2A/2B junction is required for optimal virus replication. However, maximal StopGo activity does not appear to be essential for the viability of FMDV.IMPORTANCEFoot-and-mouth disease virus (FMDV) causes one of the most economically important diseases of farm animals. Cotranslational “cleavage” of the FMDV polyprotein precursor at the 2A/2B junction, termed StopGo, is mediated by the short 2A peptide through a nonproteolytic mechanism which leads to release of the nascent protein and continued translation of the downstream sequence. Improved understanding of this process will not only give a better insight into how this peptide influences the FMDV replication cycle but may also assist the application of this sequence in biotechnology for the production of multiple proteins from a single mRNA. Our data show that single amino acid substitutions in the 2A peptide can have a major influence on viral protein synthesis, virus viability, and polyprotein processing. They also indicate that efficient “cleavage” at the 2A/2B junction is required for optimal virus replication. However, maximal StopGo activity is not essential for the viability of FMDV.

Analysis of foot-and-mouth disease virus replication using strand-specific quantitative RT-PCR

2007 ◽  
Vol 144 (1-2) ◽  
pp. 149-155 ◽  
Author(s):  
Jacquelyn Horsington ◽  
Zhidong Zhang
Keyword(s):  
Disease Virus ◽  
Virus Replication ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Rt Pcr ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Diagnostic potential of recombinant nonstructural protein 3B to detect antibodies induced by foot-and-mouth disease virus infection in bovines

2014 ◽  
Vol 159 (9) ◽  
pp. 2359-2369 ◽  
Author(s):  
Amiya Kumar Mohapatra ◽  
Jajati Keshari Mohapatra ◽  
Laxmi Kant Pandey ◽  
Aniket Sanyal ◽  
Bramhadev Pattnaik
Keyword(s):  
Virus Infection ◽  
Disease Virus ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Diagnostic Potential ◽  
Mouth Disease Virus ◽  
Foot And Mouth
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