scholarly journals Molecular characterization of a 13-amino acid deletion in VP1 (1D) protein and novel amino acid substitutions in 3D polymerase protein of foot and mouth disease virus subtype A/Iran87

2011 ◽  
Vol 12 (4) ◽  
pp. 363 ◽  
Author(s):  
Majid Esmaelizad ◽  
Saber Jelokhani-Niaraki ◽  
Khadije Hashemnejad ◽  
Morteza Kamalzadeh ◽  
Mohsen Lotfi
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Amino Acid Substitutions ◽  
Amino Acid Deletion ◽  
Mouth Disease Virus ◽  
Subtype A ◽  
Virus Subtype

scholarly journals Sequence and phylogenetic analysis of the non-structural 3A and 3B protein-coding regions of foot-and-mouth disease virus subtype A Iran 05

2010 ◽  
Vol 11 (3) ◽  
pp. 243
Author(s):  
Saber Jelokhani-Niaraki ◽  
Majid Esmaelizad ◽  
Morteza Daliri ◽  
Rasoul Vaez-Torshizi ◽  
Morteza Kamalzadeh ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Protein Coding ◽  
Coding Regions ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Subtype A ◽  
Virus Subtype

scholarly journals Molecular Characterization of Foot-and-Mouth Disease Virus Type C of Indian Origin

2005 ◽  
Vol 43 (2) ◽  
pp. 966-969 ◽  
Author(s):  
S. B. Nagendrakumar ◽  
G. S. Reddy ◽  
D. Chandran ◽  
D. Thiagarajan ◽  
P. N. Rangarajan ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Disease Virus ◽  
Virus Type ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Indian Origin ◽  
Mouth Disease Virus ◽  
Disease Virus Type ◽  
Type C

scholarly journals Seroprevalence and molecular characterization of foot‐and‐mouth disease virus in Chad

2019 ◽  
Vol 6 (1) ◽  
pp. 114-121
Author(s):  
Arada Izzedine Abdel‐Aziz ◽  
Aurore Romey ◽  
Anthony Relmy ◽  
Kamila Gorna ◽  
Eve Laloy ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
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.

Emerging foot-and-mouth disease virus variants with antigenically critical amino acid substitutions predicted by model studies using reference viruses

Vaccine ◽  
1996 ◽  
Vol 14 (2) ◽  
pp. 97-102 ◽  
Author(s):  
Dino A. Feigelstock ◽  
Mauricio G. Mateu ◽  
M. Luz Valero ◽  
David Andreu ◽  
Esteban Domingo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Amino Acid Substitutions ◽  
Model Studies ◽  
Critical Amino Acid ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals ISOLATION AND MOLECULAR CHARACTERIZATION OF FOOT AND MOUTH DISEASE VIRUS IN KAFRELSHEIKH GOVERNORATE, EGYPT 2014

2015 ◽  
Vol 13 (2) ◽  
pp. 17-35
Author(s):  
Samy Kasem ◽  
Asmaa Magouz ◽  
G. Fekry EL- Bagoury ◽  
Magdy Abdelaty ◽  
Abeer Zaghlol
Keyword(s):  
Molecular Characterization ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth
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