The first full genome characterization of an Iranian foot and mouth disease virus

Najafi, Hamideh; FallahMehrabadi, Mohammad Hossein; Hosseini, Hossein; Kafi, Zahra Ziafati; Hamdan, Amir Modiri; Ghalyanchilangeroudi, Arash

doi:10.1016/j.virusres.2020.197888

Cited by 4 publications

(3 citation statements)

References 37 publications

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“…Similarly, VP2 can boost virus replication by interacting with Heat Shock Protein Family B member 1 (HSPB1), which activates the EIF2S1-ATF4 pathway, ultimately promoting autophagy and enhanced virus replication [ 57 ]. The VP2 of the FMDV is smaller compared to the VP2 found in other picornaviruses [ 58 , 59 ]. VP2 N-terminal amino acids within three adjacent pentamers are organized at each three-fold symmetrical axis of the capsid to form a tightly bound C-shaped structure, which serves as a calcium-binding site [ 12 ].…”

Section: Adaptive Amino Acid Substitutions In Capsid Proteinsmentioning

confidence: 99%

Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism

Mushtaq,

Shah,

Zarlashat

et al. 2024

Viruses

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The foot-and-mouth disease virus is a highly contagious and economically devastating virus of cloven-hooved animals, including cattle, buffalo, sheep, and goats, causing reduced animal productivity and posing international trade restrictions. For decades, chemically inactivated vaccines have been serving as the most effective strategy for the management of foot-and-mouth disease. Inactivated vaccines are commercially produced in cell culture systems, which require successful propagation and adaptation of field isolates, demanding a high cost and laborious time. Cell culture adaptation is chiefly indebted to amino acid substitutions in surface-exposed capsid proteins, altering the necessity of RGD-dependent receptors to heparan sulfate macromolecules for virus binding. Several amino acid substations in VP1, VP2, and VP3 capsid proteins of FMDV, both at structural and functional levels, have been characterized previously. This literature review combines frequently reported amino acid substitutions in virus capsid proteins, their critical roles in virus adaptation, and functional characterization of the substitutions. Furthermore, this data can facilitate molecular virologists to develop new vaccine strains against the foot-and-mouth disease virus, revolutionizing vaccinology via reverse genetic engineering and synthetic biology.

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Section: Adaptive Amino Acid Substitutions In Capsid Proteinsmentioning

confidence: 99%

Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism

Mushtaq,

Shah,

Zarlashat

et al. 2024

Viruses

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“…Foot and mouth disease (FMD) is caused by a virus (FMD virus) that contains positive-strand ribonucleic acid (RNA) and belongs to the genus Aphthovirus and Picornaviridae family (1). The FMD has highly variable RNA that engenders O, A, C, Asia 1, SAT 1, SAT 2, and SAT 3 serotypes and a wide range of subtypes.…”

Section: Introductionmentioning

confidence: 99%

Restraint of VP1 Protein of Foot and Mouth Disease Virus using Specific Antiviral Peptides: an in Silico Investigation

2023

ARI

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Foot and mouth diseases are among the important threats in the animal husbandry industry which lead to huge economic losses. In this regard, the current project aimed to inhibit the VP1 protein of foot and mouth disease viruses using specific peptides. For this purpose, a wide range of potential antiviral peptides were collected from the database. Physicochemical properties, hydrophobicity/hydrophilicity, and solubility properties of potential antiviral peptides were investigated using reliable servers. Afterward, the tertiary structures of the selected peptides along with the VP1 protein were modeled by the I-TASSER server. Moreover, interactions between VP1 protein and selected antiviral peptides were investigated using the ClusPro 2.0 server. Finally, the outputs of molecular docking were assessed by LigPlot+ and visualized by PyMol software. The results revealed that Dermaseptin-3, Ginkbilobin, Circulin-F, Maximin1, Cycloviolin-A, Cycloviolin-D, Circulin-C, Cycloviolin-C, and Antihypertensive protein BDS-1 peptides with a hydrophobicity value of > 30 were soluble with positive instability index and positive net charge. Moreover, the results of the molecular docking process demonstrated that Dermaseptin-3 and Ginkbilobin peptides could strongly inhibit the VP1 protein using 10 hydrogen bonds. Therefore, these two peptides, which had the most hydrogen bonds, were introduced as the best anti-foot and mouth disease virus peptides to apply.

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“…Type A, O, and C FMDV phylogenetic trees primarily rely on the VP1 gene's nucleotide sequence, with VP1-based phylogenetic grouping correlating with classical serological classification [6][7][8]. Furthermore, the VP1-encoded nucleotide sequence is pivotal for FMDV characterization and phylogenetic analysis of capsid constituents [9][10][11]. According to Jamal et al [4], FMDV comprises seven serotypes (O, A, C, Asia-1, SAT-1, SAT-2, and SAT-3).…”

Section: Introductionmentioning

confidence: 99%

Designing one-step reverse transcriptase loop-mediated isothermal amplification for serotype O foot-and-mouth disease virus detection during the 2022 outbreak in East Java, Indonesia

Aksono,

Lamid,

Rimayanti

et al. 2023

Vet World

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Background and Aim: Various methods can detect foot-and-mouth disease (FMD) in cows, but they necessitate resources, time, costs, laboratory facilities, and specific clinical specimen submission, often leading to FMD virus (FMDV) diagnosis delays. The 2022 FMD outbreak in East Java, Indonesia, highlighted the need for an easy, inexpensive, rapid, and accurate detection approach. This study aims to devise a one-step reverse transcriptase loop-mediated isothermal amplification (RT-LAMP) technique and phylogenetic analysis to detect the serotype O FMDV outbreak in East Java. Materials and Methods: Swab samples were collected from the foot vesicles, nasal secretions, and saliva of five suspected FMDV-infected cows in East Java between June and July 2022. The RT-LAMP design used hydroxy naphthol blue dye or SYBR Green I dye, with confirmatory analysis through reverse transcriptase polymerase chain reaction (RT-PCR) targeting 249 base pairs. PCR products underwent purification, sequencing, and nucleotide alignment, followed by phylogenetic analysis. Results: The RT-LAMP method using hydroxy naphthol blue dye displayed a positive reaction through a color shift from purple to blue in the tube. Naked-eye observation in standard light or ultraviolet (UV) light at 365 nm, with SYBR Green I stain, also revealed color change. Specifically, using SYBR Green I dye, UV light at 365 nm revealed a color shift from yellow to green, signifying a positive reaction. Nucleotide alignment revealed mutations and deletion at the 15th sequence in the JT-INDO-K3 isolate from the East Java FMDV outbreak. Despite differing branches, the phylogenetic tree placed it in the same cluster as serotype O FMDV from Malaysia and Mongolia. Conclusion: JT-INDO-K3 exhibited distinctions from Indonesian serotype O FMDV isolates and those documented in GenBank. Then, the RT-LAMP method used in this study has a detection limit 10 times higher latter than the conventional RT-PCR limit, without any cross-reactivity among strains. Keywords: cow, East Java, foot-and-mouth disease virus, reverse transcriptase loop-mediated isothermal amplification, reverse transcriptase polymerase chain reaction, serotype O.

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The first full genome characterization of an Iranian foot and mouth disease virus

Cited by 4 publications

References 37 publications

Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism

Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism

Restraint of VP1 Protein of Foot and Mouth Disease Virus using Specific Antiviral Peptides: an in Silico Investigation

Designing one-step reverse transcriptase loop-mediated isothermal amplification for serotype O foot-and-mouth disease virus detection during the 2022 outbreak in East Java, Indonesia

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