scholarly journals Common Host Factors Involved in the Function of the Foot-and-mouth Disease Virus and Classical Swine Fever Virus Internal Ribosomal Entry Sites

2021 ◽  
Author(s):  
Yutaro Ide ◽  
Nobumasa Ito ◽  
Takafumi Matsui ◽  
Kyoko Tsukiyama-Kohara
Keyword(s):  
Disease Virus ◽  
Classical Swine Fever Virus ◽  
Foot And Mouth Disease ◽  
Classical Swine Fever ◽  
Host Factor ◽  
Mouth Disease ◽  
Fever Virus ◽  
Host Factors ◽  
Mouth Disease Virus ◽  
Ires Element

Abstract Foot-and-mouth disease virus (FMDV) and classical swine fever virus (CSFV) both possess positive strand RNA genomes and an internal ribosomal entry site (IRES) element within their 5¢-untranslated regions. To identify common host factors involved with the activity of these IRESes, we utilized cell lines expressing a bicistronic luciferase reporter plasmid, which contained an FMDV-IRES or CSFV-IRES element between the Renilla and firefly luciferase genes. First, we treated FMDV-IRES cells with French maritime pine extract, Pycnogenol® (PYC), and evaluated its suppressive effect on FMDV-IRES activity, as anti-viral effect of PYC was reported so far. We next performed microarray analysis to identify host factors affected by PYC, and confirmed host-factor-IRES interaction by applying host factor-specific siRNAs. We found that polycystic kidney disease 1-like 3 (PKD1L3) and ubiquitin specific peptidase 31 (USP31) are involved in FMDV-IRES activity. Moreover, silencing of these factors also significantly suppressed CSFV-IRES activity. Accordingly, we suggest that PKD1L3 and USP31 are host factors that are involved in the function of the FMDV and CSFV-IRES elements.

Establishment of multiple RT-PCR diagnostic techniques forAvian influenza virus(AIV),Newcastle disease virus(NDV),Classical swine fever virus(CSFV) andFoot-and-mouth disease virus(FMDV)

2005 ◽  
Vol 2 (3) ◽  
pp. 161-165
Author(s):  
Liu Wei-Quan ◽  
Liu Hai-Peng ◽  
Jiang Yu ◽  
Wang Ben-Xu ◽  
Wang Ji-Gui ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Classical Swine Fever Virus ◽  
Newcastle Disease ◽  
Classical Swine Fever ◽  
Mouth Disease ◽  
Fever Virus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Mouth Disease Virus

AbstractThe homology of the sequences, reported and registered in GenBank, of different strains ofAvian influenza virus(AIV),Newcastle disease virus(NDV),Classical swine fever virus(CSFV) andFoot-and-mouth disease virus(FMDV), was analysed and compared with each other. According to the properties of these viruses, the conservative domain of theMgene for AIV, theFgene for NDV, the 5' non-coding domain end for CSFV and the2Bgene for FMDV were selected for polymerase chain reaction (PCR) amplification. In order to prevent the formation of conformational dimers between different primers, four pairs of primers designed with the DNAsis system under the condition of G+C (50–60%),18–25 bp in length andTm(72–85), were analysed using the VNTI5.5 system. The specific fragments amplified were as follows: 141 bp for FMDV, 200 bp for CSFV, 319 bp for NDV and 471 bp for AIV. The optimal conditions of PCR for each virus mentioned above were determined by orthogonal assay, and two or four of the four pairs of primers were then combined and used for amplification trials. The results showed that four specific fragments of different lengths would be successfully amplified in one tube at the same time. The products of PCR were tested to be specific by sequencing. Out of 46 pathological samples detected with the multiple PCR, there were 5 AIVs, 7 NDVs, 15 CSFVs and 6 FMDVs. The amplification above was identified with a single PCR. On the other hand, the results corresponded to those of electronic microscopy, haemagglutination (HA) and enzyme-linked immunosorbent assay (ELISA). The method described here is practicable, sensitive, specific, simple and cheap. It could be used for diagnosing AIV, NDV, CSFV and FMDV in different animals.

scholarly journals The 3′ end of the foot-and-mouth disease virus genome establishes two distinct long-range RNA–RNA interactions with the 5′ end region

2006 ◽  
Vol 87 (10) ◽  
pp. 3013-3022 ◽  
Author(s):  
Paula Serrano ◽  
Miguel Rodriguez Pulido ◽  
Margarita Sáiz ◽  
Encarnacion Martínez-Salas
Keyword(s):  
Disease Virus ◽  
Long Range ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Order Structure ◽  
Entry Site ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Ires Element ◽  
Rna Interaction

The untranslated regions (UTRs) of the foot-and-mouth disease virus (FMDV) genome contain multiple functional elements. In the 5′ UTR, the internal ribosome entry site (IRES) element governs cap-independent translation initiation, whereas the S region is presumably involved in RNA replication. The 3′ UTR, composed of two stem–loops and a poly(A) tract, is required for viral infectivity and stimulates IRES activity. Here, it was found that the 3′ end established two distinct strand-specific, long-range RNA–RNA interactions, one with the S region and another with the IRES element. These interactions were not observed with the 3′ UTR of a different picornavirus. Several results indicated that different 3′ UTR motifs participated in IRES or S region interactions. Firstly, a high-order structure adopted by both the entire IRES and the 3′ UTR was essential for RNA interaction. In contrast, the S region interacted with each of the stem–loops. Secondly, S–3′ UTR interaction but not IRES–3′ UTR interaction was dependent on a poly(A)-dependent conformation. However, no other complexes were observed in mixtures containing the three transcripts, suggesting that these regions did not interact simultaneously with the 3′ UTR probe. Cellular proteins have been found to bind the S region and one of these also binds to the 3′ UTR in a competitive manner. Our data suggest that 5′–3′-end bridging through both direct RNA–RNA contacts and RNA–protein interactions may play an essential role in the FMDV replication cycle.

High resolution surface structure of foot-and-mouth disease virus

1978 ◽  
Vol 36 (2) ◽  
pp. 376-377
Author(s):  
S. S. Breese ◽  
H. L. Bachrach
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Surface Structure ◽  
Disease Virus ◽  
Potassium Phosphate ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Physical Measurements ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Models for the structure of foot-and-mouth disease virus (FMDV) have been proposed from chemical and physical measurements (Brown, et al., 1970; Talbot and Brown, 1972; Strohmaier and Adam, 1976) and from rotational image-enhancement electron microscopy (Breese, et al., 1965). In this report we examine the surface structure of FMDV particles by high resolution electron microscopy and compare it with that of particles in which the outermost capsid protein VP3 (ca. 30, 000 daltons) has been split into smaller segments, two of which VP3a and VP3b have molecular weights of about 15, 000 daltons (Bachrach, et al., 1975).Highly purified and concentrated type A12, strain 119 FMDV (5 mg/ml) was prepared as previously described (Bachrach, et al., 1964) and stored at 4°C in 0. 2 M KC1-0. 5 M potassium phosphate buffer at pH 7. 5. For electron microscopy, 1. 0 ml samples of purified virus and trypsin-treated virus were dialyzed at 4°C against 0. 2 M NH4OAC at pH 7. 3, deposited onto carbonized formvar-coated copper screens and stained with phosphotungstic acid, pH 7. 3.

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