Estudios evolutivos y moleculares en el género Pestivirus

2003 ◽  
Author(s):  
◽  
Leandro Roberto Jones
Keyword(s):  
Hepatitis C ◽  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Hog Cholera ◽  
Hog Cholera Virus ◽  
Type 3

El género Pestivirus pertenece a la familia Flaviviridae, la cual también incluye a los géneros Flavivirus y Hepacivirus (Virus de la Hepatitis C). Dentro del género Pestivirus hay cuatro especies reconocidas por el Comité Internacional de Taxonomía de Virus (ICTV). Estas son Bovine Viral Diarrea Virus 1 (=BVDV 1, Pestivirus Type 1), Bovine Viral Diarrea 2 (=BVDV 2, Pestivirus Type 4), Classical Swine Fever Virus (=Pestivirus Type 2, Hog Cholera Virus, CSFV) y Border Desease Virus (=Pestivirus Type 3, BDV). Como los nombres sugieren, BVDV 1 y BVDV 2 infectan principalmente ganado bovino.

scholarly journals Analysis of hepatitis C virus/classical swine fever virus chimeric 5′NTRs: sequences within the hepatitis C virus IRES are required for viral RNA replication

2003 ◽  
Vol 84 (7) ◽  
pp. 1761-1769 ◽  
Author(s):  
Chantal B. E. M. Reusken ◽  
Tim J. Dalebout ◽  
Peter Eerligh ◽  
Peter J. Bredenbeek ◽  
Willy J. M. Spaan
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Rna Replication ◽  
Fever Virus ◽  
Viral Rna

scholarly journals Generation and Immunogenicity of a Recombinant Pseudorabies Virus Co-Expressing Classical Swine Fever Virus E2 Protein and Porcine Circovirus Type 2 Capsid Protein Based on Fosmid Library Platform

Pathogens ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 279
Author(s):  
Muhammad Abid ◽  
Teshale Teklue ◽  
Yongfeng Li ◽  
Hongxia Wu ◽  
Tao Wang ◽  
...  
Keyword(s):  
Classical Swine Fever Virus ◽  
Pseudorabies Virus ◽  
Classical Swine Fever ◽  
Porcine Circovirus Type ◽  
Porcine Circovirus Type 2 ◽  
Fosmid Library ◽  
Fever Virus ◽  
Porcine Circovirus ◽  
Live Virus

Pseudorabies (PR), classical swine fever (CSF), and porcine circovirus type 2 (PCV2)-associated disease (PCVAD) are economically important infectious diseases of pigs. Co-infections of these diseases often occur in the field, posing significant threat to the swine industry worldwide. gE/gI/TK-gene-deleted vaccines are safe and capable of providing full protection against PR. Classical swine fever virus (CSFV) E2 glycoprotein is mainly used in the development of CSF vaccines. PCV2 capsid (Cap) protein is the major antigen targeted for developing PCV2 subunit vaccines. Multivalent vaccines, and especially virus-vectored vaccines expressing foreign proteins, are attractive strategies to fight co-infections for various swine diseases. The gene-deleted pseudorabies virus (PRV) can be used to develop promising and economical multivalent live virus-vectored vaccines. Herein, we constructed a gE/gI/TK-gene-deleted PRV co-expressing E2 of CSFV and Cap of PCV2 by fosmid library platform established for PRV, and the expression of E2 and Cap proteins was confirmed using immunofluorescence assay and western blotting. The recombinant virus propagated in porcine kidney 15 (PK-15) cells for 20 passages was genetically stable. The evaluation results in rabbits and pigs demonstrate that rPRVTJ-delgE/gI/TK-E2-Cap elicited detectable anti-PRV antibodies, but not anti-PCV2 or anti-CSFV antibodies. These findings provide insights that rPRVTJ-delgE/gI/TK-E2-Cap needs to be optimally engineered as a promising trivalent vaccine candidate against PRV, PCV2 and CSFV co-infections in future.

scholarly journals Influence of PPV, PRV and PRRSV on Efficacy of the Lapinized Hog Cholera Vaccine and Pathogenicity of Classical swine fever virus

2012 ◽  
Vol 11 (11) ◽  
pp. 1892-1897
Author(s):  
Yi-bao NING ◽  
Yun ZHAO ◽  
Qin WANG ◽  
Xue-zheng FAN ◽  
Yu-ming QIN ◽  
...  
Keyword(s):  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Cholera Vaccine ◽  
Hog Cholera

scholarly journals Specific Interaction of Eukaryotic Translation Initiation Factor 3 with the 5′ Nontranslated Regions of Hepatitis C Virus and Classical Swine Fever Virus RNAs

1998 ◽  
Vol 72 (6) ◽  
pp. 4775-4782 ◽  
Author(s):  
Daria V. Sizova ◽  
Victoria G. Kolupaeva ◽  
Tatyana V. Pestova ◽  
Ivan N. Shatsky ◽  
Christopher U. T. Hellen
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Classical Swine Fever Virus ◽  
Specific Interaction ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Domain Iii ◽  
Hcv Ires

ABSTRACT Translation of hepatitis C virus (HCV) and classical swine fever virus (CSFV) RNAs is initiated by cap-independent attachment (internal entry) of ribosomes to the ∼350-nucleotide internal ribosomal entry segment (IRES) at the 5′ end of both RNAs. Eukaryotic initiation factor 3 (eIF3) binds specifically to HCV and CSFV IRESs and plays an essential role in the initiation process on them. Here we report the results of chemical and enzymatic footprinting analyses of binary eIF3-IRES complexes, which have been used to identify the eIF3 binding sites on HCV and CSFV IRESs. eIF3 protected an internal bulge in the apical stem IIIb of domain III of the CSFV IRES from chemical modification and protected bonds in and adjacent to this bulge from cleavage by RNases ONE and V1. eIF3 protected an analagous region in domain III of the HCV IRES from cleavage by these enzymes. These results are consistent with the results of primer extension analyses and were supported by observations that deletion of stem-loop IIIb or of the adjacent hairpin IIIc from the HCV IRES abrogated the binding of eIF3 to this RNA. This is the first report that eIF3 is able to bind a eukaryotic mRNA in a sequence- or structure-specific manner. UV cross-linking of eIF3 to [32P]UTP-labelled HCV and CSFV IRES elements resulted in strong labelling of 4 (p170, p116, p66, and p47) of the 10 subunits of eIF3, 1 or more of which are likely to be determinants of these interactions. In the cytoplasm, eIF3 is stoichiometrically associated with free 40S ribosomal subunits. The results presented here are consistent with a model in which binding of these two translation components to separate, specific sites on both HCV and CSFV IRESs enhances the efficiency and accuracy of binding of these RNAs to 40S subunits in an orientation that promotes entry of the initiation codon into the ribosomal P site.

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