Molecular characterization of E2 glycoprotein of classical swine fever virus: adaptation and propagation in porcine kidney cells

Classical swine fever virus (CSFV) is the causative agent of a highly contagious disease, hog cholera in pigs. The disease is endemic in many parts of the world, and vaccination is the only way to protect the animals from CSFV infection. The lapinized vaccine strains are occasionally not protective...

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Published inIn vitro cellular & developmental biology. Animal Vol. 51; no. 5; pp. 441 - 446
Main Authors Kumar, Rakesh, Barman, Nagendra N, Khatoon, Elina, Rajbongshi, Gitika, Deka, Nipu, Morla, Sudhir, Kumar, Sachin
Format Journal Article
LanguageEnglish
Published New York Springer-Verlag 01.05.2015
Springer Science & Business Media LLC
Springer US
Society for In Vitro Biology
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ISSN1071-2690
1543-706X
1543-706X
DOI10.1007/s11626-014-9859-6

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Summary:Classical swine fever virus (CSFV) is the causative agent of a highly contagious disease, hog cholera in pigs. The disease is endemic in many parts of the world, and vaccination is the only way to protect the animals from CSFV infection. The lapinized vaccine strains are occasionally not protective because of animal to animal passage, inadequate vaccination strategy, suboptimal vaccine dose, and emergence of new variants. The surface glycoprotein E2 of CSFV is a major antigenic determinant and can modulate the disease outcome in pigs. In the present study, we characterized the CSFV in porcine kidney cells. The CSFV vaccine strains showed enhanced replication following 15 passages in porcine kidney cells. Nucleotide sequence analysis of the E2 protein gene of the cell culture-adapted vaccine strain of CSFV showed a mutation in putative amino acid sequences that are identical to its virulent counterpart. The study suggests the possibility of exaltation in vaccine strains following its adaptation in host cells and paves the way for a further exploration of the biology of its outbreak.
Bibliography:http://dx.doi.org/10.1007/s11626-014-9859-6
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ISSN:1071-2690
1543-706X
1543-706X
DOI:10.1007/s11626-014-9859-6