Thermal stress treatment does not affect the stability and protective capacity of goat milk derived E2-marker vaccine formulation against CSFV.

Classical swine fever virus produces a huge mortality in infected herds during recurrent outbreaks, predominantly in tropical and subtropical areas. In this scenario, it is common that cold-chain related issues affect the efficacy of virus attenuated-derived vaccines, which are frequently used in eradication programs. In the present work, the stability and protective capacity of a recombinant vaccine preparation, based on goat milk derived E2 glycoprotein extracellular domain, were both analyzed after incubation at 4 degrees C or 37 degrees C for 1 week.

Classical swine fever virus E2 glycoprotein antigen produced in adenovirally transduced PK-15 cells confers complete protection in pigs upon viral challenge.

E2 is the major envelope glycoprotein present on the outer surface of the classical swine fever virus (CSFV). It is exposed as a homodimer originated by disulfide linkage and represents an important target for the induction of neutralizing immune responses against the viral infection. The E2his glycoprotein nucleotide sequence used in this work contains the CSFV E2 extracellular domain preceded by the tissue plasminogen signal peptide and a hexa-histidine tag in the 3' terminus.