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Real-time SPR characterization of the interactions between multi-epitope proteins and antibodies against classical swine fever virus.

Abstract：

:The envelope glycoprotein E2 is the major immunodominant protein of the classical swine fever virus and can induce neutralizing antibodies and protective host-immune responses in infected swine. We designed, expressed, and purified multi-epitope protein (GST-BT22) that contains a tandem repeat of the E2 antigenic-determinant residues 693-704, 770-780, and 826-843, each of which is separated by a GGSSGG sequence. In the same manner, we also designed, expressed, and purified a second protein (GST-BT23) that contains a C-terminal sequence consisting of residues 1446-1460 from the classical swine fever virus nonstructural protein NS2-3 separated from the GST-BT22 sequence by a GGSSGG sequence. Western blotting of GST-BT22 and GST-BT23 with serum from a swine that had been experimentally infected with the virus showed that the proteins reacted with anti-serum, whereas GST did not. Surface plasmon resonance was used to quantify the affinities of GST-BT22 and GST-BT23 for serum antibodies (K(a) = 4.31 × 10(8) and 5.01 × 10(8), respectively). GST, used as a control, was reacted an order of magnitude less strongly than did GST-BT22 and GST-BT23. Surface plasmon resonance, therefore, appears to be a sensitive and precise method for epitope evaluation and can be used to characterize the immunogenicity of a recombinant protein.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tian H,Hou X,Liu X

doi

10.1016/j.bbrc.2012.12.104

subject

Has Abstract

pub_date

2013-02-08 00:00:00

pages

315-20

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)02464-3

journal_volume

431

pub_type

杂志文章

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