Expression of E2 gene of CSFV and analysis of epitope diversity


Citation

Sheik Omar A. R., . and Mohd Azmi M. L., . and A. R. Bahaman, . and Aini Ideris, . and Zeenathul N. A., . and A. R. Mutalib, . Expression of E2 gene of CSFV and analysis of epitope diversity. pp. 21-25. ISSN 9128-2506

Abstract

Infection of cells with classical swine fever virus (CSFV) is mediated by the interaction of envelope glycoproteins with receptor molecules on the cell surface. The E2 protein is one of the major envelope antigens for eliciting neutralising antibodies and conferring protective immunity. The study found a distinct substitution of two amino acids at positions 94 (R G) and 97 (P S) in the deduced E2 protein sequence of GPE strain of CSFV which contributed to 0.5 difference from the original sequence. Nevertheless successful E2 expression from the plasmid cassette was detelmined via in vitro analysis. Two different MAbs WH303 and WH211 were used for E2 protein detection. The E2 detection was accomplished by using MAb WH211. However the usage of the MAb WH303 for the E2 expression analyses was unsuccessful. It was observed that the alanine in minimal antigenic domain recognised by WH303 had been substituted with tyrosine in the critical epitope of E2 peptide of GPE-strain at position 163. Therefore the mapping data for these neutralising epitopes will be useful for the development of diagnostic tests.


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Abstract

Infection of cells with classical swine fever virus (CSFV) is mediated by the interaction of envelope glycoproteins with receptor molecules on the cell surface. The E2 protein is one of the major envelope antigens for eliciting neutralising antibodies and conferring protective immunity. The study found a distinct substitution of two amino acids at positions 94 (R G) and 97 (P S) in the deduced E2 protein sequence of GPE strain of CSFV which contributed to 0.5 difference from the original sequence. Nevertheless successful E2 expression from the plasmid cassette was detelmined via in vitro analysis. Two different MAbs WH303 and WH211 were used for E2 protein detection. The E2 detection was accomplished by using MAb WH211. However the usage of the MAb WH303 for the E2 expression analyses was unsuccessful. It was observed that the alanine in minimal antigenic domain recognised by WH303 had been substituted with tyrosine in the critical epitope of E2 peptide of GPE-strain at position 163. Therefore the mapping data for these neutralising epitopes will be useful for the development of diagnostic tests.

Additional Metadata

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Item Type: Article
AGROVOC Term: Classical swine fever virus
AGROVOC Term: Infection
AGROVOC Term: Gene expression
AGROVOC Term: Gene mapping
AGROVOC Term: Glycoproteins
AGROVOC Term: Gene cloning
AGROVOC Term: Plasmids
AGROVOC Term: Tyrosine
AGROVOC Term: Envelope materials
AGROVOC Term: Binding proteins
Depositing User: Mr. AFANDI ABDUL MALEK
Last Modified: 24 Apr 2025 00:54
URI: http://webagris.upm.edu.my/id/eprint/8431

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