Application of purified recombinant antigenic spike fragments to the diagnosis of avian infectious bronchitis virus infection.
Identifieur interne : 001358 ( PubMed/Corpus ); précédent : 001357; suivant : 001359Application of purified recombinant antigenic spike fragments to the diagnosis of avian infectious bronchitis virus infection.
Auteurs : Kuan-Hsun Lin ; Chuen-Fu Lin ; Shyan-Song Chiou ; Ai-Ping Hsu ; Min-Shiuh Lee ; Chao-Chin Chang ; Tien-Jye Chang ; Jui-Hung Shien ; Wei-Li HsuSource :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2012.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Viral (blood), Antigens, Viral (genetics), Antigens, Viral (immunology), Antigens, Viral (isolation & purification), Antigens, Viral (metabolism), Chickens, Coronavirus Infections (diagnosis), Coronavirus Infections (immunology), Coronavirus Infections (veterinary), Coronavirus Infections (virology), Enzyme-Linked Immunosorbent Assay, Infectious bronchitis virus (genetics), Infectious bronchitis virus (immunology), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (isolation & purification), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Poultry Diseases (diagnosis), Poultry Diseases (immunology), Poultry Diseases (virology), Recombinant Proteins (genetics), Recombinant Proteins (immunology), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Sensitivity and Specificity, Sequence Analysis, DNA, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (isolation & purification), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , blood : Antibodies, Viral.
- chemical , genetics : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , isolation & purification : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- diagnosis : Coronavirus Infections, Poultry Diseases.
- genetics : Infectious bronchitis virus.
- immunology : Coronavirus Infections, Infectious bronchitis virus, Poultry Diseases.
- veterinary : Coronavirus Infections.
- virology : Coronavirus Infections, Poultry Diseases.
- Amino Acid Sequence, Animals, Chickens, Enzyme-Linked Immunosorbent Assay, Molecular Sequence Data, Sensitivity and Specificity, Sequence Analysis, DNA, Spike Glycoprotein, Coronavirus.
Abstract
The spike (S) protein, containing two subunits, S1 and S2, is the major immunity-eliciting antigen of avian infectious bronchitis virus (IBV), a highly contagious disease of chickens. Several immunogenic regions, mainly located within the S1 subunit, have been identified. Nonetheless, these immune-dominant regions were defined using selected monoclonal antibodies or using a short peptide approach that involves only certain limited regions of the S protein. In addition, some immune-dominant regions are located in hypervariable regions (HVRs) which are not present in all serotypes. Hence, the aim of this study was to determine a broader range of antigenic regions that have strong antibody eliciting ability; these could then be applied for development of an IBV-diagnostic tool. Initially, the S1 and part of the S2 subunit protein (24-567 amino acids) were expressed as five fragments in prokaryotic system. The antigenicity was confirmed using IBV immunized sera. Performance of the S subfragments was evaluated by ELISA using a panel of field chicken sera with known IBV titres determined by a commercial kit. This indicated that, among the five antigenic recombinant proteins, the region S-E showed the highest specificity and sensitivity, namely 95.38 % and 96.29 %, respectively. The κ value for the in-house ELISA using the S-E fragment compared to a commercial kit was 0.9172, indicating a high agreement between these two methods. As region S-E harbors strong immunogenicity within the spike protein, it has the potential to be exploited as an antigen when developing a cost-effective ELISA-based diagnosis tool.
DOI: 10.1007/s00253-012-4143-8
PubMed: 22627759
Links to Exploration step
pubmed:22627759Le document en format XML
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<term>Antigens, Viral (genetics)</term>
<term>Antigens, Viral (immunology)</term>
<term>Antigens, Viral (isolation & purification)</term>
<term>Antigens, Viral (metabolism)</term>
<term>Chickens</term>
<term>Coronavirus Infections (diagnosis)</term>
<term>Coronavirus Infections (immunology)</term>
<term>Coronavirus Infections (veterinary)</term>
<term>Coronavirus Infections (virology)</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Infectious bronchitis virus (genetics)</term>
<term>Infectious bronchitis virus (immunology)</term>
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<front><div type="abstract" xml:lang="en">The spike (S) protein, containing two subunits, S1 and S2, is the major immunity-eliciting antigen of avian infectious bronchitis virus (IBV), a highly contagious disease of chickens. Several immunogenic regions, mainly located within the S1 subunit, have been identified. Nonetheless, these immune-dominant regions were defined using selected monoclonal antibodies or using a short peptide approach that involves only certain limited regions of the S protein. In addition, some immune-dominant regions are located in hypervariable regions (HVRs) which are not present in all serotypes. Hence, the aim of this study was to determine a broader range of antigenic regions that have strong antibody eliciting ability; these could then be applied for development of an IBV-diagnostic tool. Initially, the S1 and part of the S2 subunit protein (24-567 amino acids) were expressed as five fragments in prokaryotic system. The antigenicity was confirmed using IBV immunized sera. Performance of the S subfragments was evaluated by ELISA using a panel of field chicken sera with known IBV titres determined by a commercial kit. This indicated that, among the five antigenic recombinant proteins, the region S-E showed the highest specificity and sensitivity, namely 95.38 % and 96.29 %, respectively. The κ value for the in-house ELISA using the S-E fragment compared to a commercial kit was 0.9172, indicating a high agreement between these two methods. As region S-E harbors strong immunogenicity within the spike protein, it has the potential to be exploited as an antigen when developing a cost-effective ELISA-based diagnosis tool.</div>
</front>
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<Abstract><AbstractText>The spike (S) protein, containing two subunits, S1 and S2, is the major immunity-eliciting antigen of avian infectious bronchitis virus (IBV), a highly contagious disease of chickens. Several immunogenic regions, mainly located within the S1 subunit, have been identified. Nonetheless, these immune-dominant regions were defined using selected monoclonal antibodies or using a short peptide approach that involves only certain limited regions of the S protein. In addition, some immune-dominant regions are located in hypervariable regions (HVRs) which are not present in all serotypes. Hence, the aim of this study was to determine a broader range of antigenic regions that have strong antibody eliciting ability; these could then be applied for development of an IBV-diagnostic tool. Initially, the S1 and part of the S2 subunit protein (24-567 amino acids) were expressed as five fragments in prokaryotic system. The antigenicity was confirmed using IBV immunized sera. Performance of the S subfragments was evaluated by ELISA using a panel of field chicken sera with known IBV titres determined by a commercial kit. This indicated that, among the five antigenic recombinant proteins, the region S-E showed the highest specificity and sensitivity, namely 95.38 % and 96.29 %, respectively. The κ value for the in-house ELISA using the S-E fragment compared to a commercial kit was 0.9172, indicating a high agreement between these two methods. As region S-E harbors strong immunogenicity within the spike protein, it has the potential to be exploited as an antigen when developing a cost-effective ELISA-based diagnosis tool.</AbstractText>
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