Development of a multi-epitope antigen of S protein-based ELISA for antibodies detection against infectious bronchitis virus

Ding, Mei; Wang, Hongning; Cao, Hai-peng; Fan, Wen-qiao; Ma, Bing-cun; Xu, Pengwei; Zhang, Anyun; Yang, Xin

doi:10.1080/09168451.2015.1025692

Cited by 15 publications

(7 citation statements)

References 33 publications

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“…The purified proteins (S1 N -SCZJ3 and S1 N -M41) and PNGase F (NEB)-treated proteins were separated by 10% SDS-PAGE and detected using polyclonal IBV-M41 antiserum (diluted 1:100 in PBS, China Institute of Veterinary Drug Control). Western blot analysis was performed as described [21].…”

Section: Protein Expression and Purificationmentioning

confidence: 99%

Heat shock protein 70 in lung and kidney of specific-pathogen-free chickens is a receptor-associated protein that interacts with the binding domain of the spike protein of infectious bronchitis virus

Zhang

Yang²,

Xu³

et al. 2017

Arch Virol

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Avian infectious bronchitis virus (IBV) is a member of the family Coronaviridae. A binding domain that mediates the attachment of the virus to its receptor has been identified in the S1 protein of prototype IBV strain M41. In this study, we identified this binding domain in a different strain, as well as the cellular proteins that interact with it. First, we expressed the S1 proteins (residues 19-270) of M41 and another isolate, SCZJ3, and compared the binding capacities of recombinant S1-M41 and S1-SCZJ3 to host tissues. Protein histochemistry showed that both S1-M41 and S1-SCZJ3 could bind to lung and kidney, and that recombinant S1-SCZJ3 displayed a distinctive staining pattern in the proventriculus. Recombinant S1-SCZJ3 was then employed to purify binding-associated proteins in lung, kidney, and proventriculus. Using an affinity chromatography assay, two common bands of about 60 kDa and 70 kDa were obtained from the total tissue proteins. These protein bands were identified by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) as protein disulfide isomerase (PDI) and heat shock protein 70 (HSP70). Finally, infection of chicken embryo kidney (CEK) cells by SCZJ3 was found to be inhibited by anti-HSP70 but not anti-PDI polyclonal antibody. These data indicate that HSP70 is part of the receptor complex of IBV and might help to understand the mechanism of S-mediated cell entry of IBV.

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Section: Protein Expression and Purificationmentioning

confidence: 99%

Heat shock protein 70 in lung and kidney of specific-pathogen-free chickens is a receptor-associated protein that interacts with the binding domain of the spike protein of infectious bronchitis virus

Zhang

Yang²,

Xu³

et al. 2017

Arch Virol

Self Cite

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“…To detect IBVspecific antibodies as accurately and comprehensively as possible, many ELISA-based antibody detection methods have been established [33][34][35]. Such as, Ding et al developed a multi-fragment antigen ELISA showed good coincidence ratio with the commercial ELISA (IDEXX) [36]. Lei et al established nsp5-based ELISA revealed consistent with the commercial ELISA in detecting IBV specific antibody levels following IBV infection and vaccination [16].…”

Section: Discussionmentioning

confidence: 99%

Peptide enzyme‐linked immunosorbent assay (pELISA) as a possible alternative to the neutralization test for evaluating the immune response to IBV vaccine

Lin

et al. 2021

BMC Vet Res

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Background Infectious bronchitis virus (IBV), a coronavirus, is one of the most important poultry pathogens worldwide due to its multiple serotypes and poor cross-protection. Vaccination plays a vital role in controlling the disease. The efficacy of vaccination in chicken flocks can be evaluated by detecting neutralizing antibodies with the neutralization test. However there are no simple and rapid methods for detecting the neutralizing antibodies. Results In this study, a peptide enzyme-linked immunosorbent assay (pELISA) as a possible alternative to the neutralization test for evaluating the immune response to IBV vaccine was developed. The pELISA could indirect evaluate neutralizing antibody titers against different types of IBV in all tested sera. The titers measured with the pELISA had a coefficient of 0.83 for neutralizing antibody titers. Conclusions The pELISA could detect antibodies against different types of IBV in all tested sera. The pELISA has the potential to evaluate samples for IBV-specific neutralizing antibodies and surveillance the infection of IBV.

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“…To detect IBV antibodies as accurately and comprehensively as possible, many ELISA antibody detection methods have been established (Chen et al, 2011;Ding et al, 2015;Lei et al, 2017). All of these methods have good efficacy, but still have some limitations.…”

Section: Discussionmentioning

confidence: 99%

Peptides with 16R in S2 protein showed broad reactions with sera against different types of infectious bronchitis viruses

Lin

Qian

et al. 2019

Veterinary Microbiology

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Vaccination plays a vital role in controlling diseases caused by chicken infectious bronchitis virus (IBV). The continuously variant antigenicity of IBV limits the application of current vaccine strategies and serological diagnostic systems. S2 protein is an invariant that harbors broad neutralizing epitopes. However, little is known about the key amino acids that contribute to the broad-spectrum S2 epitopes. In this study, we aimed to elucidate the specific amino acids contributing to S2 epitopes. Site mutagenesis and peptide-based enzyme-linked immunosorbent assays (ELISAs) showed that 16R in S2 protein was a key amino acid mediating the antigenicity of S2 protein. S2-derived peptides with 16R, but not those with 16 K, could react with sera against different types of IBVs. Notably, a commercial ELISA kit for detection of antibodies against IBV did not react with sera against all types of IBVs. Taken together, these data demonstrated that S2-derived peptides with 16R could be used as novel marker-based antigens for developing both broad-spectrum vaccines and serological diagnostic kits to control IBV.

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Development of a multi-epitope antigen of S protein-based ELISA for antibodies detection against infectious bronchitis virus

Abstract: (2015) Development of a multi-epitope antigen of S protein-based ELISA for antibodies detection against infectious bronchitis virus, Bioscience, Biotechnology, and Biochemistry, 79:8, 1287-1295,

Cited by 15 publications

References 33 publications

Heat shock protein 70 in lung and kidney of specific-pathogen-free chickens is a receptor-associated protein that interacts with the binding domain of the spike protein of infectious bronchitis virus

Heat shock protein 70 in lung and kidney of specific-pathogen-free chickens is a receptor-associated protein that interacts with the binding domain of the spike protein of infectious bronchitis virus

Peptide enzyme‐linked immunosorbent assay (pELISA) as a possible alternative to the neutralization test for evaluating the immune response to IBV vaccine

Peptides with 16R in S2 protein showed broad reactions with sera against different types of infectious bronchitis viruses

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