Identification of two novel B cell epitopes on porcine epidemic diarrhea virus spike protein

  title={Identification of two novel B cell epitopes on porcine epidemic diarrhea virus spike protein},
  author={Dongbo Sun and Li Feng and Hongyan Shi and Jianfei Chen and Xiaochen Cui and Hongyan Chen and Shengwang Liu and You En Tong and Yunfeng Wang and Guang-zhi Tong},
  journal={Veterinary Microbiology},
  pages={73 - 81}

Figures and Tables from this paper

Identification of a conserved linear B-cell epitope in the M protein of porcine epidemic diarrhea virus

The 4D4-defined epitope identified provides a basis for the development of epitope-based differential diagnostic techniques and may be useful in the design of epitopes-based vaccines.

Identification and characterization of a novel linear epitope in the spike protein of the porcine epidemic diarrhea virus.

The linear epitope of the 3F10 non-neutralizing monoclonal antibody that was previously prepared in the laboratory was identified and homology analysis of the regions corresponding to 20 typical strains of different PEDV subtypes showed that the epitope is highly conserved.

Immunodominant and Neutralizing Linear B-Cell Epitopes Spanning the Spike and Membrane Proteins of Porcine Epidemic Diarrhea Virus

The findings unveil important roles of the PEDV S2 subunit in both immune stimulation and virus neutralization, and shows the first time that the M protein is also the target of P EDV neutralization with seven neutralizing epitopes identified.

Immunodominant and neutralizing linear B cell epitopes spanning the spike and membrane proteins of Porcine Epidemic Diarrhea Virus

The immunoinformatics approach for linear B cell epitope identification and a more complete profile of linear Bcell epitopes across the PEDV S and M proteins are offered, which may contribute to the development of a greater P EDV vaccine as well as peptide-based immunoassays.

Putative phage-display epitopes of the porcine epidemic diarrhea virus S1 protein and their anti-viral activity

Data from real-time PCR and indirect immunofluorescence assays were consistent with the ability of peptides M, L and W to block viral protein expression and thereby function as antiviral agents for PEDV.

Identification and characterization of a neutralizing-epitope-containing spike protein fragment in turkey coronavirus

The results of a virus neutralization assay indicated that the carboxyl terminal region of the S1 protein (Mod4F/Epi4R) or the combined car boxyl terminal S1 and amino terminal S2 protein (4f/4R), while the S2 fragment (6F/6R) contains antigenic epitopes but not neutralizing epitopes.

Identification of Neutralizing Monoclonal Antibodies Targeting Novel Conformational Epitopes of the Porcine Epidemic Diarrhoea Virus Spike Protein

The neutralizing epitopes of a new genotype 2b PEDV isolate from Taiwan, PEDv Pintung 52 (PEDV-PT), are characterized by the generation of neutralizing monoclonal antibodies (NmAbs) to improve the understanding of the antigenic structures of the P EDV S protein and facilitate future development of novel epitope-based vaccines.

Novel Neutralizing Epitope of PEDV S1 Protein Identified by IgM Monoclonal Antibody

Porcine epidemic diarrhea virus (PEDV) causes devastating enteric disease that inflicts huge economic damage on the swine industry worldwide. A safe and highly effective PEDV vaccine that contains



Screening and identification of B cell antigenic epitopes of porcine epidemic diarrhea virus spike glycoprotein by phage display

The result of indirect immunofluorescence assay(IFA) demonstrated that the antisera induced by S1P2-GST,S1P3- GST and S1p123-G ST fusion proteins possessed binding ability to the native S protein of PEDV cultured in Vero cells.

Spike protein region (aa 636789) of porcine epidemic diarrhea virus is essential for induction of neutralizing antibodies.

It is found that the region of S1 signed as S1D was able to react with PEDV antiserum and to elicit formation of neutralization antibodies in mice, and the immune serum against S1d showed the binding ability to the native S protein of PEDv.

Identification of the epitope region capable of inducing neutralizing antibodies against the porcine epidemic diarrhea virus.

The amino acid sequences that are deduced from the genes for the determined-neutralizing epitope were highly homologous among the PEDV strains that were isolated from different geographical areas, which suggests conservation of the antigen gene.

Sequence of the spike protein of the porcine epidemic diarrhoea virus.

The complete sequence of the spike (S) gene of the Br1/87 isolate of porcine epidemic diarrhoea virus (PEDV) was determined from cDNA clones and revealed a second domain of about 90 residues with increased sequence divergence which might possibly express virus-specific determinants.

Cloning and Sequence Analysis of the Spike Gene of Porcine Epidemic Diarrhea Virus Chinju99

The spike (S) gene of the porcine epidemic diarrhea virus (PEDV) Chinju99 which was previously isolated in Chinju, Korea was cloned and sequenced to aid in the development of genetically engineered

Cloning and further sequence analysis of the spike gene of attenuated porcine epidemic diarrhea virus DR13

The spike (S) gene of the attenuated porcine epidemic diarrhea virus (PEDV) DR13 was cloned and sequenced and suggested that attenuated PEDV DR13 is closely related to CV777, Br1/87, JS-2004-2 and parent DR13, rather than to Spk1 and Chinju99 and is especially close to the Chinese P EDV strain JS- 2004-2.

Porcine aminopeptidase N is a functional receptor for the PEDV coronavirus

The spike protein of severe acute respiratory syndrome (SARS) is cleaved in virus infected Vero-E6 cells

Investigation of the maturation and proteolytic processing of the S protein of SARS CoV demonstrated that the cleavage of S protein was observed in the lysate, indicating that proteolytically processed S protein is present in host cells.

Cooperative Involvement of the S1 and S2 Subunits of the Murine Coronavirus Spike Protein in Receptor Binding and Extended Host Range

The observations suggest that the amino-terminal region of the S protein, including the receptor-binding domain, and a region in the central part of theS protein containing HR1 and FP, communicate and may even interact physically in the higher-order structure of the spike.