Recombinant PEDV S/Spike glycoprotein Protein, N-His & C-His

Description of Recombinant PEDV S/Spike glycoprotein Protein, N-His & C-His

Introduction

Recombinant proteins have revolutionized the field of biotechnology and are widely used in various applications, including diagnostics and therapeutics. One such recombinant protein is the Porcine Epidemic Diarrhea Virus (PEDV) S/Spike glycoprotein, which has gained significant attention due to its potential use as an antigen in vaccine development against PEDV. In this article, we will provide a detailed description of the structure, activity, and application of recombinant PEDV S/Spike glycoprotein protein.

Structure of Recombinant PEDV S/Spike glycoprotein Protein

The PEDV S/Spike glycoprotein is a type I transmembrane protein, consisting of 1383 amino acids with a molecular weight of approximately 150 kDa. The protein is composed of two subunits, S1 and S2, which are connected by a cleavage site. The S1 subunit is responsible for receptor binding, while the S2 subunit is involved in virus-cell membrane fusion. The S1 subunit contains a receptor-binding domain (RBD) and a variable region, which are important for virus attachment and entry into the host cell. The S2 subunit contains a fusion peptide, two heptad repeat regions, and a transmembrane domain, which are essential for virus-cell membrane fusion.

Activity of Recombinant PEDV S/Spike glycoprotein Protein

The primary function of the PEDV S/Spike glycoprotein is to mediate virus entry into the host cell by binding to the receptor on the cell surface. The receptor for PEDV is aminopeptidase N (APN), which is expressed on the surface of intestinal epithelial cells in pigs. The RBD of the S1 subunit binds to the APN receptor, facilitating virus attachment and entry into the host cell. The S2 subunit then undergoes conformational changes, leading to virus-cell membrane fusion and release of the viral genome into the host cell.

Application of Recombinant PEDV S/Spike glycoprotein Protein

Recombinant PEDV S/Spike glycoprotein protein has shown great potential as an antigen in vaccine development against PEDV. Vaccines based on the whole virus or inactivated virus have been used in the past, but they have shown limited efficacy and safety concerns. Recombinant protein-based vaccines offer several advantages over traditional vaccines, including improved safety, stability, and ease of production. The recombinant PEDV S/Spike glycoprotein protein can be produced in large quantities using recombinant DNA technology, ensuring a consistent and reliable source of antigen for vaccine production.

Several studies have demonstrated the immunogenicity and protective efficacy of recombinant PEDV S/Spike glycoprotein protein in pigs. One study showed that pigs immunized with a recombinant S1 protein-based vaccine had significantly higher levels of neutralizing antibodies and reduced virus shedding after challenge with a virulent PEDV strain. Another study showed that a vaccine containing a recombinant S1 subunit and an adjuvant induced a robust immune response and provided complete protection against PEDV challenge in pigs.

In addition to vaccine development, recombinant PEDV S/Spike glycoprotein protein has also been used in diagnostic assays for the detection of PEDV. The recombinant protein can be used as an antigen in serological assays, such as ELISA, for the detection of antibodies against PEDV. It can also be used in molecular assays, such as PCR, for the detection of viral RNA in clinical samples.

Conclusion

Recombinant PEDV S/Spike glycoprotein protein is a promising antigen for vaccine development against PEDV. Its well-defined structure and activity make it an ideal candidate for inducing a robust immune response in pigs. The recombinant protein has also shown potential for use in diagnostic assays for the detection of PEDV. Further research and development of recombinant PEDV S/Spike glycoprotein protein-based vaccines and diagnostic assays will help in controlling and preventing the spread of PEDV in the swine industry.