Porcine circovirus type 3 (PCV3) is endemic in swine worldwide and causes reproductive disorders, dermatitis and nephrotic syndrome, and multi-organ inflammation. Currently, there is a growing need for rapid and accurate diagnostic methods in disease monitoring. In this study, four monoclonal antibodies (mAbs) against PCV3 capsid proteins were prepared (mAbs 2F6, 2G8, 6E2, and 7E3). MAb 7E3, which had the highest binding affinity for the Cap protein, was chosen for further investigation. A novel B cell epitope DLDGAW was identified using mAb 7E3. An epitope-blocking (EB) enzyme-linked immunosorbent assay (ELISA) was successfully developed using horseradish-peroxidase-labeled mAb 7E3 to detect PCV3 antibodies in porcine sera. Moreover, the EB-ELISA showed no specific reaction with other porcine disease sera, and the cut-off value was defined as 35%. Compared with the commercial ELISA, the percentage agreement was 95.59%. Overall, we have developed a novel EB-ELISA method that accurately and conveniently detects PCV3 in serum, making it a valuable tool for the clinical detection of PCV3 infection.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10812811PMC
http://dx.doi.org/10.3390/ani14020235DOI Listing

Publication Analysis

Top Keywords

mab 7e3
12
monoclonal antibodies
8
epitope-blocking enzyme-linked
8
enzyme-linked immunosorbent
8
immunosorbent assay
8
porcine circovirus
8
pcv3
5
preparation monoclonal
4
antibodies capsid
4
capsid protein
4

Similar Publications

Article Synopsis
  • - Monoclonal antibodies (mAbs) have been used to study the platelet αIIbβ3 protein, and a new mAb called R21D10 was identified that interferes with protein disulfide isomerase (PDI) binding to activated platelets.
  • - R21D10 not only inhibits PDI binding but also affects fibrinogen and PAC-1 binding, as well as platelet aggregation induced by specific peptides, without impacting the binding of other known mAbs against αIIbβ3.
  • - Structural analysis using cryogenic electron microscopy showed that R21D10 binds to a specific domain on β3 integrin and induces conformational changes in αIIbβ3, suggesting a
View Article and Find Full Text PDF

Porcine circovirus type 3 (PCV3) is endemic in swine worldwide and causes reproductive disorders, dermatitis and nephrotic syndrome, and multi-organ inflammation. Currently, there is a growing need for rapid and accurate diagnostic methods in disease monitoring. In this study, four monoclonal antibodies (mAbs) against PCV3 capsid proteins were prepared (mAbs 2F6, 2G8, 6E2, and 7E3).

View Article and Find Full Text PDF

The molecular basis of platelet-fibrin interactions remains poorly understood despite the predominance of fibrin in thrombi. We have studied the interaction of platelets with polymerizing fibrin by adding thrombin to washed platelets in the presence of the peptide RGDW, which inhibits the initial platelet aggregation mediated by fibrinogen binding to αIIbβ3 but leaves intact a delayed increase in light transmission (delayed wave; DW) as platelets interact with the polymerizing fibrin. The DW was absent in platelets from a patient with Glanzmann thrombasthenia, indicating a requirement for αIIbβ3.

View Article and Find Full Text PDF
Article Synopsis
  • The murine mAb PT25-2 promotes platelet aggregation by causing the αIIbβ3 receptor to bind ligands, though its mechanism was previously unknown.
  • Recent studies using cryo-electron microscopy and negative-stain techniques revealed that PT25-2 binding partially exposes ligand-binding sites and alters the αIIbβ3 receptor's structure without triggering the typical conformational changes seen in other binding scenarios.
  • The research suggests that PT25-2 prefers to attach to extended forms of the receptor, hindering its ability to revert to a bent shape, thus facilitating ligand binding necessary for platelet activation.
View Article and Find Full Text PDF

Although much is known about the interaction of fibrinogen with αIIbβ3, much less is known about the interaction of platelets with cross-linked fibrin. Fibrinogen residue Lys406 plays a vital role in the interaction of fibrinogen with αIIbβ3, but because it participates in fibrin cross-linking, it is not available for interacting with αIIbβ3. We studied the adhesion of platelets and HEK cells expressing normal and constitutively active αIIbβ3 to both immobilized fibrinogen and D-dimer, a proteolytic fragment of cross-linked fibrin, as well as platelet-mediated clot retraction.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!