7 results about "Particulate antigen" patented technology

The present disclosure provides a type A foot-and-mouth disease virus-like particle antigen assembled by VP2, VP3 and VP1 antigen proteins of an epidemic strain of type A foot-and-mouth disease virus. The type A foot-and-mouth disease virus VP2 antigen protein is encoded by a nucleotide sequence shown in SEQ ID No. 1 or its degenerate sequence, the type A foot-and-mouth disease virus VP3 antigen protein is encoded by a nucleotide sequence shown in SEQ ID No. 2 or its degenerate sequence, and the type A foot-and-mouth disease virus VP1 antigen protein is encoded by a nucleotide sequence shown in SEQ ID No. 3 or its degenerate sequence.

This invention relates to the field of Clostridium perfringens antigen technology, and particularly to a Clostridium perfringens α-toxin-ferritin nanoparticle antigen, its preparation method, and its application. The Clostridium perfringens α-toxin-ferritin nanoparticle antigen is assembled from αm2ST protein and FeSC protein. The αm2ST protein is expressed using an α-protein mutant expression plasmid, and the FeSC protein is expressed using a ferritin expression plasmid. The nucleotide sequence of the α-protein mutant expression plasmid is shown in SEQ ID NO: 1, and the nucleotide sequence of the ferritin expression plasmid is shown in SEQ ID NO: 2. The Clostridium perfringens α-toxin-ferritin nanoparticle antigen provided by this invention can effectively stimulate humoral and cellular immunity, providing a new approach for the development of Clostridium perfringens subunit vaccines.

The application belongs to the field of biological medicine, and particularly relates to a bivalent nanoparticle antigen for preventing respiratory syncytial virus infection and application thereof. The F protein sequences of two subtypes of RSVA and B and the human Ferritin protein sequence are connected in series, the post-F specific I and IV epitope sequences and the pre-F and post-F shared III epitope partial sequences are removed, and the bivalent antigen nanoparticle containing the new F protein of the two subtypes A and B is obtained through the self-assembly of the Ferritin protein. The bivalent nanoparticle antigen has a larger molecular weight, can effectively improve the immunogenicity of the antigen, stimulate the body to produce more neutralizing antibodies, and produce neutralizing antibodies against the two subtypes A and B of viruses, and is more broad-spectrum.

The invention relates to the field of protein detection, in particular to a method for detecting phosphorylated Tau-231 protein in urine of a patient with Alzheimer's disease, which comprises the following steps: firstly, immobilizing a non-phosphorylated anti-Tau-231 antibody on a magnetic particle microsphere, immobilizing a phosphorylated anti-Tau-p-231 antibody on a fluorescent microsphere, and then, immobilizing a phosphorylated anti-Tau-p-231 antibody on the fluorescent microsphere. Forming a sandwich compound of magnetic particle-antigen-fluorescent probe by the detected object; the method specifically comprises the following steps: using fresh morning urine; the method comprises the following steps: taking out 100 [mu] l of urine by using a pipette, and adding the urine into a 5.0 ml centrifugal tube in which a phosphorylated anti-Tau-p-231 antibody which is prefabricated with a fluorescence label and a non-phosphorylated anti-Tau-p-231 antibody which is connected with nano magnetic particle microspheres are prefabricated; 4.9 ml of a urine diluent is added to dilute the urine; repeatedly reversing and uniformly mixing, reacting at room temperature for 8-12 hours, and placing a reaction tube on a separation test tube rack with a magnet for more than 20 minutes; irradiating the test tube by using a highlighter with the wavelength of about 340nm in a dark environment to judge a result; finally, the purposes of early screening, early intervention and early diagnosis of the Alzheimer's disease are achieved.

This invention discloses a fusion protein, PEDV RBD nanoparticle antigen, its preparation method, and its applications. The fusion protein is obtained by fusing the receptor-binding domain of the porcine epidemic diarrhea virus (PEDV) Spike protein to the N-terminus of a ferritin monomer via a linker peptide. It can self-assemble into PEDV RBD nanoparticle antigens with an average diameter of approximately 15 nm. The nanoparticle antigens exhibit structural integrity, enabling high-density multivalent display of the RBD, and possess excellent antigenic activity, specificity, thermal stability, and biocompatibility, making them suitable for large-scale production. This invention provides a safe, infection-free, and easily industrialized vaccine strategy for addressing PEDV infection. It can be further expanded for applications in veterinary vaccine formulation optimization and the research and development of diagnostic antigens and reagents, demonstrating good practicality and industrialization prospects.

The present application relates to the technical field of virology, more particularly to O-type foot-and-mouth disease virus-like particle antigen and its preparation method and application. The O-type foot-and-mouth disease virus structural protein is constructed, and the recombinant expression vector comprises a Sumo-VP1 sequence, a Sumo-VP3 sequence, a Sumo-VP0 sequence and a chaperone sequence; the recombinant expression vector is transformed into a genetically engineered bacterium, and Sumo-VP1 protein, Sumo-VP3 protein, Sumo-VP0 protein and chaperone protein are expressed; the initial extraction solution is obtained by crushing; the purified extraction solution is obtained by purification; the self-assembled O-type foot-and-mouth disease virus-like particle antigen is obtained by enzyme cutting and removal of Sumo enzyme. The present application improves the soluble expression proportion and overall expression amount of the target protein in the supernatant by optimizing the construction mode and transformation strategy of the foot-and-mouth disease structural protein, and overcomes the technical bottleneck that the supernatant expression amount of the existing E. coli expression system is low and the inclusion body is prone to be formed.