Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Swine fever antigen epitope peptide and use thereof

An antigen epitope and swine fever technology, applied in the field of biomedicine, can solve the problems of low protein conformation folding accuracy, low antigen epitope abundance, complex purification methods, etc., and achieve excellent immune effect, short cycle time, and simple purification methods Effect

Active Publication Date: 2021-04-20
INSITUTE OF BIOPHYSICS CHINESE ACADEMY OF SCIENCES
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] Therefore, the technical problem to be solved in the present invention is that the existing African swine fever multi-epitope fusion protein antigen epitope abundance is low, the immune effect is low, and the protein conformation folds The accuracy rate is low, and the purification method is complicated, and a hog fever antigen epitope peptide and its application are provided. The hog fever antigen epitope peptide can trigger an effective immune response, and the recombinant The antigens are all in the form of virus-like particles or multimeric proteins, not in the form of monomers, so that the abundance of antigenic epitopes is high, and the immune effect is excellent, and the recombinant antigens are expressed in soluble form, and the accuracy of protein conformation and folding is high , the purification method is simple

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Swine fever antigen epitope peptide and use thereof
  • Swine fever antigen epitope peptide and use thereof
  • Swine fever antigen epitope peptide and use thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0042] Embodiment 1 hog fever antigenic epitope peptide

[0043] In this example, four key epitope peptides ER1, ER2, ER3 and ER4 were designed according to the N-terminal 100-550 amino acids of the ASFV P72 antigen.

[0044] ER1 is the amino acid sequence shown in SEQ ID NO.1, which is selected from N-terminal D119-R174 of African swine fever virus protein P72.

[0045] ER2 is the amino acid sequence shown in SEQ ID NO.2, which is selected from N-terminal P240-D305 of African swine fever virus protein P72.

[0046] ER3 is the amino acid sequence shown in SEQ ID NO.3, which is selected from N-terminal G373-P399 of African swine fever virus protein P72.

[0047] ER4 is the amino acid sequence shown in SEQ ID NO.4, which is selected from N-terminal A496-T529 of African swine fever virus protein P72.

[0048] ER1, ER2, ER3 and ER4 can be embedded in the Cap protein of porcine circovirus PCV2, the immunodominant region of hepatitis B core antigen monomer, human ferritin and trim...

Embodiment 2

[0049] The preparation of embodiment 2 recombinant antigen HBCAG-ER4

[0050] The preparation of recombinant antigen HBCAG-ER4 comprises the following steps:

[0051] (1) Gene synthesis and molecular construction: embed the gene sequence of the ER4 antigen epitope peptide between 79-80aa of the gene sequence of the HBCAG protein backbone (the amino acid sequence of the HBCAG protein backbone is shown in SEQ ID NO.5), and place The obtained recombinant gene sequence was inserted between NcoI and xhoI of the pET-28a vector to obtain a recombinant plasmid. The synthesis and plasmid construction of the above-mentioned genes were all carried out by Nanjing GenScript Company.

[0052] (2) Plasmid transformation: Add 2 μl of the recombinant plasmid (80ng / μl) described in step (1) to Escherichia coli BL21(DE3) competent cells (purchased from Bomide), and put it on ice for 30 minutes, then 42°C Heat shock for 90 seconds, place on ice again for 2 minutes, add 800 μl of LB medium, plac...

Embodiment 3

[0055] The preparation of embodiment 3 recombinant antigen HBCAG-ER2

[0056] The preparation method of this embodiment is basically the same as that of Example 2, the only difference is that in step (1) gene synthesis and molecular construction, in order to embed the gene sequence of the ER2 epitope peptide into the HBCAG protein skeleton (the HBCAG protein skeleton is as shown in SEQ The amino acid sequence shown in ID NO.5) is between 79-80aa of the gene sequence, and the obtained recombinant gene sequence is inserted between the pET-28a vector NcoI and xhoI to obtain a recombinant plasmid. The synthesis and plasmid construction of the above-mentioned genes were all carried out by Nanjing GenScript Company. in, image 3 The SDS-PAGE results of the HBCAG-ER2 recombinant antigen are shown, Figure 4 The negative-stained electron microscope picture of the HBCAG-ER2 recombinant antigen is shown. It can be seen that the HBCAG-ER2 recombinant antigen has successfully assembled ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The invention belongs to the field of biomedicines and particularly relates to a swine fever antigen epitope peptide and use thereof. The swine fever antigen epitope peptide is selected from 100th-550th amino acids of a N-terminal of an African swine fever viral protein P72 and has the length of 20-210 amino acids, and an independent swine fever antigen epitope peptide maybe comprise a recombinant antigen of the swine fever antigen epitope peptide and can induce an immune reaction of a mammal to the African swine fever viral protein P72. Inventors disclose epitope information on a major antigen protein P72 of an African swine fever virus according to a resolved full virus structure of a natural African swine fever virus; and compared with epitope information predicted by means of bioinformatics and the like, the swine fever antigen epitope peptide disclosed by the invention is more real, more reliable and more effective.

Description

technical field [0001] The invention belongs to the field of biomedicine, and in particular relates to a hog fever antigenic epitope peptide and its application. Background technique [0002] African swine fever (ASF) is an acute, febrile, highly contagious disease caused by African swine fever virus (ASFV), the only member of the African swine fever virus family. Domestic pigs and European wild boars are generally susceptible, showing complex clinical symptoms, causing congestion, hemorrhage and dysfunction of the digestive system and respiratory system. It is a highly contagious disease in domestic pigs, with a short onset course and an incubation period of 5-15 days. There is a high morbidity and mortality rate, and the mortality rate can even be as high as 100%. The World Organization for Animal Health (OIE) lists it as an animal disease that must be reported, and my country lists it as a first-class animal disease. [0003] ASFV is a complex icosahedral virus with fea...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
IPC IPC(8): C07K14/01C07K19/00C07K16/08C12N15/63G01N33/68G01N33/569A61K39/12A61P31/20
Inventor 王祥喜饶子和孙瑶王佳灵朱丹丹宋庆春
Owner INSITUTE OF BIOPHYSICS CHINESE ACADEMY OF SCIENCES
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com