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
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  • 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 pept

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  • 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
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Example Embodiment

[0042]Example 1 Pork fever antigenic epitope peptide

[0043]In this embodiment, four key antigenic epitope peptide ER1, ER2, ER3, and ER4 were designed in accordance with N-ends of the ASFV P72 antigen.

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

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

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

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

[0048]ER1, ER2, ER3 and ER4 can be embedded in either or in the arrangement of the CAP protein, the immune dominant region of the hepatitis B core antigen monomer, the human iron protein, and the trimer protein, and the expression of rec...

Example Embodiment

[0049]Example 2 Preparation of recombinant antigen HBCAG-ER4

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

[0051](1) Gene synthesis and molecule construction: ER4 antigenic epitope peptide gene sequence is embedded between the 79-80AA of the gene sequence of the HBCAG protein skeleton (HBCAG protein skeleton such as the amino acid sequence shown in SEQ ID NO. ", and will The obtained recombinant gene sequence is inserted between the PET-28A carrier NCOI and XHOI to obtain a recombinant plasmid. The above genes were constructed of the above genes by Nanjing Jinsuri.

[0052](2) Plasmid transformation: 2 μl of the recombinant plasmid (80 ng / μL), ice bath, 30 minutes, and 112 ° C after 30 minutes of ice bath to E. coli BL21 (DE3) sensitic cells (purchased from Bomide). The heat shovel is 90 seconds, and then placed in ice for 2 minutes, after 800 μl of LB medium, placed in a constant temperature oscillating incubator, 37 ° C, 200 rpm for 1 hour. 100 ...

Example Embodiment

[0055]Example 3 Preparation of recombinant antigen HBCAG-ER2

[0056]The preparation method of the present embodiment is substantially the same as that of Example 2, and the difference is only that in step (1) gene synthesis and molecular construction, it is embedded in the HBCAG protein skeleton for gene sequences of ER2 antigenic epitope peptide (HBCAG protein skeleton, such as SEQ) The amino acid sequence shown in IDNO.5 is between 79-80AA, and the obtained recombinant gene sequence is inserted between the PET-28A carrier NCOI and XHOI to obtain a recombinant plasmid. The above genes were constructed of the above genes by Nanjing Jinsuri. among them,image 3 SDS-PAGE results of HBCAG-ER2 recombinant antigen,Figure 4 The HBCAG-ER2 recombinant antigen is shown, and the HBCAG-ER2 recombinant antigen is showneed into virological particles in accordance with the expected success, and can be seen from the negative electron microscope picture, which can be seen from 30 nm-40 nm. Improve the...

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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

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Application Information

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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
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