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RTG fusion protein capable of enhancing immunogenicity and immune protection effect

A technology for immune protection and immune enhancement, applied in the field of genetic engineering, can solve the problems of weak cellular immune response and achieve the effect of improving ability and good immunogenicity

Pending Publication Date: 2022-05-24
HEILONGJIANG BAYI AGRICULTURAL UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0003] GapC (Glyceraldehyde-3-phosphate dehydrogenase C, GapC) is a streptococcal surface protein with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) activity, which is crucial to the growth and survival of bacteria. Different streptococcal GapC proteins The homology is more than 90.77%, and it has been proven to have good immunogenicity, which can mediate the body to produce specific antibodies and play an anti-streptococcal infection effect, but the level of cellular immune response induced by it is relatively weak

Method used

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  • RTG fusion protein capable of enhancing immunogenicity and immune protection effect
  • RTG fusion protein capable of enhancing immunogenicity and immune protection effect
  • RTG fusion protein capable of enhancing immunogenicity and immune protection effect

Examples

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Effect test

Embodiment 1

[0024] This example illustrates the immunogenicity of fusion protein RTG.

[0025] 1. Construction of recombinant fusion protein

[0026] According to the amino-terminal sequence of Streptococcus agalactiae GapC published by Genebank (ID: AAM73770.1), the GSGSGSGS protein flexible Linker was used to convert APL R106A The amino acid sequence of (RNFGGFKSYRLLAPAKGTTY) is concatenated with amino acids 1-150 of GapC of Streptococcus agalactiae to form a recombinant fusion protein APL R106A -GapC 1-150 , named RTG (such as figure 1 shown). Codon optimization was used for codon optimization, and Primer 5.0 was used to design specific upstream and downstream primers. The BamH I restriction site was introduced at the 5' end of the upstream primer, and the Xho I restriction site was introduced at the 3' end of the downstream primer. The primer sequences are shown in Table 1, and the underlines represent restriction enzyme cleavage sites. The target gene was amplified by PCR and co...

Embodiment 2

[0044] This example illustrates the immunoprotective effect of fusion protein RTG.

[0045] 1. Immunization of experimental animals

[0046] SPF grade 4-6 weeks old female BALB / c mice were randomly divided into RTG experimental group, APL R106A Experimental group, GapC 1-150 The experimental group and the PBS control group were given free access to food and water. After a week of feeding, the purified protein was emulsified with Freund's complete adjuvant in a volume ratio of 1:1, and injected into the leg muscle by intramuscular injection into each mouse. 50 μg, three weeks after the primary immunization, the same amount of immunogen was emulsified with incomplete Freund's adjuvant and the mice were immunized again. PBS was simultaneously emulsified with the same adjuvant as a control.

[0047] 2. Culture of strains and challenge test of experimental animals

[0048] Take out the glycerol bacteria Streptococcus agalactiae HLJ-6 strain and Staphylococcus aureus Newman stra...

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Abstract

The invention relates to an RTG fusion protein capable of enhancing immunogenicity and immune protection effect, which is formed by carrying out series fusion expression on a modified peptide ligand APLR106A obtained by mutating an epitope peptide of staphylococcus aureus TRAP and streptococcus agalactiae GapC1-150 through Linker-(GS) 4, and the amino acid sequence of the RTG fusion protein is as shown in SEQ ID No.1. The invention also discloses a function of the RTG fusion protein. According to the present invention, the APLR106A and the GapC1-150 are subjected to series fusion expression through the flexible Linker to obtain the recombinant fusion protein RTG, the APLR106A can significantly enhance the level of the cellular immune response and the humoral immune response induced by the GapC1-150, and the recombinant fusion protein RTG has good immunogenicity, and can simultaneously improve the streptococcus resistance and the staphylococcus aureus resistance of the body.

Description

technical field [0001] The invention belongs to the field of genetic engineering, and relates to an RTG fusion protein, in particular to an RTG fusion protein capable of enhancing immunogenicity and immune protection. Background technique [0002] Streptococcus is a widely distributed pathogenic bacteria that can cause multi-organ infection and fatal sepsis and meningitis. In recent years, the infection rate of pregnant women, the elderly and people with low immunity has increased year by year. In addition, Streptococcus is also one of the important pathogenic bacteria that cause mastitis in dairy cows, causing huge economic losses to the global dairy farming industry. Although antibiotic treatment can relieve symptoms, the efficacy of antibiotic treatment is declining year by year due to increasing drug resistance. Vaccination is the most effective alternative to antibiotic treatment. Early streptococcal vaccine development focused on enhancing the humoral immune response....

Claims

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Application Information

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IPC IPC(8): C07K19/00A61K39/116A61K39/085A61K39/09A61P31/04
CPCC07K14/31C12N9/0008C12Y102/01012A61K39/085A61K39/092A61P31/04C07K2319/00A61K2039/70Y02A50/30
Inventor 陈晶崔玉东李皖豫
Owner HEILONGJIANG BAYI AGRICULTURAL UNIVERSITY
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