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

Preparation and application of antimicrobial peptide fusion cytokine campils co-expression biological preparation

A technology of biological materials and immune cells, applied in the direction of fusion polypeptide, antibody mimic/scaffold, cells modified by introducing foreign genetic material, etc., can solve problems such as decreased immune resistance, threats to human health, and weakened health levels , to inhibit the growth of

Active Publication Date: 2020-09-29
SICHUAN UNIV
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The abuse of feed antibiotic additives not only increases the cost of feeding, but also leads to a significant increase in the drug resistance and pathogenicity of pathogenic microorganisms, and the health of livestock and poultry bodies is weakened due to the side effects of drugs, and the immunity and disease resistance are significantly reduced
In such a vicious cycle, various severe infectious diseases of livestock and poultry frequently occur, making it difficult to control and treat
On the other hand, drug residues and the increasingly serious food safety problems of livestock and poultry products not only directly threaten the health of human beings themselves, but also hinder the development of the breeding industry.
[0006] The addition of antibiotics to animal feed, long-term or inappropriate use will not only induce drug resistance in bacteria, but also cause drug residues in animal products, causing serious food safety hazards, damaging human health and inducing the failure of drugs used to treat antibiotics

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
  • Preparation and application of antimicrobial peptide fusion cytokine campils co-expression biological preparation
  • Preparation and application of antimicrobial peptide fusion cytokine campils co-expression biological preparation
  • Preparation and application of antimicrobial peptide fusion cytokine campils co-expression biological preparation

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0117] Embodiment 1, antimicrobial peptide (CAMPILs) has bacteriostasis

[0118] The present invention provides an antimicrobial peptide named CAMPILs, its amino acid sequence is shown in sequence 1 in the sequence listing, and the nucleotide sequence encoding CAMPILs is shown in sequence 2.

[0119] 1. Preparation of recombinant yeast SMDpG-P

[0120] 1. Preparation of recombinant bacteria

[0121] Replace the DNA fragment between the EcoR I and Xba I recognition sequences of the pGAPZα A vector with the CAMPILs gene shown in Sequence 2, keep the other sequences of the carrier unchanged, and obtain a recombinant vector, which is named pGAPZα A-P (abbreviated as pG- P). pG-P can express antimicrobial peptides (CAMPILs) shown in sequence 1.

[0122] Use AvrII to digest pG-P to obtain linearized pG-P; introduce linearized pG-P into Pichia pastoris SMD1168, and screen to obtain recombinant yeast with linearized pG-P inserted in the genome. The recombinant yeast is named SMDpG-...

Embodiment 2

[0160] Embodiment 2, the biological activity research of SMDpG-P fermentation product in mice

[0161] 1. Preparation of fermentation products

[0162] The SMDpG-P (hereinafter referred to as SGP) of Step 1 of Example 1 was activated and inoculated in a 100mL Erlenmeyer flask containing 30mL of YPD medium, and cultivated at 30°C and 220rpm for 48h to make the OD 600 About 25 to obtain the SGP fermented liquid.

[0163] According to the above method, the SMDpG-P was replaced by the SMDpG (hereinafter referred to as SG) in the first step of Example 1, and the other steps were all unchanged to obtain the SG fermentation broth.

[0164] 2. Grouping of experimental ICR mice

[0165] Take 80 18-20g 3-week-old healthy female ICR mice, randomly divide them into 8 groups, 10 mice in each group, and the group numbers are 1-8, of which Group 1, Group 4, and Group 7 are SG negative control groups, Groups 3 and 6 are vaccine negative control groups, and groups 2, 5 and 8 are experimenta...

Embodiment 3

[0189] Embodiment 3, the biological activity research of SMDpG-P fermentation product in piglet body

[0190] 1. Preparation of fermentation products

[0191] The SMDpG-P (hereinafter referred to as SGP) of Step 1 of Example 1 was activated and inoculated in a 100mL Erlenmeyer flask containing 30mL of YPD medium, and cultivated at 30°C and 220rpm for 48h to make the OD 600 About 40, obtain the SGP fermented liquid.

[0192] According to the above method, the SMDpG-P was replaced by the SMDpG (hereinafter referred to as SG) in the first step of Example 1, and the other steps were all unchanged to obtain the SG fermentation broth.

[0193] 2. Experimental animals were fed fermentation broth

[0194] Seventeen 45-day-old healthy Tibetan pigs weighing about 8 kg were selected from the Jianyang Base of Sichuan Breeding Pig Performance Testing Center, and randomly divided into the experimental group (9 pigs) and the control group (8 pigs). Each pig in the experimental group was f...

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 discloses the preparation and application of an antimicrobial peptide fusion cytokine CAMPILs co-expression biological preparation. The antimicrobial peptide fusion cytokine CAMPILs provided by the present invention is as follows A1), A2) or A3): A1) the amino acid sequence is the protein of sequence 1 in the sequence listing; A2) the amino acid sequence shown in sequence 1 in the sequence listing is passed through a or several amino acid residue substitutions and / or deletions and / or additions and proteins with the same function; A3) A fusion protein obtained by linking tags at the N-terminal or / and C-terminal of A1) or A2). Experiments have proved that CAMPILs of the present invention can promote the proliferation of lymphocytes, red blood cells and white blood cells, inhibit the growth of pathogenic microorganisms, promote the secretion of non-specific antibodies (IgG, IgG1, IgG2a) and disease-specific antibodies, and improve the immunity and survival of animals. Rate.

Description

technical field [0001] The invention relates to the preparation and application of an antimicrobial peptide fusion cytokine CAMPILs co-expression biological preparation in the field of biotechnology. Background technique [0002] The aquaculture industry (animal husbandry and aquatic products) is an important part of large-scale agriculture. It is one of the important foundations for my country's agricultural modernization, rural economic development, and social stability. The aquaculture industry in advanced countries in Europe and the United States is very developed, accounting for 50% of large-scale agriculture. % above the specific gravity. It provides human beings with meat, milk, eggs, fur and other high-grade foods and important textile raw materials. Animal products are the main source of high-quality protein, minerals, vitamins and other nutrients for people. Their safety is directly related to human health. In recent years, vicious events such as poisoning and dise...

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
Patent Type & Authority Patents(China)
IPC IPC(8): A61K38/16C07K19/00C12N15/62C12N15/63C12N1/15C12N1/19C12N1/21C12N5/10A61P37/04A61P31/00A61K48/00
CPCA61K38/16A61K48/005C07K14/00C07K2319/00
Inventor 高荣万小平陈骞王泽洲胡立博黎凌陈建林吕学斌李江凌
Owner SICHUAN UNIV
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