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

H-2d restricted Th epitope P2 of trichina paramyosin, its composition and application thereof

A composition and antigen epitope technology, applied in the field of immunobiology, can solve problems such as difficult correct diagnosis, difficult drug treatment, repeated infection of the worm, etc.

Active Publication Date: 2016-08-03
CAPITAL UNIVERSITY OF MEDICAL SCIENCES
View PDF3 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Due to the complex clinical symptoms of trichinellosis, including diarrhea, fever, myalgia, edema, etc., it is difficult to diagnose correctly, which makes timely drug treatment difficult and drug treatment cannot solve the problem of repeated infection of the worm (GottsteinB, PozioE, Nockler K. Epidemiology, diagnosis, treatment, and control of trichinellosis. [J]. Clin Microbiol Rev, 2009, 22 (1): 127-145.)

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
  • H-2d restricted Th epitope P2 of trichina paramyosin, its composition and application thereof
  • H-2d restricted Th epitope P2 of trichina paramyosin, its composition and application thereof
  • H-2d restricted Th epitope P2 of trichina paramyosin, its composition and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0053] Embodiment 1: Preparation of rTs-Pmy protein

[0054] The Ts-Pmy plasmid bacterial liquid is transformed into Escherichia coli with a full-length plasmid containing the paramyosin gene (Ts-PmyGenBankaccessionNo.: EF429310) reading frame, which is equivalent to the implementation in the patent application with the publication number CN100999737A (application number 200710000018.1). Escherichia coli BL21 transformed with the paramyosin gene (Ts86cDNA) prepared in Example 2, and its preparation method can also refer to this patent application. The recombinant Ts-Pmy protein (rTs-Pmy protein) was prepared with reference to this patent application.

Embodiment 2

[0055] Embodiment 2: the synthesis of polypeptide sequence

[0056] 12 polypeptide sequences were synthesized according to the amino acid sequence of the recombinant Ts-Pmy protein (rTs-Pmy protein), as shown in Table 1 below. Wherein the position refers to the amino acid position on the rTs-Pmy protein.

[0057] Entrust Beijing Ovia Biotechnology Co., Ltd. to synthesize.

[0058] Table 1: Peptide sequences

[0059]

Embodiment 3

[0060] Embodiment 3: In vitro test identification of polypeptide

[0061] 1. Experimental samples:

[0062] The recombinant Ts-Pmy protein (rTs-Pmy) prepared in Example 1.

[0063] Polypeptides P1-P12 synthesized in Example 2.

[0064]2. Experimental animals and groups:

[0065] BALB / c female mice aged 6-8 weeks were randomly divided into two groups, the recombinant protein group and the PBS control group, with 6 mice in each group.

[0066] 3. Experimental method

[0067] (1) Immunization of animals: rTs-Pmy 50 μg (dissolved in 50 μl PBS) or PBS 50 μl plus an equal volume of adjuvant MONTANIDE per mouse TM ISA50V2 (Seppic Company), multi-point subcutaneously immunized mice, boosted immunization twice with the same dose after 2 weeks and 4 weeks.

[0068] (2) Proliferation and isolation of spleen lymphocytes:

[0069] One week after the last immunization, the mice were killed and splenic lymphocytes were isolated (operated according to the instructions of the mouse lym...

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 immunobiology, and relates to H-2d restricted Th epitope P2 of trichina paramyosin, its composition and an application thereof. The invention concretely relates to Th2 epitope of trichina paramyosin, which contains an amino acid sequence shown in any one of SEQ ID NO: 2-5. The epitope of the present invention can stimulate / promote significant proliferation of splenic lymphocyte, can stimulate / promote cells increase of mice spleen cell CD4<+>T, can stimulate / promote differentiation of Th0 cell to Th2, can stimulate / promote increase of Th1-type cytokine IFN-gamma, IL-2 and Th2-type cytokine IL-4, IL-5, and can stimulate / promote differentiation of Th0 cell to Th2, after mice is immunized, a Th2 immunization reaction is generated through induction, and the epitope has potential for preparing vaccines such as multi-epitope vaccine.

Description

technical field [0001] The invention belongs to the field of immunobiology, and relates to a trichinella paramyosin Th2 epitope, such as trichinella spiralis paramyosin H-2d restricted Th epitope P2. The invention also relates to its composition and application. Background technique [0002] Trichinellosis is a zoonotic parasitic disease with global distribution. Human infection mainly comes from the highly pathogenic Trichinella spp. (Pozio E. World distribution of Trichinella spp. infections in animals and humans. [J]. Vet Parasitol, 2007, 149 (1-2): 3-21.). Due to the complex clinical symptoms of trichinellosis, including diarrhea, fever, myalgia, edema, etc., it is difficult to diagnose correctly, which makes timely drug treatment difficult and drug treatment cannot solve the problem of repeated infection of the worm (GottsteinB, PozioE, Nockler K. Epidemiology, diagnosis, treatment, and control of trichinellosis. [J]. Clin Microbiol Rev, 2009, 22(1): 127-145.). The p...

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 Applications(China)
IPC IPC(8): C07K14/435C12N15/12C07K19/00A61K39/00A61K47/48A61P33/10A01N47/44A01P5/00C07K16/18A61K39/395
Inventor 诸欣平顾园杨静黄京京
Owner CAPITAL UNIVERSITY OF MEDICAL 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