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

Tuberculosis-resisting-drug-related efflux-protein-sourced tuberculosis resisting CTL (Cytotoxic T Lymphocyte) epitope peptide and application thereof

A technology for efflux proteins and epitope peptides, which is applied in the direction of peptides, antibacterial drugs, bacterial antigen components, etc., and can solve the problem of few reports on membrane proteins

Active Publication Date: 2013-06-26
ZHENGZHOU UNIV
View PDF2 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

CD8 currently studied + CTL protein epitopes are mainly concentrated on tuberculosis-specific secreted proteins, such as ESAT-6, CFP-10, CFP-21, MPT64, Ag85 complexes, etc., while for membrane proteins, especially the drug efflux protein CD8+CTL Epitopes are rarely reported

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
  • Tuberculosis-resisting-drug-related efflux-protein-sourced tuberculosis resisting CTL (Cytotoxic T Lymphocyte) epitope peptide and application thereof
  • Tuberculosis-resisting-drug-related efflux-protein-sourced tuberculosis resisting CTL (Cytotoxic T Lymphocyte) epitope peptide and application thereof
  • Tuberculosis-resisting-drug-related efflux-protein-sourced tuberculosis resisting CTL (Cytotoxic T Lymphocyte) epitope peptide and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0013] The anti-tuberculosis CTL epitope peptide derived from the tuberculosis drug resistance-related efflux protein of the present invention is a nonapeptide, and the amino acid sequence of the nonapeptide is:

[0014] P5: Tyr-Leu-Gly-Gly-Thr-Thr-Gly-Pro-Val (YLGGTTGPV) molecular weight: 864.6 (theoretical value: 863.44)

[0015] Or P6: Tyr-Ile-Val-Gly-Phe-Cys-Leu-Leu-Val (YIVGFCLLV) Molecular weight: 1026.7 (theoretical value: 1025.86)

[0016] or P7: Thr-Leu-Thr-Trp-Leu-Phe-Ala-Phe-Val (TLTWLFAFV) molecular weight: 1097.7 (theoretical value: 1097.32)

[0017] or P8: Gly-Leu-Val-Ala-Gly-Leu-Ser-Ala-Val (GLVAGLSAV) molecular weight: 786.7 (theoretical value: 786.7)

[0018] Or P9: Ala-Leu-Gly-Met-Leu-Ile-Ala-Gly-Leu (ALGMLIAGL) molecular weight: 858.7 (theoretical value: 857.81)

[0019] or P10: Met-Leu-Ile-Ala-Gly-Leu-Pro-Cys-Leu (MLIAGLPCL) molecular weight: 930.6 (theoretical value: 930.24)

[0020] or P11: Leu-Leu-Cys-Ala-Ile-Phe-Ala-Glu-Val (LLCAIFAEV) molecular weig...

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 a tuberculosis-resisting-drug-related efflux-protein-sourced tuberculosis resisting CTL (Cytotoxic T Lymphocyte) epitope peptide which is a nonapeptide, wherein the amino acid sequence of the nonapeptide is P8: GLVAGLSAV. According to the tuberculosis-resisting-drug-related efflux-protein-sourced tuberculosis resisting CTL epitope peptide, immunological informatics means are adopted according to a primary structure of an antigen, an HLA-A*0201-restrictive CTL epitope of a tuberculosis-resisting-drug-related protein antigen is subjected to predictive analysis by using databases, namely SYFPEITHI, BIMAS and NetCTL1.2, the epitope peptide is obtained through screening, and assayed nonapeptides are not reported in documents. The epitope peptide is assayed through in-vitro ELISPOT experiments, and the results provide a theoretical basis for the development of tuberculosis vaccines based on resisting-drug-associated protein antigens and provide more information for designing tuberculosis multi-epitope peptide vaccines based on mixed T cell epitopes.

Description

[0001] The patent application of the present invention is a patent application number: 201110138646.2, application date: May 26, 2011, and a divisional application titled "Anti-tuberculosis CTL epitope peptide derived from efflux protein related to tuberculosis drug resistance and its application". technical field [0002] The present invention relates to a therapeutic polypeptide vaccine for tuberculosis, in particular to an anti-tuberculosis CTL epitope peptide with therapeutic activity screened out by using the tuberculosis self-resistance-related antigen, and also relates to the application of the peptide in the preparation of a therapeutic polypeptide vaccine for tuberculosis . Background technique [0003] The increasing number of drug-resistant Mycobacterium tuberculosis is an important reason for the resurgence of tuberculosis in recent years. The drug resistance mechanism of Mycobacterium tuberculosis can be divided into natural drug resistance mechanism and acquire...

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): C07K7/06A61K39/04A61P31/06
Inventor 祁元明陈飞高艳锋朱宇皇吴亚红陈艳平韩艳林
Owner ZHENGZHOU 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

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