A target of anti-tuberculosis mycobacterium and its application

A technology of Mycobacterium tuberculosis and target, applied in the field of cell biology, can solve the problem that the relationship between Mycobacterium tuberculosis infection and lung cancer has not been reported and so on

Active Publication Date: 2021-05-04
INST OF MICROBIOLOGY - CHINESE ACAD OF SCI
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the correlation between Mycobacterium tuberculosis infection and the occurrence or development of lung cancer has not been 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
  • A target of anti-tuberculosis mycobacterium and its application
  • A target of anti-tuberculosis mycobacterium and its application
  • A target of anti-tuberculosis mycobacterium and its application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] Example 1 The erythroid redoxin domain of the Mycobacterium tuberculosis secretory protein PknG

[0024] Through bioinformatics analysis, it was found that Mycobacterium tuberculosis has a segment of structure domain similar to that of eukaryotic redoxin domain, which we named as rubredoxin domain. This domain exists in the amino acid position 97-139 of the effector protein PknG of Mycobacterium tuberculosis, which can interact with host ubiquitin protein, promote the proliferation and migration of tumor cells and the intracellular survival of Mycobacterium tuberculosis, and its amino acid sequence As shown in SEQ ID NO:1. The sequence of the pknG gene is shown in Gene ID: 886397.

Embodiment 2

[0025] Example 2 PknG interacts with ubiquitin through the rubidoxin domain

[0026] The full-length PknG gene, the gene encoding the redoxin domain (amino acid 97-139 of PknG protein) and the gene encoding the ubiquitin-like domain (amino acid 140-234 of PknG protein) were respectively constructed into pEGFP -On the N1 plasmid; construct ubiquitin (Ub, GI number: 6647297) and its mutant Ub (I44A) (the I44 position of Ub is the key site for non-covalent hydrophobic interaction between Ub and other proteins) into PCS2 On the plasmid; use Lipofectamine 2000 (Invitrogen) to transfect the recombinant plasmid into HEK293T cells; replace the fresh medium after 6 hours of transfection; discard the medium after 24 hours of transfection, wash the cells twice with PBS, and then wash the cells with protease inhibitor The cell lysate was used to lyse the cells; the cell lysate was collected into a 1.5ml centrifuge tube and centrifuged at 13000rpm for 5 minutes; the supernatant was transfe...

Embodiment 3

[0028] Example 3 PknG activates self-shearing function by interacting with Ub

[0029] The full-length gene encoding PknG and the deletion gene of the redoxin domain (PknG△97~139) were respectively constructed on the pEGFP-N1 plasmid; figure 2 Transfect the indicated cells into HEK293T cells; replace the fresh medium 6 hours after transfection; discard the medium 24 hours after transfection, wash the cells twice with PBS, and then lyse the cells with a cell lysate containing protease inhibitors; collect the cells Centrifuge the lysate into a 1.5ml centrifuge tube at 13000rpm for 5 minutes; transfer the supernatant to a new 1.5ml centrifuge tube, add 20 microliters of GFP-Nanoab-Agarose respectively; collect Beads by centrifugation at 4 degrees for 4 hours, The cell lysate was washed 3 times; SDS-PAGE loading buffer was added; after heating in boiling water for 10 minutes, the sample was loaded and detected by Western Blotting.

[0030] The result is as figure 2 As shown, i...

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 an anti-tuberculosis mycobacterium target and application thereof, belonging to the field of cell biology. The present invention discovers a PknG erythroid redoxin resultant domain, which can promote the intracellular survival process of mycobacterium tuberculosis and the proliferation of tumor cells by interacting with host ubiquitin. The present invention can guide the development of anti-mycobacterium tuberculosis antibodies against this domain and the transformation of existing tuberculosis vaccines. For example, inhibitors or drugs targeting this domain can partially inhibit the intracellular survival of Mycobacterium tuberculosis. In addition, this domain in the PknG gene in existing tuberculosis vaccines (such as BCG) can also be deleted to avoid the risk of promoting cancer. At the same time, when the modified vaccine is applied to clinical tumor treatment, it will also avoid side effects such as tumor occurrence.

Description

technical field [0001] The invention relates to an anti-tuberculosis mycobacterium target and application thereof. in the field of cell biology. Background technique [0002] In recent years, the key role of chronic inflammation in the occurrence and development of cancer has been generally recognized, and its mechanism of promoting cancer has become one of the current life science research hotspots. Studies have shown that chronic inflammation caused by viral or bacterial infection is one of the biggest risk factors for liver, colon or stomach cancer. Tuberculosis (TB) is an ancient disease caused by Mycobacterium tuberculosis (Mtb), and it is still one of the infectious diseases that seriously threaten human health around the world. However, the correlation between Mycobacterium tuberculosis infection and the occurrence or development of lung cancer has not been reported. Contents of the invention [0003] The present invention predicts through bioinformatics analysis...

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): C07K14/35A61K39/00A61K45/00A61P31/06A61P35/00
CPCA61K39/00A61K45/00A61P31/06A61P35/00C07K14/35
Inventor 刘翠华汪静
Owner INST OF MICROBIOLOGY - CHINESE ACAD OF SCI
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap