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

Monoclonal antibody recongnizing epitope for HCV (hepatitis C virus) NS3 helicase ATP (adenosine triphosphate) binding site

A hepatitis C virus, monoclonal antibody technology, applied in the direction of antibodies, antiviral agents, antibody medical components, etc., can solve the problems of complicated operation, inability to be widely used, expensive, etc., and achieve the effect of good specific recognition ability

Inactive Publication Date: 2012-11-07
SOUTHERN MEDICAL UNIVERSITY
View PDF4 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] In addition, the current main diagnostic method for HCV is to detect HCV antibodies in serum by radioimmunodiagnosis (RIA) or enzyme-linked immunoassay (ELISA), but antibody detection generally has a window period of 7 to 10 weeks, which threatens the safety of blood use.
Detection of HCV nucleic acid can effectively shorten the window period, but it cannot be widely used due to its complicated operation, easy contamination and high price

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
  • Monoclonal antibody recongnizing epitope for HCV (hepatitis C virus) NS3 helicase ATP (adenosine triphosphate) binding site
  • Monoclonal antibody recongnizing epitope for HCV (hepatitis C virus) NS3 helicase ATP (adenosine triphosphate) binding site
  • Monoclonal antibody recongnizing epitope for HCV (hepatitis C virus) NS3 helicase ATP (adenosine triphosphate) binding site

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0032] The present invention will be further described below in combination with specific experiments, but it is not limited thereto.

[0033] Referring to the literature, the truncated HCV NS3 (1192aa~1459aa) belongs to the immunologically active region, and was determined as the target protein to be expressed. The HCV NS3 protein can be prepared by genetic engineering, or the purified HCV NS3 protein can be purchased directly.

[0034] The gene method is as follows: the DNA sequence encoding HCV NS3 (1192aa~1459aa) is cloned by PCR method, and then inserted into the multi-cloning site of the expression vector to construct the recombinant expression plasmid, and then transformed into the expression host bacteria to construct the engineering Bacterial strains, engineered strains are induced to express, isolated and purified to obtain HCV NS3 recombinant protein. This specific method is many kinds, and a specific embodiment is given as an example below:

[0035] Constructio...

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 monoclonal antibody recongnizing epitope for HCV (hepatitis C virus) NS3 helicase ATP (adenosine triphosphate) binding site The epitope has the following amino acid sequence: PTGSGKSTK (SEQ ID NO: 1). The invention also discloses a monoclonal antibody capable of recongnizing the epitope and an application of the epitope and the monoclonal antibody. The monoclonal antibody recongnizing epitope for HCV NS3 helicase ATP binding site is a newly discovered NS3 protein epitope which lies in the ATP binding site of the first region of NS3C terminal helicase. The monoclonal antibody of the present invention can specifically identify the above-mentioned ATP binding site, making the activity of the helicase diminished or disappeared, thus affecting the combination of replication antibody of HCV and this site, and is expected to achieve the purpose of treating HCV.

Description

technical field [0001] The invention relates to a hepatitis C virus NS3 protein B cell epitope, which is the hepatitis C virus NS3 helicase ATP binding site monoclonal antibody recognition epitope, and the anti-hepatitis C obtained by stimulating the cell epitope The monoclonal antibody of NS3 protein also relates to the application of the cell epitope and the application of the antibody stimulated by the cell epitope. Background technique [0002] Hepatitis C is a disease mainly transmitted by blood. Chronic infection of hepatitis C virus (HCV) can lead to chronic inflammation, necrosis and fibrosis of the liver. Some patients may develop liver cirrhosis or even hepatocellular carcinoma (HCC). It is extremely harmful to health and life, and has become a serious social and public health problem. According to the statistics of the World Health Organization, the global HCV infection rate is about 3%, it is estimated that about 170 million people are infected with HCV, and abo...

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): C07K7/06G01N33/68A61K39/29A61P31/14C07K16/10G01N33/577A61K39/42
Inventor 黎诚耀边奕鑫李婷婷王文敬
Owner SOUTHERN MEDICAL UNIVERSITY
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