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

A h1n1 influenza virus antibody and its application in ultra-trace detection of h1n1 virus

An influenza virus and antibody technology, applied in the field of biotechnology influenza virus antibodies, can solve the problems of undiminished virulence and transmission performance, patient neuraminidase inhibitor resistance, side effects, etc., and achieve important economic and social significance. Effect

Active Publication Date: 2021-03-23
WEIFANG MEDICAL UNIV +1
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Ion channel inhibitors include amantadine and rimantadine and their derivatives. Long-term use will cause side effects in the gastrointestinal tract and central nervous system, and lead to the generation of drug-resistant strains with undiminished virulence and transmission performance; The neuraminidase inhibitors mainly include zanamivir and oseltamivir, which have a good therapeutic effect on patients with H1N1 influenza in the early stage, but patients after treatment are likely to develop resistance to neuraminidase inhibitors

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 h1n1 influenza virus antibody and its application in ultra-trace detection of h1n1 virus
  • A h1n1 influenza virus antibody and its application in ultra-trace detection of h1n1 virus
  • A h1n1 influenza virus antibody and its application in ultra-trace detection of h1n1 virus

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[0048] Use inactivated H1N1 virus particles to immunize mice, and after influenza virus antibodies appear in the mouse blood, remove the spleen of the mice, extract the total ribonucleic acid (RNA) and synthesize DNA (cDNA) with a complementary base sequence to the RNA chain , using antibody-specific primers, perform a polymerase chain reaction (PCR) to amplify the antibody gene. After the antibody gene was processed, it was cloned into the phage display vector pDong1, and the constructed vector was used to further transform Escherichia coli TG-1 to make a phage display antibody library. The H1N1 virus was screened to obtain an antibody F1, which can bind to the H1N1 virus but not to bovine serum albumin, and has specificity to the H1N1 virus. The specific process is as follows:

[0049] 1. Immunization of mice and confirmation of anti-H1N1 antibody in mouse serum after immunization

[0050] Firstly, mice were immunized with inactivated H1N1A / Beijing / 262 / 95 virus. The mice ...

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

PropertyMeasurementUnit
molecular weightaaaaaaaaaa
absorbanceaaaaaaaaaa
Login to View More

Abstract

The invention discloses an H1N1 influenza virus antibody and application thereof in ultra-micro detection of H1N1 viruses. The H1N1 influenza virus antibody comprises a heavy chain variable region, afirst heavy chain hypervariable region, a second heavy chain hypervariable region, a third heavy chain hypervariable region, a light chain variable region, a first light chain hypervariable region, asecond light chain hypervariable region and a third light chain hypervariable region. The H1N1 influenza virus antibody can be specifically combined with the H1N1 influenza viruses, and is used for ultra-micro detection of H1N1 influenza to achieve early prevention and treatment of the H1N1 influenza, thereby being of great economic and social significance.

Description

technical field [0001] The invention relates to the field of biotechnology influenza virus antibody technology, in particular to an H1N1 influenza virus antibody and its application in ultra-trace detection of H1N1 virus. Background technique [0002] Influenza virus (Influenzavirus) is an infectious disease pathogen that can cause influenza, and highly pathogenic influenza virus can cause the death of humans and animals. The virus belongs to the family Orthomyxoviridae and belongs to the genus Influenzavirus. According to the antigenicity of nucleoprotein and matrix protein, influenza virus can be divided into three types: A, B, and C. There are two important proteins, hemagglutinin (HA) and neuraminidase (NA), on the surface of virus particles. According to the difference of these two proteins, influenza viruses can be divided into multiple subtypes, with A For example, HA has 18 subtypes (H1-H18) and NA has 11 subtypes (NA1-11). The surface protein of type A influenza ...

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): C07K16/10C12N15/11G01N33/569
CPCC07K16/1018C07K2317/56G01N33/56983G01N2469/10
Inventor 董金华董航单喜军李海梅陈丽梅
Owner WEIFANG MEDICAL 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