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

Application of dipterin b protein and/or dipterin b gene and antiviral drugs

An antiviral drug and B protein technology, which is applied in the field of biomedicine to achieve wide application prospects and the effect of inhibiting virus replication

Active Publication Date: 2022-05-24
SHENZHEN CENT FOR DISEASE CONTROL & PREVENTION
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] The purpose of the present invention is to provide an application of dipteric peptide B protein and / or dipteric peptide B gene and antiviral drugs, aiming to solve the technical problem of providing more choices for existing antiviral drugs

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
  • Application of dipterin b protein and/or dipterin b gene and antiviral drugs
  • Application of dipterin b protein and/or dipterin b gene and antiviral drugs
  • Application of dipterin b protein and/or dipterin b gene and antiviral drugs

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0025] Further, in the embodiment of the present invention, the preparation method of the dipteropeptide B protein comprises:

[0026] S01: construct a recombinant plasmid containing the sequence shown in SEQ ID NO.2;

[0027] S02: The recombinant plasmid is transferred into a host cell for expression to obtain the dipteropeptide B protein.

[0028] In the embodiment of the present invention, when verifying the function of dipteropeptide B protein, the function verification can be achieved by constructing a recombinant plasmid that does not have a partial nucleotide sequence expressing the signal peptide in SEQ ID NO. 2. The specific steps include:

[0029] S011: extract the total RNA of Drosophila, and then reverse-transcribe to obtain cDNA;

[0030] S012: Amplify the nucleotide sequence of the non-signal peptide part in SEQ ID NO.2 from the cDNA;

[0031] S013: Connect the nucleotide sequence of the non-signal peptide part in SEQ ID NO. 2 with the backbone plasmid vector t...

Embodiment 1

[0042] Example 1 Validation of dsRNA inhibiting DmDptB gene expression to promote replication of vesicular stomatitis virus

[0043] 1. Preparation of dsRNA

[0044] 1. The primers designed to prepare the coding DNA of the dsRNA that inhibits the expression of the DmDptB gene are as follows:

[0045] DmDptB-F (SEQ ID NO. 3):

[0046]

[0047] DmDptB-R (SEQ ID NO. 4):

[0048]

[0049] In the above primers, the region marked by the box is the T7 promoter sequence.

[0050] 2. The total RNA of S2 cells was extracted and reverse transcribed into cDNA. Using cDNA as a template, PCR amplification was performed with a primer pair composed of DmDptB-F and DmDptB-R to obtain a PCR amplification product.

[0051] 3. Take the PCR amplification product obtained in step 2, use Ambion MEGAscriptT7High YieldTranscription Kit (catalog No. AM1334) and conduct in vitro transcription according to the kit instructions. Since both DmDptB-F and DmDptB-R have T7 promoters, in vitro transcr...

Embodiment 2

[0073] Example 2 Validation of DmDptB protein in inhibiting dengue virus replication

[0074] 1. Construction of recombinant plasmid pMT-DmDptB-V5-HisA

[0075] 1. The total RNA of Drosophila was extracted and reverse transcribed to obtain cDNA.

[0076] 2. Using the cDNA obtained in step 1 as a template, use F1 and R1 primer pairs to carry out PCR amplification to obtain a PCR amplification product. The primer sequences are as follows (the underlined sequences represent restriction sites):

[0077] F1 (SEQ ID NO. 12): 5'-AAGAA gaattc TTATCCCTATCCTGATCCCCG-3’

[0078] F1 (SEQ ID NO. 13): 5'-AAGAA tctaga AAACCTGAAGGTATACACTC-3’

[0079] 3. The PCR amplification product of step 2 was double digested with restriction enzymes EcoRI and XbaI, and the digested product was recovered.

[0080] 4. The plasmid pMT / BiP / V5-HisA was digested with restriction enzymes ECORI and XbaI, and the vector backbone of about 5000 bp was recovered.

[0081] 5. Connect the enzyme cut product obt...

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 technical field of biomedicine, and in particular relates to the application of dipteric peptide B protein and / or dipteric peptide B gene and antiviral drugs. An application of dipterin B protein and / or dipterin B gene in the preparation of antiviral drugs; wherein, the amino acid sequence of the dipterin B protein is shown in SEQ ID NO.1, and the dipterin The nucleic acid sequence of the B gene is shown in SEQ ID NO.2. In the present invention, it is verified by experiments that the dipteric peptide B protein has the function of significantly inhibiting the replication of various viruses. Therefore, the dipteric peptide B protein and / or dipteric peptide B gene can be used to prepare antiviral drugs, and has broad application prospects.

Description

technical field [0001] The invention belongs to the technical field of biomedicine, in particular to the application of a dipteropeptide B protein and / or a dipteropeptide B gene and an antiviral drug. Background technique [0002] After insects are irritated or infected, a class of polypeptides produced by hemolymph has broad-spectrum antibacterial activity, called antimicrobial peptides. According to the characteristics of the polypeptide amino acid composition of antimicrobial peptides, they are mainly divided into 4 types: antimicrobial peptides without cysteine ​​residues (representative: Cecropins), basic polypeptides rich in cysteine ​​residues (representatives) Defensins, death proteins), antimicrobial peptides rich in glycine residues (representatives are dipteran, aggressin), antimicrobial peptides rich in proline residues (representatives are bee peptides). Diptericin was first isolated by Dimarcq from the hemolymph of Phormia terranovae larvae induced by bacteria...

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): C07K14/435C12N15/12A61K38/17A61P31/14
CPCY02A50/30
Inventor 肖小平林颖阳帆黄达娜张仁利
Owner SHENZHEN CENT FOR DISEASE CONTROL & PREVENTION
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