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

Compositions and methods using same for the detection of viruses

A composition and virus technology, applied in the direction of biochemical equipment and methods, virus antigen components, measuring devices, etc.

Inactive Publication Date: 2009-08-05
MND DIAGNOSTICS LTD
View PDF30 Cites 11 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0012] However, none of the aforementioned methods describe, suggest, or mention the selection of viral substrates for optimal affinities that ultimately enable rapid simultaneous analysis of multiple samples, multiple viruses, and specific identification of novel strains.

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
  • Compositions and methods using same for the detection of viruses
  • Compositions and methods using same for the detection of viruses
  • Compositions and methods using same for the detection of viruses

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0160] In general, peptide synthesis methods involve the sequential addition of one or more amino acids or appropriately protected amino acids to a growing peptide chain. Usually, the amino or carboxyl group of the first amino acid is protected with an appropriate protecting group. The complimentary group (amino or carboxyl) of the amino acid is suitably protected by adding the next amino acid in the sequence under conditions suitable for the formation of an amide bond, and the protected or modified amino acid can either be combined with an inert Solid supports are attached or used in solution. The protecting group is then removed from the newly added amino acid residue, and the next amino acid (appropriately protected) is added, etc.; traditionally, this process is also accompanied by washing steps. After all desired amino acids have been attached in the correct order, any remaining protecting groups (and any solid support) are sequentially or simultaneously removed to obtai...

Embodiment 1

[0249] Identification of Consensus Cutting Sequence of Hepatitis C NS3 Protease

[0250] The identification of an optimized cleavage sequence for the hepatitis C NS3 protease is described below.

[0251] Phase 1: Obtaining the mechanism by which the polyprotein is cleaved by its viral protease, the gist of which is the sequence of cleavage events in the viral life cycle (1, 4, see from Hepatitis C virus (HCV) Figure 11 : Models structure and genome organization (model structure and genome organization structure), Vol 5; November 19, 2003, Cambridge University Press).

[0252] Stage 2: Using databases such as Swiss prot., Pubmed, Gene bank and OWL to compare all cut sequences of as many strains of the same virus as possible, and align them using FASTA software (see Table 1 below).

[0253] Table 1

[0254]

[0255]

[0256] E1NS1

cell HCV 633202 FSGVDA|ETYIT 99 E1NS1

cell HCV 221615 ISQAEA|ALENL 100 E2NS1

cell HCV 22129793...

Embodiment 2

[0312] Kinetic optimized substrates identified according to the teachings of the present invention

[0313] The following notations are used to denote expressions of consensus sequences.

[0314] Hydrophobic amino acids: G, A, V, L, I, M, W, F, Y, H

[0315] Basic amino acids: Q, N, K, H, R

[0316] HB donor: K, R, S, C, T, Q, N, Y

[0317] Acidic amino acids: E, D, Y

[0318] Aromatic amino acids: Y, F, H, W

[0319] - / -: cleavage site

[0320] Adenoviridae (1-9):

[0321] Ape: Adenovirus 25, Adenovirus 24, Adenovirus 23, Adenovirus 22, Adenovirus 21, Adenovirus 19.

[0322] Pig: Adenovirus C, Adenovirus B, Adenovirus A, Adenovirus 5, Adenovirus 4, Adenovirus 3, Adenovirus 2, Adenovirus 1.

[0323] Sheep: Adenovirus B, Adenovirus A, Adenovirus 5, Adenovirus 4, Adenovirus 3, Adenovirus 2, Adenovirus 1.

[0324] Mouse: Adenovirus A, Adenovirus 1.

[0325] Human: Adenovirus F, Adenovirus E, Adenovirus D, Adenovirus C, Adenovirus B, Adenovirus A, Adenovirus 9, Adenovirus 8...

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

An isolated peptide is provided. The isolated peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46 and 47, said amino acid sequence being no more than 14 amino acids in length. Also provided are compositions which comprise the peptides and use of same in the detection of viruses.

Description

technical field [0001] The present invention relates to novel compositions for the rapid and simple detection of the cleavage activity of catalytic molecules. The invention also provides diagnostic tests and kits employing these compositions. Background technique [0002] Rapid, specific and cost-effective detection of health-related agents, whether markers of disease or health risks, markers or factors of normal and pathogenic processes or disease, or indicators of exotic pathogens and their by-products growing demand. With the repeated outbreaks of infectious diseases sweeping the world such as HIV, SARS, bird flu, West Nile fever, and drug-resistant pathogenic bacteria diseases, the above needs are made even more significant. Facing the threat of increasing epidemic and pandemic disease outbreaks, early detection of causative agents is crucial for adequate attention and prevention. However, the cost, complexity, and inefficiency of many currently available pathogen det...

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): A61K38/00A61K39/00A61K39/12A61K39/385C12Q1/00G01N33/53G01N33/542
CPCY02A50/30
Inventor 阿萨夫·以斯拉多里特·阿拉德吉拉德·韦里德
Owner MND DIAGNOSTICS LTD
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