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

Vaccine

a technology of vaccines and antibodies, applied in the field of vaccines, can solve the problems of m proteins causing harmful host immune responses, affecting the immune response of the host, so as to reduce the colonisation of the throat, reduce the burden on healthcare resources, and effectively stimulate the immune response.

Inactive Publication Date: 2008-07-24
ID BIOMEDICAL CORP LAVAL +1
View PDF44 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

This is not life threatening and usually treatable with antibiotics, however such large numbers of affected puts considerable burden on healthcare resources.
A number of complications have been reported to occur subsequent to the primary infection, including in some cases invasive, life threatening diseases.
The M proteins may also induce harmful host immune responses through their ability to induce cross-reactive antibody and T cell responses in humans.
Added to the variability and number of these proteins, the development of an effective vaccine against a variety of serotypes has been problematic.
The most significant impediment to the use of synthetic peptides as vaccines (parenteral delivery) has been that they are only weakly or non-immunogenic when injected by themselves into animals.
Selecting a carrier protein for peptide vaccines is problematic.
Besides insufficient titres against the various peptides, the development of the conjugates can be both expensive and time consuming.
In general, it is difficult to induce a secretory, and also systemic, immunity when using the mucosal route for a subunit (peptide) vaccine without added adjuvant.

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
  • Vaccine
  • Vaccine
  • Vaccine

Examples

Experimental program
Comparison scheme
Effect test

example 1

Subcutaneous Immunisation

[0232]The integrity of the conformational structure and immunogenicity of the J14 and J14 anchor candidates were determined.

[0233]Peptides, with or without anchors, as described in table 3.2, were emulsified in Complete Freund's adjuvant CFA and administered subcutaneously at the tail base of B10.BR inbred mice. After the primary immunisation, boosts of 30 μg antigen in PBS were given on days 21 and 28. Sera were collected 1 day prior to boosts and 15 days after.

example 1a

Immunogenicity of the Peptide / Proteosomes Delivered Subcutaneously

[0234]Antibody titres, specific for the J14 peptide, are shown in FIG. 4. The antibody titres, after a primary immunisation in CFA and two boosts in PBS (groups 1-3), indicate that the J14 peptide with the addition of either the amino terminal (group 2) or carboxyl terminal (group 3) anchors, have resulted in sera that is able to recognise the standard chimeric J14 peptide. This infers that the addition of either the amino terminal or carboxyl terminal anchor did not disrupt the conformational structure of the J14 chimeric peptide.

TABLE 1Murine Groups for Example 1.GroupImmunisationNumberNumberImmunogenRouteof Mice1J14 (CFA)S / C52J14 amino terminal anchor (CFA)S / C53J14 carboxyl terminal anchor (CFA)S / C54PBS (CFA)S / C55J14 amino terminal anchor / S / C5proteosome adjuvant (ratio A)6J14 carboxyl terminal anchor / S / C5proteosome adjuvant (ratio A)7Proteosome adjuvant onlyS / C

[0235]The subcutaneous immunisation of the peptide-prot...

example 1b

Opsonic Potential of Sera from Immunised Mice

[0237]Sera were tested for their ability to opsonise or kill the M1 GAS reference strain (FIG. 5). All of the mice in groups one and three opsonised the GAS strain, with killing ranging from 18 to 43% and 22 to 62%, respectively. For group two only 3 of 5 mice opsonised the M1 GAS.

[0238]Both of the J14 / proteosome adjuvant immunised groups (five and six) opsonised the GAS strain. However, the opsonic potential of the individual mice varied with only 2 out of 4 mice from group five (mouse number 4 died before the opsonisation assay) and 3 out of 5 mice opsonising the bacteria from group six. Both of the control groups (four and seven) did not kill the bacteria in the in vitro assay.

Discussion and Conclusions

[0239]The experiment showed that sera raised to the peptides containing the anchors were able to recognise the standard J14 chimeric peptide and therefore the anchors did not appear to disrupt the conformational structure of the peptide....

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

Effective stimulation of immune responses is achieved through the use of a group A streptococcal antigen combined with proteosome adjuvant. The compositions are provided in particular for intranasal administration. The vaccine compositions are provided for use in inducing an immune response in an individual for the treatment or prophylaxis of group A streptococcal infection in an individual, preferably via prevention or reduction of colonisation of the throat following intranasal administration.

Description

CROSS-REFERENCES TO RELATED APPLICATIONS[0001]This application is a continuation of U.S. application Ser. No. 10 / 706,275 filed Nov. 13, 2003, now allowed, which claims the benefit of U.S. Provisional Application No. 60 / 426,409, filed Nov. 15, 2002 and Australian Application No. 2002302132, filed Nov. 15, 2002, all of which are herein incorporated by reference in their entireties.STATEMENT REGARDING SEQUENCE LISTING[0002]The Sequence Listing associated with this application is provided in text format in lieu of a paper copy, and is hereby incorporated by reference into the specification. The name of the text file containing the Sequence Listing is 484112—413Cl_SEQUENCE_LISTING.txt. The text file is 7 KB, was created on Jul. 24, 2007, and is being submitted electronically via EFS-Web, concurrent with the filing of the specification.FIELD OF INVENTION[0003]The invention relates to vaccines, and in particular to vaccines useful in treatment or prophylaxis of Streptococcus pyogenes infec...

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(United States)
IPC IPC(8): A61K39/09A61K39/02
CPCA61K39/092A61K2039/6068A61K2039/55555A61K2039/55516
Inventor LOWELL, GEORGE H.WHITE, GEORGE L.BATZLOFF, MICHAEL RAYMONDBURT, DAVID S.LEANDERSON, TOMAS B.GOOD, MICHAEL F.
Owner ID BIOMEDICAL CORP LAVAL
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