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Moraxella (branhamella) catarrhalis antigens

a technology of moraxella and bacterial catarrhalis, which is applied in the field of polypeptides, can solve the problems of many of these surface proteins that are still not characterized

Inactive Publication Date: 2009-03-19
ID BIOMEDICAL
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, many of these surface proteins are still not characterized, nor has the immune response resulting in protection from infection by different strains been determined.

Method used

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  • Moraxella (branhamella) catarrhalis antigens
  • Moraxella (branhamella) catarrhalis antigens
  • Moraxella (branhamella) catarrhalis antigens

Examples

Experimental program
Comparison scheme
Effect test

example 1

[0197]This example illustrates the cloning and molecular characteristics of BVH-MC2 gene and corresponding polypeptide.

[0198]The coding region of M. catarrhalis BVH-MC2 (SEQ ID NO: 1) gene was amplified by PCR (DNA Thermal Cycler GeneAmp® PCR system 2400 Perkin Elmer, San Jose, Calif.) from genomic DNA of M. catarrhalis strain ETSU C-2 using the following oligos that contained base extensions for the addition of restriction sites NdeI (CATATG) and XhoI (CTCGAG): DMAR544 (5′-CATCAGTGCATATGAATACGACACACCATCACACG-3′) (SEQ ID NO:15); DMAR545 (5′-GAGTTATTCTCGAGTTTGTCCAAATTTGGCTTAGTTTTAC-3′) (SEQ ID NO: 15). PCR products were purified from agarose gel using a QIA® quick gel extraction kit from QIA®gen following the manufacturer's instructions (Chatsworth, Calif.), and digested with NdeI and XhoI (AMERSHAM Pharmacia Biotech, Inc, Baie d'Urfë, Canada). The pET21b(+) vector (NOVAGEN, Madison, Wis.) was digested with NdeI and XhoI and purified from agarose gel using a QIA® quick gel extraction...

example 2

[0202]This example illustrates the cloning and molecular characteristics of BVH-MC3 gene and corresponding polypeptide.

[0203]The coding region of M. catarrhalis BVH-MC3 (SEQ ID NO: 9) gene was amplified by PCR (DNA Thermal Cycler GeneAmp® PCR system 2400 Perkin Elmer, San Jose, Calif.) from genomic DNA of M. catarrhalis strain ETSU C-2 using the following oligos that contained base extensions for the addition of restriction sites NdeI (CATATG) and XhoI (CTCGAG): DMAR592 and DMAR593, which are presented in Table 1. The methods used for cloning BVH-MC3 into an expression vector and sequencing are similar to the methods described in Example 1.

[0204]It was determined that the open reading frame (ORF) which codes for BVH-MC3 contains 1656-bp and encodes a 551 amino acid residues polypeptide with a predicted pI of 4.68 and a predicted molecular mass of 58910.13 Da. Analysis of the predicted amino acid residues sequence (SEQ ID NO: 10) using the Spscan software (Wisconsin Sequence Analysis...

example 3

[0206]This example illustrates the cloning and molecular characteristics of BVH-MC4 gene and corresponding polypeptide.

[0207]The coding region of M. catarrhalis BVH-MC4 (SEQ ID NO: 11) gene was amplified by PCR (DNA Thermal Cycler GeneAmp PCR system 2400 Perkin Elmer, San Jose, Calif.) from genomic DNA of M. catarrhalis strain ETSU C-2 using the following oligos that contained base extensions for the addition of restriction sites NdeI (CATATG) and XhoI (CTCGAG): RIOS71 and RIOS72, which are presented in Table 1. The methods used for cloning BVH-MC4 into an expression vector and sequencing are similar to the methods described in Example 1.

[0208]It was determined that the open reading frame (ORF) which codes for BVH-MC4 contains 1251-bp and encodes a 416 amino acid residues polypeptide with a predicted pI of 4.84 and a predicted molecular mass of 46125.11 Da. Analysis of the predicted amino acid residues sequence (SEQ ID NO: 12) using the Spscan software (Wisconsin Sequence Analysis P...

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Abstract

The present invention relates to polypeptides of Moraxella (Branhamella) catarrhalis which may be useful for prophylaxis, diagnostic and / or therapy purposes.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS[0001]This application is a continuation of U.S. patent application Ser. No. 10 / 477,592, now allowed, which has a filing date of Jun. 2, 2004, and which is a national stage application filed under 35 U.S.C. § 371 of International Patent Application PCT / CA02 / 00706, accorded an international filing date of May 15, 2002, which claims the benefit U.S. Provisional Application No. 60 / 290,653, filed May 15, 2001, all of which applications are incorporated herein 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—425C1_SEQUENCE_LISTING.txt. The text file is 46 KB, was created on Jul. 15, 2008, and is being submitted electronically via EFS-Web.FIELD OF THE INVENTION[0003]The present invention is ...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A61K39/02A61P31/04G01N33/53A61K39/00A61P11/00A61P11/02A61P27/02A61P27/16C07K14/195C07K14/21C07K19/00C12N1/15C12N1/19C12N1/21C12N5/10C12N15/09C12N15/31C12P21/02G01N33/569
CPCA61K39/00C07K2319/00C07K14/212A61P11/00A61P11/02A61P11/04A61P11/14A61P27/02A61P27/16A61P31/04A61P37/04
Inventor MARTIN, DENISHAMEL, JOSEEBRODEUR, BERNARD R.RIOUX, STEPHANECOUTURE, JULIE
Owner ID BIOMEDICAL
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