EP0964699A1 - SEQUENCES NUCLEOTIDIQUES ET AMINOACIDES EN RAPPORT AVEC $i(HELICOBACTER PYLORI) ET COMPOSITIONS VACCINALES CORRESPONDANTES - Google Patents

SEQUENCES NUCLEOTIDIQUES ET AMINOACIDES EN RAPPORT AVEC $i(HELICOBACTER PYLORI) ET COMPOSITIONS VACCINALES CORRESPONDANTES

Info

Publication number
EP0964699A1
EP0964699A1 EP97954525A EP97954525A EP0964699A1 EP 0964699 A1 EP0964699 A1 EP 0964699A1 EP 97954525 A EP97954525 A EP 97954525A EP 97954525 A EP97954525 A EP 97954525A EP 0964699 A1 EP0964699 A1 EP 0964699A1
Authority
EP
European Patent Office
Prior art keywords
seq
pylori
polypeptide
nucleic acid
fragment
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP97954525A
Other languages
German (de)
English (en)
Other versions
EP0964699A4 (fr
Inventor
Douglas Smith
Richard A. Alm
Peter C. Doig
Zita Kabok
Lillian Marie Castriotta
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
AstraZeneca AB
Original Assignee
Astra AB
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Astra AB filed Critical Astra AB
Publication of EP0964699A1 publication Critical patent/EP0964699A1/fr
Publication of EP0964699A4 publication Critical patent/EP0964699A4/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/205—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Campylobacter (G)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/04—Antibacterial agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K39/02—Bacterial antigens
    • A61K2039/106—Vibrio; Campylobacter; Not used, see subgroups
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide

Definitions

  • the invention features a substantially pure nucleic acid encoding an H. pylori polypeptide having an amino acid sequence of SEQ ID NO: 99, such as a nucleic acid comprising a nucleotide sequence of SEQ ID NO: 2.
  • the invention features a substantially pure nucleic acid encoding an H. pylori polypeptide having an amino acid sequence of SEQ ID NO: 102, such as a nucleic acid comprising a nucleotide sequence of SEQ ID NO: 5.
  • the invention features a substantially pure nucleic acid encoding an H. pylori polypeptide having an amino acid sequence of SEQ ID NO: 193, such as a nucleic acid comprising a nucleotide sequence of SEQ ID NO: 96.
  • the H. pylori cell envelope polypeptide or a fragment thereof is an H. pylori flagella-associated polypeptide or a fragment thereof encoded by a nucleic acid having a nucleotide sequence of SEQ ID NO: 63, or a complement thereof.
  • the H pylori cell envelope polypeptide or a fragment thereof is an H. pylori outer membrane polypeptide or a fragment thereof encoded by a nucleic acid selected from the group consisting of SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 61, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 84, SEQ ID NO: 85, SEQ ID NO: 91, SEQ ID NO: 94, SEQ ID NO: 5, SEQ ID NO: 1 1, SEQ ID NO: 26, SEQ ID NO: 36, SEQ ID NO: 42, SEQ ID NO: 52, SEQ ID NO: 22, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 65, and SEQ ID NO: 66.
  • the H. pylori cytoplasmic polypeptide or a fragment thereof is an H. pylori polypeptide or a fragment thereof involved in mRNA translation, wherein the polypeptide is encoded by a nucleic acid selected from the group consisting of SEQ ID NO: 57, and SEQ ID NO: 58.
  • the H. pylori cytoplasmic polypeptide or a fragment thereof is an H. pylori polypeptide or a fragment thereof involved in genome replication, transcription, recombination and repair, wherein the polypeptide is encoded by a nucleic acid selected from the group consisting of SEQ ID NO: 86 and SEQ ID NO: 87.
  • the invention pertains to any individual H. pylori polypeptide member or nucleic acid encoding such a member from the above-identified groups of H. pylori polypeptides.
  • the invention features nucleic acids capable of binding mRNA of H. pylori. Such nucleic acid is capable of acting as antisense nucleic acid to control the translation of mRNA of H. pylori.
  • a further aspect features a nucleic acid which is capable of binding specifically to an H. pylori nucleic acid. These nucleic acids are also referred to herein as complements and have utility as probes and as capture reagents.
  • H pylori polypeptides characterized as shown in Table 1 below, including: H pylori cell envelope proteins, H pylori secreted proteins, H pylori cytoplasmic proteins and H pylori cellular proteins.
  • H pylori cell envelope proteins H pylori secreted proteins
  • H pylori cytoplasmic proteins H pylori cellular proteins.
  • purified polypeptide and “isolated polypeptide” and “a substantially pure preparation of a polypeptide” are used interchangeably herein and, as used herein, mean a polypeptide that has been substantially, and preferably completely, separated from other proteins, lipids, and nucleic acids with which it naturally occurs.
  • the polypeptide is also separated from substances, e.g., antibodies or gel matrix, e.g., polyacrylamide, which are used to purify it.
  • the polypeptide constitutes at least 10, 20, 50 70, 80 or 95% dry weight of the purified preparation.
  • an "isolated” or “purified” protein or biologically active portion thereof is substantially free of cellular material or other contaminating proteins from the cell or tissue source from which the H. pylori protein is derived, or substantially free from chemical precursors or other chemicals when chemically synthesized.
  • the language “substantially free of cellular material” includes preparations of H. pylori protein in which the protein is separated from cellular components of the cells from which it is isolated or recombinantly produced. In one embodiment, the language
  • transgenic cell refers to a cell containing a transgene.
  • a transgenic animal is any animal in which one or more, and preferably essentially all, of the cells of the animal includes a transgene.
  • the transgene can be introduced into the cell, directly or indirectly by introduction into a precursor of the cell, by way of deliberate genetic manipulation, such as by a process of transformation of competent cells or by microinjection or by infection with a recombinant virus. This molecule may be integrated within a chromosome, or it may be extrachromosomallv replicating DNA.
  • This invention provides nucleotide sequences of the genome of H. pylori which thus comprises a DNA sequence library of H. pylori genomic DNA.
  • the detailed description that follows provides nucleotide sequences of H. pylori, and also describes how the sequences were obtained and how ORFs and protein-coding sequences were identified. Also described are methods of using the disclosed H. pylori sec uences in methods including diagnostic and therapeutic applications.
  • the library can be used as a database for identification and comparison of medically important sequences in this and other strains of H. pylori.
  • Clones carrying the desired sequences described in this invention may also be obtained by screening the libraries by means of the PCR or by hybridization of synthetic oligonucleotide probes to filter lifts of the library colonies or plaques as known in the art (see, e.g., Sambrook et al., Molecular Cloning, A Laboratory Manual 2nd edition, 1989, Cold Spring Harbor Press, NY).
  • This invention encompasses isolated H pylori polypeptides encoded by the disclosed H pylori genomic sequences, including the polypeptides of the invention contained in the Sequence Listing. Polypeptides of the invention are preferably at least 5 amino acid residues in length. Using the DNA sequence information provided herein, the amino acid sequences of the polypeptides encompassed by the invention can be deduced using methods well-known in the art. It will be understood that the sequence of an entire nucleic acid encoding an H. pylori polypeptide can be isolated and identified based on an ORF that encodes only a fragment of the cognate protein-coding region.
  • Amino acid sequence variants of a protein can be prepared by random mutagenesis of DNA which encodes a protein or a particular domain or region of a protein. Useful methods include PCR mutagenesis and saturation mutagenesis. A library of random amino acid sequence variants can also be generated by the synthesis of a set of degenerate oligonucleotide sequences. (Methods for screening proteins in a library of variants are elsewhere herein).
  • a second difference is the set of biological biases affecting the population of peptides actually present in the libraries.
  • the La fusion molecules are confined to the cytoplasm of the host cells.
  • the phage coat fusions are exposed briefly to the cytoplasm during translation but are rapidly secreted through the inner membrane into the periplasmic compartment, remaining anchored in the membrane by their C-terminal hydrophobic domains, with the N-termini, containing the peptides, protruding into the periplasm while awaiting assembly into phage particles.
  • the peptides in the Lad and phage libraries may differ significantly as a result of their exposure to different proteolytic activities.
  • a common assay for T cell proliferation entails measuring tritiated thymidine incorporation.
  • the proliferation of T cells can be measured in vitro by determining the amount of ⁇ H-labeled thymidine incorporated into the replicating DNA of cultured cells. Therefore, the rate of DNA synthesis and, in turn, the rate of cell division can be quantified.
  • DNA inserts were cloned (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994) into the previously digested pET-28b expression vector, except for the amplified insert for ppiB, which was cloned into the pET-28a expression vector. Products of the ligation reaction were then used to transform the BL21 strain of E. coli (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et ?1., d ⁇ s., 1994) as described below.
  • Fractions containing the recombinant protein were identified by absorbance at 280 nm and analyzed by SDS-PAGE. Fractions were pooled and concentrated by centrifugal filtration.
  • This combination of primers would enable each ORF of interest to be cloned into p ⁇ T28b (to produce a ⁇ is-tagged recombinant protein) or pET30a (to produce a non ⁇ is-tagged or native recombinant protein).
  • the pET28b vector provides sequence encoding an additional 20 amino- terminal amino acids (plus the methionine in the Ndel restriction site) including a stretch of six histidine residues which makes up the ⁇ is-tag.
  • Transformants were collected from LB agar plates containing 25ug/ml kanamycin sulfate (ensures maintenance of the pET28b-based recombinant plasmids) and used to inoculate LB broth containing 25ug/ml kanamycin sulfate and grown to an optical density at 600nm of 0.5 to 1.0 OD units, at which point ImM IPTG was added to the culture for one to three hours to induce gene expression of the H. pylori recombinant DNA constructions.
  • Oral immunization with vac36 antigen interfered with the establishment ofH. pylori infection upon challenge with live H. pylori organisms. Mice immunized with purified recombinant vac36 antigen exhibited a significantly lower level of colonization by H pylori, as assessed by gastric urease activity and bacterial count assays (Table 6). Oral immunization with vac36 antigen also resulted in the generation of a local protective gastric immune response. Greater numbers of CD4 + T cells and of IgACC were recruited in the gastric tissues of vac36-immunized mice when compared with unimmunized H. #y/orz ' -infected mice (Table 7).
  • the ligation products are transformed into XL-1 Blue or DH5-a E.coli cells by electroporation as described previously. After recovery in SOC, cells are plated onto LB plates containing 100 microgram/ml Ampicillin and grown overnight at 37°C. These plates are then replica plated onto plates containing 25 microgram/ml Kanamycin and allowed to grow overnight. Resultant colonies have both the Ampicillin resistance gene present in the pT7Blue vector, .a d the newly introduced Kanamycin resistance gene. Colonies are picked into LB containing 25 microgram/ml Kanamycin and plasmid DNA is isolated from the cultured cells using the Qiagen miniprep protocol (Qiagen, Gaithersburg, MD, USA).
  • TEST 1 PCR with cloning primers originally used to amplify the gene/ORF.
  • a positive result of homologous recombination at the correct chromosomal location should show a single PCR product whose size is expected to be the size of the deleted gene/ORF but increased in size by the addition of a 1.4 kilobase Kanamycin cassette.
  • a PCR product of just the size of the gene/ORF is proof that the gene had not been knocked out and that the transformant is not the result of homologous recombination at the correct chromosome location.
  • DNA was subjected to electrophoresis on 1.0% agarose gels. The DNA was visualized by exposure to ethidium bromide and long wave UV irradiation, and cut out in gel slices. DNA was purified using the Wizard PCR Preps kit (Promega Corp., Madison WI, USA), and then subjected to digestion with BamHl and EcoRI (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). The digested PCR amplicon was then re-electrophoresed and purified as before.

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  • Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Communicable Diseases (AREA)
  • General Chemical & Material Sciences (AREA)
  • Biophysics (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biochemistry (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Oncology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Genetics & Genomics (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Animal Behavior & Ethology (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Peptides Or Proteins (AREA)
  • Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

L'invention a trait à des préparations de recombinaison ou sensiblement pures de polypeptides d'H. pylori. Elle porte également sur les acides nucléiques codant ces polypeptides. Les polypeptides d'H. pylori se révèlent utiles en matière de compositions diagnostiques et vaccinales. La Figure représente un alignement de séquence aminoacide de cinq protéines d'Helicobacter pylori.
EP97954525A 1996-12-05 1997-12-05 Sequences nucleotidiques et aminoacides en rapport avec helicobacter pylori et compositions vaccinales correspondantes Withdrawn EP0964699A4 (fr)

Applications Claiming Priority (7)

Application Number Priority Date Filing Date Title
US75962596A 1996-12-05 1996-12-05
US759625 1996-12-05
US82374597A 1997-03-25 1997-03-25
US823745 1997-03-25
US89192897A 1997-07-14 1997-07-14
US891928 1997-07-14
PCT/US1997/022104 WO1998024475A1 (fr) 1996-12-05 1997-12-05 Sequences nucleotidiques et aminoacides en rapport avec helicobacter pylori et compositions vaccinales correspondantes

Publications (2)

Publication Number Publication Date
EP0964699A1 true EP0964699A1 (fr) 1999-12-22
EP0964699A4 EP0964699A4 (fr) 2005-04-06

Family

ID=27419527

Family Applications (1)

Application Number Title Priority Date Filing Date
EP97954525A Withdrawn EP0964699A4 (fr) 1996-12-05 1997-12-05 Sequences nucleotidiques et aminoacides en rapport avec helicobacter pylori et compositions vaccinales correspondantes

Country Status (18)

Country Link
EP (1) EP0964699A4 (fr)
JP (1) JP2001510992A (fr)
KR (1) KR20000069297A (fr)
CN (1) CN1246799A (fr)
AR (1) AR010337A1 (fr)
AU (1) AU739641B2 (fr)
BR (1) BR9714133A (fr)
CA (1) CA2273199A1 (fr)
EE (1) EE9900226A (fr)
ID (1) ID21946A (fr)
IL (1) IL129746A0 (fr)
IS (1) IS5047A (fr)
NO (1) NO992158L (fr)
NZ (1) NZ335633A (fr)
PL (1) PL333943A1 (fr)
SK (1) SK57999A3 (fr)
TR (1) TR199901262T2 (fr)
WO (1) WO1998024475A1 (fr)

Families Citing this family (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
ATE332968T1 (de) * 1998-10-26 2006-08-15 Novozymes As Erstellung und durchmusterung von interessierenden dna-banken in zellen von filamentösen pilzen
US7034132B2 (en) 2001-06-04 2006-04-25 Anderson David W Therapeutic polypeptides, nucleic acids encoding same, and methods of use
AUPQ347199A0 (en) * 1999-10-15 1999-11-11 Csl Limited Novel polypeptide fragments
US6951729B1 (en) 1999-10-27 2005-10-04 Affinium Pharmaceuticals, Inc. High throughput screening method for biological agents affecting fatty acid biosynthesis
US7048926B2 (en) 2000-10-06 2006-05-23 Affinium Pharmaceuticals, Inc. Methods of agonizing and antagonizing FabK
WO2002031128A1 (fr) * 2000-10-06 2002-04-18 Smithkline Beecham Corporation Procedes d'utilisation d'agonistes et d'antagonistesdes polypeptides fabk
WO2002066502A1 (fr) * 2001-02-21 2002-08-29 Boren Thomas Adhesine de liaison de l'acide sialique d'helicobacter pylori, saba et gene de saba
JP2012505197A (ja) * 2008-10-08 2012-03-01 イミューン・ソリューションズ・リミテッド 粘膜免疫を生成するための経口ワクチン
US10828358B2 (en) 2015-12-14 2020-11-10 Technische Universität München Helicobacter pylori vaccines
CN110343697B (zh) * 2019-08-05 2024-07-12 南京昊斯亭网络科技有限公司 一种植物病害菌总dna提取方法
CN113435168B (zh) * 2021-06-10 2024-03-22 上海美吉生物医药科技有限公司 胶图自动编辑方法、系统、终端及介质
CN114057854B (zh) * 2021-09-30 2022-07-15 河北医科大学第四医院 一种幽门螺杆菌cd4+t细胞耐受多肽融合抗原及其应用

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994016714A1 (fr) * 1993-01-19 1994-08-04 Medicarb Ab COMPOSITION UTILISEE DANS LE TRAITEMENT D'INFECTIONS CAUSEES PAR $i(HELICOBACTER PYLORI)

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994016714A1 (fr) * 1993-01-19 1994-08-04 Medicarb Ab COMPOSITION UTILISEE DANS LE TRAITEMENT D'INFECTIONS CAUSEES PAR $i(HELICOBACTER PYLORI)

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
JEAN-F. TOMB ET AL.: "The complete genome sequence of the gastric pathogen Helicobacter pylori" NATURE, vol. 389, 25 September 1997 (1997-09-25), pages 539-547, XP002062106 & DATABASE UniProt Entry O224870 1 January 1998 (1998-01-01), TOMB, J.-F. ET AL.: "Outer membrane protein (Omp2)" Database accession no. O224870 & DATABASE EMBL Entry AE000525 25 August 1997 (1997-08-25), TOMB, J.-F. ET AL.: "Helicobacter pylori section 3 of 134 of the complete genome" Database accession no. AE000525 *
SCHMITT W ET AL: "GENETIC ANALYSIS OF THE HELICOBACTER PYLORI VACUOLATING CYTOTOXIN: STRUCTURAL SIMILARITIES WITH THE IGA PROTEASE TYPE OF EXPORTED PROTEIN" MOLECULAR MICROBIOLOGY, BLACKWELL SCIENTIFIC, OXFORD, GB, vol. 12, no. 2, 1 April 1994 (1994-04-01), pages 307-319, XP000605827 ISSN: 0950-382X *
See also references of WO9824475A1 *

Also Published As

Publication number Publication date
EP0964699A4 (fr) 2005-04-06
KR20000069297A (ko) 2000-11-25
IL129746A0 (en) 2000-02-29
NZ335633A (en) 2000-10-27
EE9900226A (et) 1999-12-15
TR199901262T2 (xx) 1999-08-23
NO992158L (no) 1999-07-05
AU5895498A (en) 1998-06-29
PL333943A1 (en) 2000-01-31
IS5047A (is) 1999-05-10
WO1998024475A1 (fr) 1998-06-11
CA2273199A1 (fr) 1998-06-11
AR010337A1 (es) 2000-06-07
AU739641B2 (en) 2001-10-18
ID21946A (id) 1999-08-12
JP2001510992A (ja) 2001-08-07
BR9714133A (pt) 2000-02-29
SK57999A3 (en) 2000-05-16
NO992158D0 (no) 1999-05-04
CN1246799A (zh) 2000-03-08

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