IL76338A - פוליפפטידים אימונוגניים של פלסמודיום פלסיפרום, מולקולות של andהמקדדים אותם, שיטה להכנת הפוליפפטידים ותכשירים המכילים את הפוליפפטיד - Google Patents
פוליפפטידים אימונוגניים של פלסמודיום פלסיפרום, מולקולות של andהמקדדים אותם, שיטה להכנת הפוליפפטידים ותכשירים המכילים את הפוליפפטידInfo
- Publication number
- IL76338A IL76338A IL7633885A IL7633885A IL76338A IL 76338 A IL76338 A IL 76338A IL 7633885 A IL7633885 A IL 7633885A IL 7633885 A IL7633885 A IL 7633885A IL 76338 A IL76338 A IL 76338A
- Authority
- IL
- Israel
- Prior art keywords
- polypeptide
- amino acid
- immunogenic
- recombinant dna
- acid sequence
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 145
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 135
- 229920001184 polypeptide Polymers 0.000 title claims description 123
- 241000223960 Plasmodium falciparum Species 0.000 title claims description 47
- 230000002163 immunogen Effects 0.000 title claims description 44
- 239000000203 mixture Substances 0.000 title claims description 10
- 239000000427 antigen Substances 0.000 claims description 42
- 108091007433 antigens Proteins 0.000 claims description 42
- 102000036639 antigens Human genes 0.000 claims description 42
- 108020004511 Recombinant DNA Proteins 0.000 claims description 30
- 239000002773 nucleotide Substances 0.000 claims description 30
- 125000003729 nucleotide group Chemical group 0.000 claims description 30
- 102000053602 DNA Human genes 0.000 claims description 23
- 150000001413 amino acids Chemical class 0.000 claims description 22
- 238000000034 method Methods 0.000 claims description 22
- 108020004414 DNA Proteins 0.000 claims description 18
- 239000013598 vector Substances 0.000 claims description 18
- 210000004027 cell Anatomy 0.000 claims description 16
- 239000003981 vehicle Substances 0.000 claims description 16
- 206010035500 Plasmodium falciparum infection Diseases 0.000 claims description 13
- 238000010367 cloning Methods 0.000 claims description 11
- 210000004369 blood Anatomy 0.000 claims description 10
- 239000008280 blood Substances 0.000 claims description 10
- 230000004936 stimulating effect Effects 0.000 claims description 4
- 241000124008 Mammalia Species 0.000 claims description 3
- 239000002671 adjuvant Substances 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 230000028993 immune response Effects 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 20
- 241000700605 Viruses Species 0.000 claims 3
- 244000005700 microbiome Species 0.000 claims 3
- 241001515965 unidentified phage Species 0.000 claims 3
- 210000004899 c-terminal region Anatomy 0.000 claims 2
- 239000013599 cloning vector Substances 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 101710179519 Ring-infected erythrocyte surface antigen Proteins 0.000 description 89
- 239000002299 complementary DNA Substances 0.000 description 22
- 241000282414 Homo sapiens Species 0.000 description 20
- 210000003743 erythrocyte Anatomy 0.000 description 20
- 239000012634 fragment Substances 0.000 description 19
- 108090000623 proteins and genes Proteins 0.000 description 18
- 210000003936 merozoite Anatomy 0.000 description 17
- 244000045947 parasite Species 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 241000283973 Oryctolagus cuniculus Species 0.000 description 9
- 238000001262 western blot Methods 0.000 description 8
- 239000002250 absorbent Substances 0.000 description 6
- 230000002745 absorbent Effects 0.000 description 6
- 230000002759 chromosomal effect Effects 0.000 description 6
- 239000010931 gold Substances 0.000 description 6
- 229910052737 gold Inorganic materials 0.000 description 6
- 238000002372 labelling Methods 0.000 description 6
- 230000003252 repetitive effect Effects 0.000 description 6
- 108700028369 Alleles Proteins 0.000 description 5
- 101150036166 FIRA gene Proteins 0.000 description 5
- 239000013504 Triton X-100 Substances 0.000 description 5
- 229920004890 Triton X-100 Polymers 0.000 description 5
- 230000000890 antigenic effect Effects 0.000 description 5
- 238000009396 hybridization Methods 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 108020004999 messenger RNA Proteins 0.000 description 5
- 210000001563 schizont Anatomy 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- 229920002684 Sepharose Polymers 0.000 description 4
- 229940098773 bovine serum albumin Drugs 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 238000003018 immunoassay Methods 0.000 description 4
- 201000004792 malaria Diseases 0.000 description 4
- 239000008363 phosphate buffer Substances 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 239000012723 sample buffer Substances 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 210000003812 trophozoite Anatomy 0.000 description 4
- 108700024394 Exon Proteins 0.000 description 3
- 108091092195 Intron Proteins 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 101710137302 Surface antigen S Proteins 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 230000037029 cross reaction Effects 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 210000003617 erythrocyte membrane Anatomy 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000036039 immunity Effects 0.000 description 3
- 238000010166 immunofluorescence Methods 0.000 description 3
- 230000005847 immunogenicity Effects 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000010532 solid phase synthesis reaction Methods 0.000 description 3
- 108090000317 Chymotrypsin Proteins 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- HNQBPUIXFDQDRJ-UHFFFAOYSA-N N-ethyl-N-(2-hydroxyethyl)nitrosamine Chemical compound CCN(N=O)CCO HNQBPUIXFDQDRJ-UHFFFAOYSA-N 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 108010065081 Phosphorylase b Proteins 0.000 description 2
- 241000224016 Plasmodium Species 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 2
- 238000002105 Southern blotting Methods 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000002788 anti-peptide Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 229960002376 chymotrypsin Drugs 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 101150089906 resA gene Proteins 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- WHTVZRBIWZFKQO-AWEZNQCLSA-N (S)-chloroquine Chemical compound ClC1=CC=C2C(N[C@@H](C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-AWEZNQCLSA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- WFIYPADYPQQLNN-UHFFFAOYSA-N 2-[2-(4-bromopyrazol-1-yl)ethyl]isoindole-1,3-dione Chemical compound C1=C(Br)C=NN1CCN1C(=O)C2=CC=CC=C2C1=O WFIYPADYPQQLNN-UHFFFAOYSA-N 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 102000003505 Myosin Human genes 0.000 description 1
- 108060008487 Myosin Proteins 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 208000009182 Parasitemia Diseases 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- COQLPRJCUIATTQ-UHFFFAOYSA-N Uranyl acetate Chemical compound O.O.O=[U]=O.CC(O)=O.CC(O)=O COQLPRJCUIATTQ-UHFFFAOYSA-N 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000003491 array Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 238000010370 cell cloning Methods 0.000 description 1
- 229960003677 chloroquine Drugs 0.000 description 1
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Natural products ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 230000017188 evasion or tolerance of host immune response Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 235000013861 fat-free Nutrition 0.000 description 1
- 230000008004 immune attack Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229940031348 multivalent vaccine Drugs 0.000 description 1
- 210000003463 organelle Anatomy 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000011896 sensitive detection Methods 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- 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
- A61K39/002—Protozoa antigens
- A61K39/015—Hemosporidia antigens, e.g. Plasmodium antigens
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/44—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from protozoa
- C07K14/445—Plasmodium
-
- 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
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Tropical Medicine & Parasitology (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Gastroenterology & Hepatology (AREA)
- Mycology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Epidemiology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AUPG706684 | 1984-09-11 | ||
| AUPG706784 | 1984-09-11 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| IL76338A true IL76338A (he) | 1994-08-26 |
Family
ID=25642846
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL7633885A IL76338A (he) | 1984-09-11 | 1985-09-09 | פוליפפטידים אימונוגניים של פלסמודיום פלסיפרום, מולקולות של andהמקדדים אותם, שיטה להכנת הפוליפפטידים ותכשירים המכילים את הפוליפפטיד |
Country Status (13)
| Country | Link |
|---|---|
| EP (1) | EP0193586B1 (he) |
| JP (1) | JPH0698773A (he) |
| AU (1) | AU599305B2 (he) |
| CA (1) | CA1340213C (he) |
| DE (1) | DE3587503T2 (he) |
| GB (1) | GB2176191B (he) |
| HK (1) | HK132693A (he) |
| IL (1) | IL76338A (he) |
| MY (1) | MY102593A (he) |
| OA (1) | OA08325A (he) |
| SG (2) | SG65089G (he) |
| WO (1) | WO1986001802A1 (he) |
| ZW (1) | ZW14985A1 (he) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3584300D1 (de) * | 1984-02-21 | 1991-11-14 | Nat Res Dev | Herstellung von malaria-impfstoffen. |
| IL81026A0 (en) * | 1985-12-24 | 1987-03-31 | Inst Medical W & E Hall | Peptides for immunizing against plasmodium falciparum,dna molecules coding for them and compositions containing said peptides |
| AU606042B2 (en) * | 1985-12-24 | 1991-01-31 | Saramane Pty Ltd | Asexual blood stage antigens of plasmodium falciparum |
| KR880701243A (ko) * | 1986-03-14 | 1988-07-26 | 원본미기재 | 말라리아에 대한 보호 면역을 제공하는 폴리펩티드 |
| US5006514A (en) * | 1986-03-20 | 1991-04-09 | Sawai Pharmaceutical Co., Ltd. | α,α-trehalose trimycolates and pharmaceutical compositions |
| IT1213576B (it) * | 1986-12-23 | 1989-12-20 | Eniricerche Spa | Composizione polipeptidica utile per la preparazione di vaccini antimalaria e di kits diagnostici per la determinazione di anticorpi antimerozoite. |
| FR2672290B1 (fr) | 1991-02-05 | 1995-04-21 | Pasteur Institut | Sequences peptidiques specifiques des stades hepatiques de p. falciparum porteuses d'epitopes capables de stimuler les lymphocytes t. |
| US5532133A (en) * | 1993-06-02 | 1996-07-02 | New York University | Plasmodium vivax blood stage antigens, PvESP-1, antibodies, and diagnostic assays |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU569722B2 (en) * | 1983-01-28 | 1988-02-18 | Saramane Pty Ltd | Expression of plasmodium falciparum polypeptides from cloned cdna |
| GB8404378D0 (en) * | 1984-02-20 | 1984-03-28 | Biogen Nv | Dna sequence recombinant dna molecules |
| PH25993A (en) * | 1984-02-22 | 1992-01-13 | Wellcome Found | Cloning of DNA for protozoal antigens |
| WO1986004922A1 (en) * | 1985-02-20 | 1986-08-28 | Memorial Sloan-Kettering Cancer Center | cDNA CODING FOR PLASMODIUM FALCIPARUM GLYCOPHORIN BINDING PROTEINS WEIGHING 130,000 DALTONS AND 155,000 DALTONS |
-
1985
- 1985-09-09 IL IL7633885A patent/IL76338A/he not_active IP Right Cessation
- 1985-09-10 DE DE85904583T patent/DE3587503T2/de not_active Expired - Fee Related
- 1985-09-10 EP EP85904583A patent/EP0193586B1/en not_active Expired - Lifetime
- 1985-09-10 GB GB8610243A patent/GB2176191B/en not_active Expired
- 1985-09-10 AU AU47326/85A patent/AU599305B2/en not_active Ceased
- 1985-09-10 WO PCT/AU1985/000223 patent/WO1986001802A1/en not_active Ceased
- 1985-09-11 CA CA000490460A patent/CA1340213C/en not_active Expired - Fee Related
- 1985-09-11 ZW ZW149/85A patent/ZW14985A1/xx unknown
-
1986
- 1986-05-07 OA OA58856A patent/OA08325A/xx unknown
-
1987
- 1987-09-11 MY MYPI87001633A patent/MY102593A/en unknown
-
1989
- 1989-09-20 SG SG65089A patent/SG65089G/en unknown
-
1993
- 1993-06-22 JP JP5150375A patent/JPH0698773A/ja active Pending
- 1993-10-29 SG SG119293A patent/SG119293G/en unknown
- 1993-12-02 HK HK1326/93A patent/HK132693A/en not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| ZW14985A1 (en) | 1986-01-29 |
| GB2176191B (en) | 1989-06-01 |
| GB8610243D0 (en) | 1986-05-29 |
| CA1340213C (en) | 1998-12-15 |
| WO1986001802A1 (en) | 1986-03-27 |
| JPH0698773A (ja) | 1994-04-12 |
| SG119293G (en) | 1994-01-21 |
| EP0193586B1 (en) | 1993-08-04 |
| AU4732685A (en) | 1986-03-20 |
| SG65089G (en) | 1990-01-26 |
| OA08325A (en) | 1988-02-29 |
| HK132693A (en) | 1993-12-10 |
| GB2176191A (en) | 1986-12-17 |
| DE3587503T2 (de) | 1993-11-25 |
| MY102593A (en) | 1992-08-17 |
| EP0193586A1 (en) | 1986-09-10 |
| EP0193586A4 (en) | 1988-03-22 |
| DE3587503D1 (en) | 1993-09-09 |
| AU599305B2 (en) | 1990-07-19 |
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