JP6034188B2 - 抗微生物剤 - Google Patents
抗微生物剤 Download PDFInfo
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- JP6034188B2 JP6034188B2 JP2012516777A JP2012516777A JP6034188B2 JP 6034188 B2 JP6034188 B2 JP 6034188B2 JP 2012516777 A JP2012516777 A JP 2012516777A JP 2012516777 A JP2012516777 A JP 2012516777A JP 6034188 B2 JP6034188 B2 JP 6034188B2
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- ZSKVGTPCRGIANV-ZXFLCMHBSA-N imipenem Chemical compound C1C(SCC\N=C\N)=C(C(O)=O)N2C(=O)[C@H]([C@H](O)C)[C@H]21 ZSKVGTPCRGIANV-ZXFLCMHBSA-N 0.000 description 1
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- MGIUUAHJVPPFEV-ABXDCCGRSA-N magainin ii Chemical compound C([C@H](NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O)C1=CC=CC=C1 MGIUUAHJVPPFEV-ABXDCCGRSA-N 0.000 description 1
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- VDXZNPDIRNWWCW-JFTDCZMZSA-N melittin Chemical compound NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(N)=O)CC1=CNC2=CC=CC=C12 VDXZNPDIRNWWCW-JFTDCZMZSA-N 0.000 description 1
- 230000007102 metabolic function Effects 0.000 description 1
- 108010005942 methionylglycine Proteins 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 210000000214 mouth Anatomy 0.000 description 1
- 229940051921 muramidase Drugs 0.000 description 1
- 229950006780 n-acetylglucosamine Drugs 0.000 description 1
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- 230000001338 necrotic effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
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- 238000003199 nucleic acid amplification method Methods 0.000 description 1
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- 229940049954 penicillin Drugs 0.000 description 1
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- 230000004850 protein–protein interaction Effects 0.000 description 1
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- 150000003856 quaternary ammonium compounds Chemical class 0.000 description 1
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- SPIDLBQKAFAVOG-HTZUFYBVSA-N sarcotoxin ia Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(N)=O)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)C(C)C)C1=CN=CN1 SPIDLBQKAFAVOG-HTZUFYBVSA-N 0.000 description 1
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- 229960002180 tetracycline Drugs 0.000 description 1
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- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
-
- 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
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2462—Lysozyme (3.2.1.17)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/33—Fusion polypeptide fusions for targeting to specific cell types, e.g. tissue specific targeting, targeting of a bacterial subspecies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Pharmacology & Pharmacy (AREA)
- Communicable Diseases (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Food Preservation Except Freezing, Refrigeration, And Drying (AREA)
- Cosmetics (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Description
[本発明1001]
グラム陽性細菌の細胞壁を分解する活性を有する酵素、および、該酵素のN末端もしくはC末端、または両方の末端において融合されるペプチドストレッチから構成される、融合タンパク質。
[本発明1002]
N末端に追加的なアミノ酸残基を含む、本発明1001の融合タンパク質。
[本発明1003]
SEQ ID NO: 63〜90記載のアミノ酸配列を呈する、本発明1001または1002の融合タンパク質。
[本発明1004]
C末端および/またはN末端にタグまたは追加的なタンパク質を含む、前記本発明のいずれかの融合タンパク質。
[本発明1005]
タグまたは追加的なタンパク質が、1個または複数の追加的なアミノ酸残基によって融合タンパク質に連結されている、本発明1004の融合タンパク質。
[本発明1006]
ペプチドストレッチが、1個または複数の追加的なアミノ酸残基によって融合タンパク質に連結されている、前記本発明のいずれかの融合タンパク質。
[本発明1007]
酵素が、エンドリシン、オートリシン、またはバクテリオシンである、本発明1001の融合タンパク質。
[本発明1008]
酵素が、SEQ ID NO: 57〜61記載のアミノ酸配列を呈する、本発明1007の融合タンパク質。
[本発明1009]
グラム陽性細菌が、表1に列挙される細菌からなる群より選択される、前記本発明のいずれかの融合タンパク質。
[本発明1010]
ペプチドストレッチが、カチオン性、より好ましくはポリカチオン性ペプチド、両親媒性ペプチド、スシ(sushi)ペプチド、デフェンシン、疎水性ペプチド、または抗微生物ペプチドである、前記本発明のいずれかの融合タンパク質。
[本発明1011]
スシペプチドが、SEQ ID NO: 54記載のアミノ酸配列を呈する、本発明1010の融合タンパク質。
[本発明1012]
カチオン性ペプチドが、アルギニン、ヒスチジン、およびリジン残基からなる群より選択される少なくとも1個のアミノ酸残基を含む、本発明1010の融合タンパク質。
[本発明1013]
抗微生物ペプチドが、SEQ ID NO:1〜11、または48〜53記載のアミノ酸配列を呈する、本発明1010の融合タンパク質。
[本発明1014]
疎水性ペプチドが、SEQ ID NO: 12、50、55、または56記載のアミノ酸配列を呈する、本発明1010の融合タンパク質。
[本発明1015]
カチオン性ペプチドに含まれるアミノ酸残基の少なくとも約70%が、アルギニン、ヒスチジン、もしくはリジン残基のいずれかであるか、または、該ペプチドに含まれるアミノ酸残基の少なくとも約70%が、アルギニンもしくはリジンのいずれかであるか、または、該ペプチドに含まれるアミノ酸残基が、アルギニンもしくはリジン残基のいずれかである、本発明1010の融合タンパク質。
[本発明1016]
カチオン性ペプチドが、SEQ ID NO: 13、または24〜44記載のアミノ酸配列を呈する、本発明1015の融合タンパク質。
[本発明1017]
両親媒性ペプチドが、バリン、イソロイシン、ロイシン、メチオニン、フェニルアラニン、トリプトファン、システイン、アラニン、チロシン、ヒスチジン、スレオニン、セリン、プロリン、およびグリシン残基からなる群より選択される少なくとも1個の疎水性アミノ酸残基と組み合わせて、リジン、アルギニン、およびヒスチジン残基からなる群より選択される少なくとも1個の正に荷電したアミノ酸残基を含む、本発明1010の融合タンパク質。
[本発明1018]
両親媒性ペプチドにおけるアミノ酸残基の少なくとも約70%が、アルギニンまたはリジン残基のいずれかであり、かつ、該両親媒性ペプチドにおける該アミノ酸残基の少なくとも約30%が、バリン、イソロイシン、ロイシン、メチオニン、フェニルアラニン、トリプトファン、システイン、アラニン、チロシン、ヒスチジン、スレオニン、セリン、プロリン、またはグリシン残基である、本発明1017の融合タンパク質。
[本発明1019]
両親媒性ペプチドが、SEQ ID NO: 1〜5、23、48、または49記載のアミノ酸配列を呈する、本発明1018の融合タンパク質。
[本発明1020]
ペプチドストレッチが、約5〜約100個のアミノ酸残基、とりわけ約5〜50個のアミノ酸残基、とりわけ約5〜30個のアミノ酸残基を含む、本発明1001〜1019のいずれかの融合タンパク質。
[本発明1021]
本発明1001〜1019のいずれかの融合タンパク質をコードする、単離された核酸分子。
[本発明1022]
本発明1021の核酸分子を含む、ベクター。
[本発明1023]
本発明1021の核酸分子、または本発明1122のベクターを含む、宿主細胞。
[本発明1024]
細菌細胞または酵母細胞である、本発明1023の宿主細胞。
[本発明1025]
酵母細胞が、ピキア・パストリス(Pichia pastoris)細胞である、本発明1024の宿主細胞。
[本発明1026]
医用薬剤、診断手段、または美容用物質としての使用のための、本発明1001〜1020のいずれかの融合タンパク質。
[本発明1027]
グラム陽性細菌感染症の処置または予防用の医用薬剤としての使用のための、本発明1001〜1020のいずれかの融合タンパク質。
[本発明1028]
殺菌剤としての使用のための、本発明1001〜1020のいずれかの融合タンパク質。
[本発明1029]
食材の、食品加工器具の、食品加工設備の、食材と接触する表面の、医療装置の、病院および手術室における表面の、グラム陽性細菌汚染の処置または予防のための、本発明1001〜1020のいずれかの融合タンパク質の使用。
[本発明1030]
医薬、食品、もしくは飼料における診断手段、または環境診断法としての、本発明1001〜1020のいずれかの融合タンパク質の使用。
[本発明1031]
本発明1001〜1020のいずれかの融合タンパク質を含む、薬学的組成物。
I.門:放線菌門(Actinobacteria)
綱:放線菌綱(Actinobacteridae)
目:放線菌目(Actinomycetales)
科:
アクチノマイセス亜目(Actinomycineae):アクチノマイセス科(Actinomycetaceae)(アクチノマイセス属(Actinomyces)、モビルンカス属(Mobiluncus))
コリネバクテリウム亜目(Corynebacterineae):マイコバクテリウム科(Mycobacteriaceae)(マイコバクテリウム属(Mycobacterium))、ノカルディア科(Nocardiaceae)、コリネバクテリウム科(Corynebacteriaceae)
フランキア亜目(Frankineae):フランキア科(Frankiaceae)
マイクロコッカス亜目(Micrococcineae):ブレビバクテリウム科(Brevibacteriaceae)
プロピオニバクテリウム科(Propionibacteriaceae)(プロピオニバクテリウム属(Propionibacterium))
目:ビフィドバクテリウム目(Bifidobacteriales)
科:
ビフィドバクテリウム科(Bifidobacteriaceae)(ビフィドバクテリウム属(Bifidobacterium)、ファルシビブリオ属(Falcivibrio)、ガードネレラ属(Gardnerella))
他の亜綱:アシドミクロビウム亜綱(Acidimicrobidae)、コリオバクター亜綱(Coriobacteridae)、ルブロバクター亜綱(Rubrobacteridae)、スフェロバクター亜綱(Sphaerobacteridae)
II.門:フィルミクテス門(Firmicutes)
綱:バチルス綱(Bacilli)
目:バチルス目(Bacillales):
科:
バチルス科(Bacillaceae)(バチルス属(Bacillus))、リステリア科(Listeriaceae)(リステリア属(Listeria))、スタフィロコッカス科(Staphylococcaceae)(スタフィロコッカス属、ゲメラ属(Gemella)、ジェオトガリコッカス属(Jeotgalicoccus))
目:ラクトバチルス目(Lactobacillales):
科:エンテロコッカス科(Enterococcaceae)(エンテロコッカス属)、ラクトバチルス科(Lactobacillaceae)(ラクトバチルス属(Lactobacillus)、ペディオコッカス属(Pediococcus))、ロイコノストック科(Leuconostocaceae)(ロイコノストック属(Leuconostoc))、ストレプトコッカス科(Streptococcaceae)(ラクトコッカス属(Lactococcus)、ストレプトコッカス属)
綱:クロストリジウム綱(Clostridia)
目:クロストリジウム目(Clostridiales)(クロストリジウム属(Clostridium)、ペプトストレプトコッカス属(Peptostreptococcus)、セレノモナス属(Selenomonas))
目:ハルアナエロビウム目(Halanaerobiales)
目:サーモアナエロバクター目(Thermoanaerobacterales)
綱:テネリクテス綱(Tenericutes)/モリクテス綱(Mollicutes)
目:マイコプラズマ目(Mycoplasmatales)(マイコプラズマ属(Mycoplasma、ウレアプラズマ属(Ureaplasma))
目:エントモプラズマ目(Entomoplasmatales)(スピロプラズマ属(Spiroplasma))
目:アナエロプラズマ目(Anaeroplasmatales)(エリジペロスリックス属(Erysipelothrix))
目:アコレプラズマ目(Acholeplasmatales)(アコレプラズマ属(Acholeplasma))
目:ハロプラズマ目(Haloplasmatales)(ハロプラズマ属(Haloplasma))
SEQ ID NO: 57記載のCpl-1は、ストレプトコッカス・ニューモニエ ファージCpl-1に由来するエンドリシンである。エンドリシンCpl-1は、SEQ ID NO: 91記載の核酸によってコードされる。SEQ ID NO: 91記載の核酸分子を、核酸分子の5'端にBamH I (5'-GGA TCC-3')制限部位を、および核酸分子の3'端にXho I (5'-CTC GAG-3')制限部位を伴って合成的に産生した。
1.3〜5 ml/分の流速での、10カラム容量までの洗浄緩衝液(20 mMイミダゾール、1 M NaCl、および20 mM Hepes、pH7.4)でのHistrap FF 5 mlカラム(GE Healthcare)の平衡化。
2.3〜5 ml/分の流速での、Histrap FF 5 mlカラムへの全溶解物(求められる融合タンパク質を含む)のローディング。
3.3〜5 ml/分の流速での、結合していない試料を除去するための10カラム容量までの洗浄緩衝液でのカラムの洗浄、続いて10%溶出緩衝液(500 mMイミダゾール、0.5 M NaCl、および20 mM Hepes、pH7.4)での第2の洗浄段階。
4.3〜5 ml/分の流速での、4カラム容量の溶出緩衝液(500 mMイミダゾール、0.5 M NaCl、および20 mM Hepes、pH7.4)の100%への直線勾配での、結合した融合タンパク質のカラムからの溶出。
N末端ペプチドストレッチのシュージン1、WLBU2-変異体、LL-37、インドリシジン、マガイニン、プレウロシジン、セクロピンA(ネッタイシマカ)、ブフォリンII、ザルコトキシンIA、およびPKを伴うCpl 1である融合タンパク質を、実施例1において記載したように産生した。ストレプトコッカス・ニューモニエDSMZ 11967およびストレプトコッカス・ニューモニエDSMZ 14378に対する融合タンパク質の抗微生物活性を、以下に記載するプレーティング試験を使用することによって試験した。測定した融合タンパク質の活性を表6に示す。
例えば、ストレプトコッカス属、リステリア属、プロピオニバクテリウム属、またはスタフィロコッカス属の対数増殖期の細胞を取得し(1ml)、氷上で冷却し、蒸留水で洗浄した。細菌を20mMトリス pH 7.0、1 mM MgCl2、0.5 Mショ糖に再懸濁した。融合タンパク質を再懸濁緩衝液において希釈し、0.5 Mの最終濃度までショ糖を添加して、それぞれの細菌と共に60分間室温でインキュベーションした(融合タンパク質の最終濃度は約10μg/ml)。その後、0.5 Mショ糖を含有する適切な寒天プレート(例えば、ストレプトコッカス属:コロンビア血液寒天)上に細菌をプレーティングし、インキュベーション後に結果として生じたコロニーを計数した。
SEQ ID NO: 12記載のN末端ペプチドストレッチのペンタペプチドを伴うPly511である融合タンパク質を、実施例1において記載したように産生した。リステリア・モノサイトゲネスDSMZ 15675およびリステリア・モノサイトゲネスDSMZ 20600に対する融合タンパク質の抗微生物活性を、実施例2において記載したプレーティング試験を使用することによって試験した。測定した融合タンパク質の活性を表7に示す。
SEQ ID NO: 13記載のN末端ペプチドストレッチPKをそれぞれ伴うLssおよびLysKである融合タンパク質、SEQ ID NO:31記載のN末端ペプチドストレッチPK2を伴うLssである融合タンパク質、ならびに、C末端ペプチドストレッチPKをそれぞれ伴うLssおよびLysKである融合タンパク質を、実施例1において記載したように産生した。スタフィロコッカス・アウレウスDSMZ 346およびスタフィロコッカス・エピデルミディス(Staphylococcus epidermidis)DSMZ 20041に対する融合タンパク質の抗微生物活性を、実施例2において記載したプレーティング試験を使用することによって、および以下に記載するような溶解試験を使用することによって試験した。
これらの融合タンパク質の抗微生物効果を検討するために、改変されたLysKおよびリゾスタフィンについて溶解試験を使用した。
SEQ ID NO: 56記載のN末端ペプチドストレッチのワルマフ1を伴うPA6-gp20である融合タンパク質を、実施例1において記載したように産生した。プロピオニバクテリウム・アクネスDSMZ 1897およびプロピオニバクテリウム・アクネスDSMZ 16379に対する融合タンパク質の抗微生物活性を、実施例2において記載したプレーティング試験を使用することによって試験した。測定した融合タンパク質の活性を表9に示す。
Claims (20)
- グラム陽性細菌の細胞壁を分解する活性を有するエンドリシン、および、該エンドリシンのN末端もしくはC末端、または両方の末端において融合される両親媒性ペプチドストレッチから構成される、融合タンパク質であって、該両親媒性ペプチドストレッチが、5〜100個のアミノ酸残基を含み、かつ両親媒性ペプチドストレッチが、SEQ ID NO: 7、1、3、4、9、11、および51からなる群より選択される、前記融合タンパク質。
- 両親媒性ペプチドストレッチが、5〜50個のアミノ酸残基を含む、請求項1記載の融合タンパク質。
- 両親媒性ペプチドストレッチが、天然に存在するペプチドである、請求項1または2記載の融合タンパク質。
- 融合タンパク質が、N末端に追加的なアミノ酸残基を含む、および/またはペプチドストレッチが、1個もしくは複数の追加的なアミノ酸残基によって融合タンパク質に連結されている、請求項1〜3のいずれか一項記載の融合タンパク質。
- グラム陽性細菌が、バチルス(Bacilli)綱の細菌である、請求項1〜4のいずれか一項記載の融合タンパク質。
- グラム陽性細菌が、スタフィロコッカス(Staphylococcus)および/またはストレプトコッカス(Streptococcus)である、請求項5記載の融合タンパク質。
- エンドリシンが、SEQ ID NO: 59、57、58、60もしくは61に記載のアミノ酸を有するエンドリシンである、請求項1〜5のいずれか一項記載の融合タンパク質。
- 前記アミノ酸残基の少なくとも30%が、正に荷電したアミノ酸残基であるリジン、アルギニン、および/またはヒスチジンである、請求項1〜7のいずれか一項記載の融合タンパク質。
- 融合タンパク質が、C末端および/またはN末端にタグまたは追加的なタンパク質を含む、請求項1〜8のいずれか一項記載の融合タンパク質。
- タグまたは追加的なタンパク質が、1個または複数の追加的なアミノ酸残基によって融合タンパク質に連結されている、請求項9記載の融合タンパク質。
- SEQ ID NO: 72、76、77、78、または81に記載のアミノ酸配列を示す、請求項1〜10のいずれか一項記載の融合タンパク質。
- 請求項1〜11のいずれか一項記載の融合タンパク質をコードする、単離された核酸分子。
- 請求項12記載の核酸分子を含む、ベクター。
- 請求項12記載の核酸分子、または請求項13記載のベクターを含む、宿主細胞。
- 請求項1〜11のいずれか一項記載の融合タンパク質を含む、薬学的組成物。
- 医用薬剤、診断手段、または美容用物質として使用するための、請求項15記載の薬学的組成物。
- グラム陽性細菌感染症の処置または予防用の医用薬剤として使用するための、請求項15記載の薬学的組成物。
- 殺菌剤として使用するための、請求項15記載の薬学的組成物。
- 食材の、食品加工器具の、食品加工設備の、食材と接触する表面の、医療装置の、病院および手術室における表面(ただし、ヒト表面を除く)の、グラム陽性細菌汚染の処置または予防のための、請求項1〜11のいずれか一項記載の融合タンパク質の使用。
- 医薬、食品もしくは飼料における診断手段または環境診断法として使用するための、請求項15記載の薬学的組成物。
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CA2765810A1 (en) | 2010-12-29 |
CN102482655B (zh) | 2018-04-10 |
BRPI1015203B1 (pt) | 2021-06-01 |
JP2012530510A (ja) | 2012-12-06 |
JP2017018092A (ja) | 2017-01-26 |
BRPI1015203A2 (pt) | 2016-08-02 |
US20190218538A1 (en) | 2019-07-18 |
EA201270082A1 (ru) | 2012-06-29 |
IL217121A0 (en) | 2012-02-29 |
MX2011013453A (es) | 2012-04-11 |
AU2010264659B2 (en) | 2016-08-04 |
EP2446028B1 (en) | 2018-04-04 |
CN102482655A (zh) | 2012-05-30 |
EP2446028A1 (en) | 2012-05-02 |
AU2010264659A1 (en) | 2011-12-15 |
US20120195872A1 (en) | 2012-08-02 |
WO2010149795A1 (en) | 2010-12-29 |
CA2765810C (en) | 2018-10-16 |
SG177704A1 (en) | 2012-02-28 |
KR20120061802A (ko) | 2012-06-13 |
EA038542B1 (ru) | 2021-09-13 |
EP3363896A1 (en) | 2018-08-22 |
US11136570B2 (en) | 2021-10-05 |
KR101701890B1 (ko) | 2017-02-02 |
IL217121B (en) | 2019-08-29 |
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