메뉴 건너뛰기




Volumn 19, Issue 7, 2018, Pages

p19-targeting ILP protein blockers of IL-23/Th-17 pro-inflammatory axis displayed on engineered bacteria of food origin

Author keywords

Albumin binding domain; Binding protein; Cytokine; IL 23; Lactococcus; Surface display

Indexed keywords

CELL SURFACE RECEPTOR; FUSION PROTEIN; IMMUNOMODULATING AGENT; INTERLEUKIN 23; INTERLEUKIN BINDING PROTEIN; MONOCLONAL ANTIBODY; PROTEIN P19; THIOREDOXIN; UNCLASSIFIED DRUG; PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 85049569279     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms19071933     Document Type: Article
Times cited : (21)

References (50)
  • 2
    • 85040588564 scopus 로고    scopus 로고
    • The role of IL-23 receptor signaling in inflammation-mediated erosive autoimmune arthritis and bone remodeling
    • Razawy, W.; van Driel, M.; Lubberts, E. The role of IL-23 receptor signaling in inflammation-mediated erosive autoimmune arthritis and bone remodeling. Eur. J. Immunol. 2018, 48, 220–229. [CrossRef] [PubMed]
    • (2018) Eur. J. Immunol. , vol.48 , pp. 220-229
    • Razawy, W.1    van Driel, M.2    Lubberts, E.3
  • 3
    • 85028328162 scopus 로고    scopus 로고
    • The Role of Proinflammatory Pathways in the Pathogenesis of Colitis-Associated Colorectal Cancer
    • Luo, C.; Zhang, H. The Role of Proinflammatory Pathways in the Pathogenesis of Colitis-Associated Colorectal Cancer. Mediat. Inflamm. 2017, 2017, 5126048. [CrossRef] [PubMed]
    • (2017) Mediat. Inflamm. , vol.2017
    • Luo, C.1    Zhang, H.2
  • 5
    • 84875935592 scopus 로고    scopus 로고
    • Role of the IL-23/IL-17 axis in Crohn’s disease
    • Siakavellas, S.I.; Bamias, G. Role of the IL-23/IL-17 axis in Crohn’s disease. Discov. Med. 2012, 14, 253–262. [PubMed]
    • (2012) Discov. Med. , vol.14 , pp. 253-262
    • Siakavellas, S.I.1    Bamias, G.2
  • 7
    • 84906535154 scopus 로고    scopus 로고
    • The IL-23-IL-17 immune axis: From mechanisms to therapeutic testing
    • Gaffen, S.L.; Jain, R.; Garg, A.V.; Cua, D.J. The IL-23-IL-17 immune axis: From mechanisms to therapeutic testing. Nat. Rev. Immunol. 2014, 14, 585–600. [CrossRef] [PubMed]
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 585-600
    • Gaffen, S.L.1    Jain, R.2    Garg, A.V.3    Cua, D.J.4
  • 8
    • 85044475552 scopus 로고    scopus 로고
    • A Systematic Review and Meta-Analysis of the Efficacy and Safety of the Interleukin (IL)-12/23 and IL-17 Inhibitors Ustekinumab, Secukinumab, Ixekizumab, Brodalumab, Guselkumab, and Tildrakizumab for the Treatment of Moderate to Severe Plaque Psoriasis
    • Bilal, J.; Berlinberg, A.; Bhattacharjee, S.; Trost, J.; Riaz, I.B.; Kurtzman, D.J.B. A Systematic Review and Meta-Analysis of the Efficacy and Safety of the Interleukin (IL)-12/23 and IL-17 Inhibitors Ustekinumab, Secukinumab, Ixekizumab, Brodalumab, Guselkumab, and Tildrakizumab for the Treatment of Moderate to Severe Plaque Psoriasis. J. Dermatol. Treat. 2018, 1–37. [CrossRef] [PubMed]
    • (2018) J. Dermatol. Treat. , pp. 1-37
    • Bilal, J.1    Berlinberg, A.2    Bhattacharjee, S.3    Trost, J.4    Riaz, I.B.5    Kurtzman, D.J.B.6
  • 13
    • 84900813603 scopus 로고    scopus 로고
    • Human interleukin-23 receptor antagonists derived from an albumin-binding domain scaffold inhibit IL-23-dependent ex vivo expansion of IL-17-producing T-cells
    • Kuchar, M.; Vankova, L.; Petrokova, H.; Cerny, J.; Osicka, R.; Pelak, O.; Sipova, H.; Schneider, B.; Homola, J.; Sebo, P.; et al. Human interleukin-23 receptor antagonists derived from an albumin-binding domain scaffold inhibit IL-23-dependent ex vivo expansion of IL-17-producing T-cells. Proteins 2014, 82, 975–989. [CrossRef] [PubMed]
    • (2014) Proteins , vol.82 , pp. 975-989
    • Kuchar, M.1    Vankova, L.2    Petrokova, H.3    Cerny, J.4    Osicka, R.5    Pelak, O.6    Sipova, H.7    Schneider, B.8    Homola, J.9    Sebo, P.10
  • 14
    • 85009968778 scopus 로고    scopus 로고
    • P19-targeted ABD-derived protein variants inhibit IL-23 binding and exert suppressive control over IL-23-stimulated expansion of primary human IL-17+ T-cells
    • Krizova, L.; Kuchar, M.; Petrokova, H.; Osicka, R.; Hlavnickova, M.; Pelak, O.; Cerny, J.; Kalina, T.; Maly, P. p19-targeted ABD-derived protein variants inhibit IL-23 binding and exert suppressive control over IL-23-stimulated expansion of primary human IL-17+ T-cells. Autoimmunity 2017, 50, 102–113. [CrossRef] [PubMed]
    • (2017) Autoimmunity , vol.50 , pp. 102-113
    • Krizova, L.1    Kuchar, M.2    Petrokova, H.3    Osicka, R.4    Hlavnickova, M.5    Pelak, O.6    Cerny, J.7    Kalina, T.8    Maly, P.9
  • 15
    • 0034464730 scopus 로고    scopus 로고
    • Oral administration of avian tumor necrosis factor antibodies effectively treats experimental colitis in rats
    • Worledge, K.L.; Godiska, R.; Barrett, T.A.; Kink, J.A. Oral administration of avian tumor necrosis factor antibodies effectively treats experimental colitis in rats. Dig. Dis. Sci. 2000, 45, 2298–2305. [CrossRef] [PubMed]
    • (2000) Dig. Dis. Sci. , vol.45 , pp. 2298-2305
    • Worledge, K.L.1    Godiska, R.2    Barrett, T.A.3    Kink, J.A.4
  • 16
    • 84908221805 scopus 로고    scopus 로고
    • Targeting of gastrointestinal tract for amended delivery of protein/peptide therapeutics: Strategies and industrial perspectives
    • Pawar, V.K.; Meher, J.G.; Singh, Y.; Chaurasia, M.; Surendar Reddy, B.; Chourasia, M.K. Targeting of gastrointestinal tract for amended delivery of protein/peptide therapeutics: Strategies and industrial perspectives. J. Control. Release 2014, 196, 168–183. [CrossRef] [PubMed]
    • (2014) J. Control. Release , vol.196 , pp. 168-183
    • Pawar, V.K.1    Meher, J.G.2    Singh, Y.3    Chaurasia, M.4    Surendar Reddy, B.5    Chourasia, M.K.6
  • 18
    • 84906841405 scopus 로고    scopus 로고
    • Functional genomics of lactic acid bacteria: From food to health
    • Douillard, F.P.; de Vos, W.M. Functional genomics of lactic acid bacteria: From food to health. Microb. Cell Factor 2014, 13. [CrossRef] [PubMed]
    • (2014) Microb. Cell Factor , vol.13
    • Douillard, F.P.1    de Vos, W.M.2
  • 19
    • 40049093710 scopus 로고    scopus 로고
    • Probiotics: Definition, sources, selection, and uses
    • discussion S144–S51
    • Sanders, M.E. Probiotics: Definition, sources, selection, and uses. Clin. Infect. Dis. 2008, 46 (Suppl. 2), S58–S61, discussion S144–S51. [CrossRef] [PubMed]
    • (2008) Clin. Infect. Dis. , vol.46 , pp. S58-S61
    • Sanders, M.E.1
  • 21
    • 84934933158 scopus 로고    scopus 로고
    • Host lysozyme-mediated lysis of Lactococcus lactis facilitates delivery of colitis-attenuating superoxide dismutase to inflamed colons
    • Ballal, S.A.; Veiga, P.; Fenn, K.; Michaud, M.; Kim, J.H.; Gallini, C.A.; Glickman, J.N.; Quere, G.; Garault, P.; Beal, C.; et al. Host lysozyme-mediated lysis of Lactococcus lactis facilitates delivery of colitis-attenuating superoxide dismutase to inflamed colons. Proc. Natl. Acad. Sci. USA 2015, 112, 7803–7808. [CrossRef] [PubMed]
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 7803-7808
    • Ballal, S.A.1    Veiga, P.2    Fenn, K.3    Michaud, M.4    Kim, J.H.5    Gallini, C.A.6    Glickman, J.N.7    Quere, G.8    Garault, P.9    Beal, C.10
  • 22
    • 84928007861 scopus 로고    scopus 로고
    • Anti-inflammatory properties of fermented soy milk with Lactococcus lactis subsp. Lactis S-SU2 in murine macrophage RAW264.7 cells and DSS-induced IBD model mice
    • Kawahara, M.; Nemoto, M.; Nakata, T.; Kondo, S.; Takahashi, H.; Kimura, B.; Kuda, T. Anti-inflammatory properties of fermented soy milk with Lactococcus lactis subsp. lactis S-SU2 in murine macrophage RAW264.7 cells and DSS-induced IBD model mice. Int. Immunopharmacol. 2015, 26, 295–303. [CrossRef] [PubMed]
    • (2015) Int. Immunopharmacol. , vol.26 , pp. 295-303
    • Kawahara, M.1    Nemoto, M.2    Nakata, T.3    Kondo, S.4    Takahashi, H.5    Kimura, B.6    Kuda, T.7
  • 23
    • 0032729983 scopus 로고    scopus 로고
    • Survival, physiology, and lysis of Lactococcus lactis in the digestive tract
    • Drouault, S.; Corthier, G.; Ehrlich, S.D.; Renault, P. Survival, physiology, and lysis of Lactococcus lactis in the digestive tract. Appl. Environ. Microbiol. 1999, 65, 4881–4886. [PubMed]
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4881-4886
    • Drouault, S.1    Corthier, G.2    Ehrlich, S.D.3    Renault, P.4
  • 24
    • 84869054314 scopus 로고    scopus 로고
    • Lactic acid bacteria as oral delivery systems for biomolecules
    • Berlec, A.; Ravnikar, M.; Strukelj, B. Lactic acid bacteria as oral delivery systems for biomolecules. Pharmazie 2012, 67, 891–898. [PubMed]
    • (2012) Pharmazie , vol.67 , pp. 891-898
    • Berlec, A.1    Ravnikar, M.2    Strukelj, B.3
  • 26
    • 85017006210 scopus 로고    scopus 로고
    • A review on Lactococcus lactis: From food to factory
    • Song, A.A.; In, L.L.A.; Lim, S.H.E.; Rahim, R.A. A review on Lactococcus lactis: From food to factory. Microb. Cell Fact. 2017, 16, 55. [CrossRef] [PubMed]
    • (2017) Microb. Cell Fact. , vol.16 , pp. 55
    • Song, A.A.1    In, L.L.A.2    Lim, S.H.E.3    Rahim, R.A.4
  • 28
    • 85007471058 scopus 로고    scopus 로고
    • Dextran sulphate sodium colitis in C57BL/6J mice is alleviated by Lactococcus lactis and worsened by the neutralization of Tumor necrosis Factor alpha
    • Berlec, A.; Perse, M.; Ravnikar, M.; Lunder, M.; Erman, A.; Cerar, A.; Strukelj, B. Dextran sulphate sodium colitis in C57BL/6J mice is alleviated by Lactococcus lactis and worsened by the neutralization of Tumor necrosis Factor alpha. Int. Immunopharmacol. 2017, 43, 219–226. [CrossRef] [PubMed]
    • (2017) Int. Immunopharmacol , vol.43 , pp. 219-226
    • Berlec, A.1    Perse, M.2    Ravnikar, M.3    Lunder, M.4    Erman, A.5    Cerar, A.6    Strukelj, B.7
  • 29
    • 4143082646 scopus 로고    scopus 로고
    • Active delivery of trefoil factors by genetically modified Lactococcus lactis prevents and heals acute colitis in mice
    • Vandenbroucke, K.; Hans, W.; Van Huysse, J.; Neirynck, S.; Demetter, P.; Remaut, E.; Rottiers, P.; Steidler, L. Active delivery of trefoil factors by genetically modified Lactococcus lactis prevents and heals acute colitis in mice. Gastroenterology 2004, 127, 502–513. [CrossRef] [PubMed]
    • (2004) Gastroenterology , vol.127 , pp. 502-513
    • Vandenbroucke, K.1    Hans, W.2    van Huysse, J.3    Neirynck, S.4    Demetter, P.5    Remaut, E.6    Rottiers, P.7    Steidler, L.8
  • 32
    • 77958608927 scopus 로고    scopus 로고
    • Engineered lactic acid bacterium Lactococcus lactis capable of binding antibodies and tumor necrosis factor alpha
    • Ravnikar, M.; Strukelj, B.; Obermajer, N.; Lunder, M.; Berlec, A. Engineered lactic acid bacterium Lactococcus lactis capable of binding antibodies and tumor necrosis factor alpha. Appl. Environ. Microbiol. 2010, 76, 6928–6932. [CrossRef] [PubMed]
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 6928-6932
    • Ravnikar, M.1    Strukelj, B.2    Obermajer, N.3    Lunder, M.4    Berlec, A.5
  • 33
    • 85032385376 scopus 로고    scopus 로고
    • Evasin-displaying lactic acid bacteria bind different chemokines and neutralize CXCL8 production in Caco-2 cells
    • Skrlec, K.; Pucer Janez, A.; Rogelj, B.; Strukelj, B.; Berlec, A. Evasin-displaying lactic acid bacteria bind different chemokines and neutralize CXCL8 production in Caco-2 cells. Microb. Biotechnol. 2017, 10, 1732–1743. [CrossRef] [PubMed]
    • (2017) Microb. Biotechnol. , vol.10 , pp. 1732-1743
    • Skrlec, K.1    Pucer Janez, A.2    Rogelj, B.3    Strukelj, B.4    Berlec, A.5
  • 34
    • 84977643680 scopus 로고    scopus 로고
    • Display of recombinant proteins at the surface of lactic acid bacteria: Strategies and applications
    • Michon, C.; Langella, P.; Eijsink, V.G.; Mathiesen, G.; Chatel, J.M. Display of recombinant proteins at the surface of lactic acid bacteria: Strategies and applications. Microb. Cell Factor. 2016, 15, 70. [CrossRef] [PubMed]
    • (2016) Microb. Cell Factor. , vol.15 , pp. 70
    • Michon, C.1    Langella, P.2    Eijsink, V.G.3    Mathiesen, G.4    Chatel, J.M.5
  • 35
    • 0034971985 scopus 로고    scopus 로고
    • Design of a protein-targeting system for lactic acid bacteria
    • Dieye, Y.; Usai, S.; Clier, F.; Gruss, A.; Piard, J.C. Design of a protein-targeting system for lactic acid bacteria. J. Bacteriol. 2001, 183, 4157–4166. [CrossRef] [PubMed]
    • (2001) J. Bacteriol. , vol.183 , pp. 4157-4166
    • Dieye, Y.1    Usai, S.2    Clier, F.3    Gruss, A.4    Piard, J.C.5
  • 36
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist, G.; Kok, J.; Leenhouts, K.J.; Dabrowska, M.; Venema, G.; Haandrikman, A.J. Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J. Bacteriol. 1995, 177, 1554–1563. [CrossRef] [PubMed]
    • (1995) J. Bacteriol. , vol.177 , pp. 1554-1563
    • Buist, G.1    Kok, J.2    Leenhouts, K.J.3    Dabrowska, M.4    Venema, G.5    Haandrikman, A.J.6
  • 37
    • 20444471564 scopus 로고    scopus 로고
    • AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning
    • Steen, A.; Buist, G.; Horsburgh, G.J.; Venema, G.; Kuipers, O.P.; Foster, S.J.; Kok, J. AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning. FEBS J. 2005, 272, 2854–2868. [CrossRef] [PubMed]
    • (2005) FEBS J , vol.272 , pp. 2854-2868
    • Steen, A.1    Buist, G.2    Horsburgh, G.J.3    Venema, G.4    Kuipers, O.P.5    Foster, S.J.6    Kok, J.7
  • 38
    • 85020391777 scopus 로고    scopus 로고
    • Lactic Acid Bacteria with Concomitant IL-17, IL-23 and TNFalpha-Binding Ability for the Treatment of Inflammatory Bowel Disease
    • Kosler, S.; Strukelj, B.; Berlec, A. Lactic Acid Bacteria with Concomitant IL-17, IL-23 and TNFalpha-Binding Ability for the Treatment of Inflammatory Bowel Disease. Curr. Pharm. Biotechnol. 2017, 18, 318–326. [CrossRef] [PubMed]
    • (2017) Curr. Pharm. Biotechnol. , vol.18 , pp. 318-326
    • Kosler, S.1    Strukelj, B.2    Berlec, A.3
  • 40
    • 0029177438 scopus 로고
    • Transformation of Lactococcus by electroporation
    • Holo, H.; Nes, I.F. Transformation of Lactococcus by electroporation. Methods Mol. Biol. 1995, 47, 195–199. [PubMed]
    • (1995) Methods Mol. Biol. , vol.47 , pp. 195-199
    • Holo, H.1    Nes, I.F.2
  • 42
    • 27544451339 scopus 로고    scopus 로고
    • 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis
    • Mierau, I.; Kleerebezem, M. 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis. Appl. Microbiol. Biotechnol. 2005, 68, 705–717. [CrossRef] [PubMed]
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 705-717
    • Mierau, I.1    Kleerebezem, M.2
  • 43
    • 84949215654 scopus 로고    scopus 로고
    • Comparative Protein Structure Modeling Using MODELLER
    • Webb, B.; Sali, A. Comparative Protein Structure Modeling Using MODELLER. Curr. Protoc. Bioinform. 2014, 47, 561-32. [CrossRef] [PubMed]
    • (2014) Curr. Protoc. Bioinform. , vol.47 , pp. 561-632
    • Webb, B.1    Sali, A.2
  • 44
    • 51249094703 scopus 로고    scopus 로고
    • The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12
    • Lupardus, P.J.; Garcia, K.C. The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12. J. Mol. Biol. 2008, 382, 931–941. [CrossRef] [PubMed]
    • (2008) J. Mol. Biol. , vol.382 , pp. 931-941
    • Lupardus, P.J.1    Garcia, K.C.2
  • 45
    • 85008042563 scopus 로고    scopus 로고
    • OpenMM: A Hardware Independent Framework for Molecular Simulations
    • Eastman, P.; Pande, V.S. OpenMM: A Hardware Independent Framework for Molecular Simulations. Comput. Sci. Eng. 2015, 12, 34–39. [CrossRef] [PubMed]
    • (2015) Comput. Sci. Eng , vol.12 , pp. 34-39
    • Eastman, P.1    Pande, V.S.2
  • 48
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32, 1792–1797. [CrossRef] [PubMed]
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 50
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: An FFT-based protein docking program with pairwise potentials
    • Kozakov, D.; Brenke, R.; Comeau, S.R.; Vajda, S. PIPER: An FFT-based protein docking program with pairwise potentials. Proteins 2006, 65, 392–406. [CrossRef] [PubMed]
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.