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Volumn 210, Issue , 2015, Pages 217-229

Immunoliposome-mediated drug delivery to Plasmodium-infected and non-infected red blood cells as a dual therapeutic/prophylactic antimalarial strategy

Author keywords

Immunoliposomes; Malaria; Nanomedicine; Plasmodium; Targeted drug delivery

Indexed keywords

ANTIBODIES; ANTIGEN-ANTIBODY REACTIONS; ANTIGENS; CELL MEMBRANES; CELLS; CYTOLOGY; DISEASES; ENCAPSULATION; ENZYME ACTIVITY; ENZYME INHIBITION; LIPOSOMES; MEDICAL NANOTECHNOLOGY; MONOCLONAL ANTIBODIES; PHOSPHOLIPIDS;

EID: 84930660625     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2015.05.284     Document Type: Article
Times cited : (72)

References (65)
  • 1
    • 34249695002 scopus 로고    scopus 로고
    • Treatment of malaria in the United States: A systematic review
    • K.S. Griffith, L.S. Lewis, S. Mali, and M.E. Parise Treatment of malaria in the United States: a systematic review JAMA 297 2007 2264 2277
    • (2007) JAMA , vol.297 , pp. 2264-2277
    • Griffith, K.S.1    Lewis, L.S.2    Mali, S.3    Parise, M.E.4
  • 4
    • 0017312150 scopus 로고
    • Drug-induced haemolysis in glucose-6-phosphate dehydrogenase deficiency
    • T.K. Chan, D. Todd, and S.C. Tso Drug-induced haemolysis in glucose-6-phosphate dehydrogenase deficiency BMJ 2 1976 1227 1229
    • (1976) BMJ , vol.2 , pp. 1227-1229
    • Chan, T.K.1    Todd, D.2    Tso, S.C.3
  • 5
    • 78649518769 scopus 로고    scopus 로고
    • On the mechanism of chloroquine resistance in Plasmodium falciparum
    • M. Chinappi, A. Via, P. Marcatili, and A. Tramontano On the mechanism of chloroquine resistance in Plasmodium falciparum PLoS One 5 2010 e14064
    • (2010) PLoS One , vol.5 , pp. e14064
    • Chinappi, M.1    Via, A.2    Marcatili, P.3    Tramontano, A.4
  • 6
    • 0024253062 scopus 로고
    • Liposomes as a drug delivery system: Optimization studies
    • G. Gregoriadis Liposomes as a drug delivery system: optimization studies Adv. Exp. Med. Biol. 238 1988 151 159
    • (1988) Adv. Exp. Med. Biol. , vol.238 , pp. 151-159
    • Gregoriadis, G.1
  • 7
    • 0022480556 scopus 로고
    • Antibody-mediated targeting of liposomes to red cells in vivo
    • A. Singhal, and C.M. Gupta Antibody-mediated targeting of liposomes to red cells in vivo FEBS Lett. 201 1986 321 326
    • (1986) FEBS Lett. , vol.201 , pp. 321-326
    • Singhal, A.1    Gupta, C.M.2
  • 8
    • 0023628457 scopus 로고
    • Functional drug targeting to erythrocytes in vivo using antibody bearing liposomes as drug vehicles
    • A.K. Agrawal, A. Singhal, and C.M. Gupta Functional drug targeting to erythrocytes in vivo using antibody bearing liposomes as drug vehicles Biochem. Biophys. Res. Commun. 148 1987 357 361
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 357-361
    • Agrawal, A.K.1    Singhal, A.2    Gupta, C.M.3
  • 9
    • 0028835871 scopus 로고
    • Chloroquine encapsulated in malaria-infected erythrocyte-specific antibody-bearing liposomes effectively controls chloroquine-resistant Plasmodium berghei infections in mice
    • M. Owais, G.C. Varshney, A. Choudhury, S. Chandra, and C.M. Gupta Chloroquine encapsulated in malaria-infected erythrocyte-specific antibody-bearing liposomes effectively controls chloroquine-resistant Plasmodium berghei infections in mice Antimicrob. Agents Chemother. 39 1995 180 184
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 180-184
    • Owais, M.1    Varshney, G.C.2    Choudhury, A.3    Chandra, S.4    Gupta, C.M.5
  • 10
    • 79956155445 scopus 로고    scopus 로고
    • A nanovector with complete discrimination for targeted delivery to Plasmodium falciparum-infected versus non-infected red blood cells in vitro
    • P. Urbán, J. Estelrich, A. Cortés, and X. Fernàndez-Busquets A nanovector with complete discrimination for targeted delivery to Plasmodium falciparum-infected versus non-infected red blood cells in vitro J. Control. Release 151 2011 202 211
    • (2011) J. Control. Release , vol.151 , pp. 202-211
    • Urbán, P.1    Estelrich, J.2    Cortés, A.3    Fernàndez-Busquets, X.4
  • 12
  • 13
    • 84860846235 scopus 로고    scopus 로고
    • Development of humanized mouse models to study human malaria parasite infection
    • A.M. Vaughan, S.H. Kappe, A. Ploss, and S.A. Mikolajczak Development of humanized mouse models to study human malaria parasite infection Future Microbiol. 7 2012 657 665
    • (2012) Future Microbiol. , vol.7 , pp. 657-665
    • Vaughan, A.M.1    Kappe, S.H.2    Ploss, A.3    Mikolajczak, S.A.4
  • 14
    • 0030045955 scopus 로고    scopus 로고
    • Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness
    • S. Paula, A.G. Volkov, A.N. Van Hoek, T.H. Haines, and D.W. Deamer Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness Biophys. J. 70 1996 339 348
    • (1996) Biophys. J. , vol.70 , pp. 339-348
    • Paula, S.1    Volkov, A.G.2    Van Hoek, A.N.3    Haines, T.H.4    Deamer, D.W.5
  • 15
    • 0034780523 scopus 로고    scopus 로고
    • Antigenic variation at the infected red cell surface in malaria
    • S. Kyes, P. Horrocks, and C. Newbold Antigenic variation at the infected red cell surface in malaria Annu. Rev. Microbiol. 55 2001 673 707
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 673-707
    • Kyes, S.1    Horrocks, P.2    Newbold, C.3
  • 16
    • 7444236944 scopus 로고    scopus 로고
    • Protein trafficking in Plasmodium falciparum-infected red blood cells
    • B.M. Cooke, K. Lingelbach, L.H. Bannister, and L. Tilley Protein trafficking in Plasmodium falciparum-infected red blood cells Trends Parasitol. 20 2004 581 589
    • (2004) Trends Parasitol. , vol.20 , pp. 581-589
    • Cooke, B.M.1    Lingelbach, K.2    Bannister, L.H.3    Tilley, L.4
  • 17
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • K. Kirk Membrane transport in the malaria-infected erythrocyte Physiol. Rev. 81 2001 495 537
    • (2001) Physiol. Rev. , vol.81 , pp. 495-537
    • Kirk, K.1
  • 18
    • 14744297207 scopus 로고    scopus 로고
    • Tension-induced fusion of bilayer membranes and vesicles
    • J.C. Shillcock, and R. Lipowsky Tension-induced fusion of bilayer membranes and vesicles Nat. Mater. 4 2005 225 228
    • (2005) Nat. Mater. , vol.4 , pp. 225-228
    • Shillcock, J.C.1    Lipowsky, R.2
  • 21
    • 0034607285 scopus 로고    scopus 로고
    • Formulation and characterisation of primaquine loaded liposomes prepared by a pH gradient using experimental design
    • G. Stensrud, S. Sande, S. Kristensen, and G. Smistad Formulation and characterisation of primaquine loaded liposomes prepared by a pH gradient using experimental design Int. J. Pharm. 198 2000 213 228
    • (2000) Int. J. Pharm. , vol.198 , pp. 213-228
    • Stensrud, G.1    Sande, S.2    Kristensen, S.3    Smistad, G.4
  • 23
    • 0030198445 scopus 로고    scopus 로고
    • 3-(2-Pyridyldithio)propionic acid hydrazide as a cross-linker in the formation of liposome-antibody conjugates
    • S.M. Ansell, P.G. Tardi, and S.S. Buchkowsky 3-(2-Pyridyldithio)propionic acid hydrazide as a cross-linker in the formation of liposome-antibody conjugates Bioconjug. Chem. 7 1996 490 496
    • (1996) Bioconjug. Chem. , vol.7 , pp. 490-496
    • Ansell, S.M.1    Tardi, P.G.2    Buchkowsky, S.S.3
  • 24
    • 0033650159 scopus 로고    scopus 로고
    • Periodate oxidation of antibodies for site-selective immobilization in immunoaffinity chromatography
    • D.S. Hage Periodate oxidation of antibodies for site-selective immobilization in immunoaffinity chromatography Methods Mol. Biol. 147 2000 69 82
    • (2000) Methods Mol. Biol. , vol.147 , pp. 69-82
    • Hage, D.S.1
  • 26
    • 0018720271 scopus 로고
    • A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels
    • R.C. Switzer III, C.R. Merril, and S. Shifrin A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels Anal. Biochem. 98 1979 231 237
    • (1979) Anal. Biochem. , vol.98 , pp. 231-237
    • Switzer, R.C.1    Merril, C.R.2    Shifrin, S.3
  • 28
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • C. Lambros, and J.P. Vanderberg Synchronization of Plasmodium falciparum erythrocytic stages in culture J. Parasitol. 65 1979 418 420
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 31
    • 79952426318 scopus 로고    scopus 로고
    • Differential detergent fractionation of eukaryotic cells
    • M. Ramsby, and G. Makowski Differential detergent fractionation of eukaryotic cells Cold Spring Harbor Protocols 2011 http://dx.doi.org/10.1101/pdb.prot5592
    • (2011) Cold Spring Harbor Protocols
    • Ramsby, M.1    Makowski, G.2
  • 32
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • P.H. O'Farrell High resolution two-dimensional electrophoresis of proteins J. Biol. Chem. 250 1975 4007 4021
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 33
    • 48249090848 scopus 로고    scopus 로고
    • A murine model of falciparum-malaria by in vivo selection of competent strains in non-myelodepleted mice engrafted with human erythrocytes
    • I. Angulo-Barturen, M.B. Jiménez-Díaz, T. Mulet, J. Rullas, E. Herreros, S. Ferrer, et al. A murine model of falciparum-malaria by in vivo selection of competent strains in non-myelodepleted mice engrafted with human erythrocytes PLoS One 3 2008 e2252
    • (2008) PLoS One , vol.3 , pp. e2252
    • Angulo-Barturen, I.1    Jiménez-Díaz, M.B.2    Mulet, T.3    Rullas, J.4    Herreros, E.5    Ferrer, S.6
  • 35
    • 47949122649 scopus 로고    scopus 로고
    • Preparation and in vitro evaluation of liposomal chloroquine diphosphate loaded by a transmembrane pH-gradient method
    • L. Qiu, N. Jing, and Y. Jin Preparation and in vitro evaluation of liposomal chloroquine diphosphate loaded by a transmembrane pH-gradient method Int. J. Pharm. 361 2008 56 63
    • (2008) Int. J. Pharm. , vol.361 , pp. 56-63
    • Qiu, L.1    Jing, N.2    Jin, Y.3
  • 37
  • 38
    • 84855893015 scopus 로고    scopus 로고
    • Biowaiver monographs for immediate-release solid oral dosage forms: Primaquine phosphate
    • A. Nair, B. Abrahamsson, D.M. Barends, D.W. Groot, S. Kopp, J.E. Polli, et al. Biowaiver monographs for immediate-release solid oral dosage forms: primaquine phosphate J. Pharm. Sci. 101 2012 936 945
    • (2012) J. Pharm. Sci. , vol.101 , pp. 936-945
    • Nair, A.1    Abrahamsson, B.2    Barends, D.M.3    Groot, D.W.4    Kopp, S.5    Polli, J.E.6
  • 39
    • 77956135821 scopus 로고    scopus 로고
    • MAHRP2, an exported protein of Plasmodium falciparum, is an essential component of Maurer's cleft tethers
    • E. Pachlatko, S. Rusch, A. Müller, A. Hemphill, L. Tilley, E. Hanssen, et al. MAHRP2, an exported protein of Plasmodium falciparum, is an essential component of Maurer's cleft tethers Mol. Microbiol. 77 2010 1136 1152
    • (2010) Mol. Microbiol. , vol.77 , pp. 1136-1152
    • Pachlatko, E.1    Rusch, S.2    Müller, A.3    Hemphill, A.4    Tilley, L.5    Hanssen, E.6
  • 40
    • 0041315581 scopus 로고    scopus 로고
    • MAHRP-1, a novel Plasmodium falciparum histidine-rich protein, binds ferriprotoporphyrin IX and localizes to the Maurer's clefts
    • C. Spycher, N. Klonis, T. Spielmann, E. Kump, S. Steiger, L. Tilley, et al. MAHRP-1, a novel Plasmodium falciparum histidine-rich protein, binds ferriprotoporphyrin IX and localizes to the Maurer's clefts J. Biol. Chem. 278 2003 35373 35383
    • (2003) J. Biol. Chem. , vol.278 , pp. 35373-35383
    • Spycher, C.1    Klonis, N.2    Spielmann, T.3    Kump, E.4    Steiger, S.5    Tilley, L.6
  • 41
    • 34249055361 scopus 로고    scopus 로고
    • Illuminating Plasmodium falciparum-infected red blood cells
    • L. Tilley, G. McFadden, A. Cowman, and N. Klonis Illuminating Plasmodium falciparum-infected red blood cells Trends Parasitol. 23 2007 268 277
    • (2007) Trends Parasitol. , vol.23 , pp. 268-277
    • Tilley, L.1    McFadden, G.2    Cowman, A.3    Klonis, N.4
  • 42
    • 43449119499 scopus 로고    scopus 로고
    • The Maurer's cleft protein MAHRP1 is essential for trafficking of PfEMP1 to the surface of Plasmodium falciparum-infected erythrocytes
    • C. Spycher, M. Rug, E. Pachlatko, E. Hanssen, D. Ferguson, A.F. Cowman, et al. The Maurer's cleft protein MAHRP1 is essential for trafficking of PfEMP1 to the surface of Plasmodium falciparum-infected erythrocytes Mol. Microbiol. 68 2008 1300 1314
    • (2008) Mol. Microbiol. , vol.68 , pp. 1300-1314
    • Spycher, C.1    Rug, M.2    Pachlatko, E.3    Hanssen, E.4    Ferguson, D.5    Cowman, A.F.6
  • 43
    • 59849116166 scopus 로고    scopus 로고
    • A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
    • J. García, H. Curtidor, O.L. Gil, M. Vanegas, and M.E. Patarroyo A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane Biochem. Biophys. Res. Commun. 380 2009 122 126
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 122-126
    • García, J.1    Curtidor, H.2    Gil, O.L.3    Vanegas, M.4    Patarroyo, M.E.5
  • 44
    • 0022994181 scopus 로고
    • Secretion of a malarial histidine-rich protein (Pf HRP II) from Plasmodium falciparum-infected erythrocytes
    • R.J. Howard, S. Uni, M. Aikawa, S.B. Aley, J.H. Leech, A.M. Lew, et al. Secretion of a malarial histidine-rich protein (Pf HRP II) from Plasmodium falciparum-infected erythrocytes J. Cell. Biol. 103 1986 1269 1277
    • (1986) J. Cell. Biol. , vol.103 , pp. 1269-1277
    • Howard, R.J.1    Uni, S.2    Aikawa, M.3    Aley, S.B.4    Leech, J.H.5    Lew, A.M.6
  • 45
    • 0343949989 scopus 로고
    • Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: Nucleotide sequence and mRNA structure
    • P.D. Siebert, and M. Fukuda Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure Proc. Natl. Acad. Sci. U. S. A. 83 1986 1665 1669
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 1665-1669
    • Siebert, P.D.1    Fukuda, M.2
  • 46
    • 0034918239 scopus 로고    scopus 로고
    • Studies on protein-liposome coupling using novel thiol-reactive coupling lipids: Influence of spacer length and polarity
    • M. Fleiner, P. Benzinger, T. Fichert, and U. Massing Studies on protein-liposome coupling using novel thiol-reactive coupling lipids: influence of spacer length and polarity Bioconjug. Chem. 12 2001 470 475
    • (2001) Bioconjug. Chem. , vol.12 , pp. 470-475
    • Fleiner, M.1    Benzinger, P.2    Fichert, T.3    Massing, U.4
  • 50
    • 84908599826 scopus 로고    scopus 로고
    • Application of heparin as a dual agent with antimalarial and liposome targeting activities towards Plasmodium-infected red blood cells
    • J. Marques, E. Moles, P. Urbán, R. Prohens, M.A. Busquets, C. Sevrin, et al. Application of heparin as a dual agent with antimalarial and liposome targeting activities towards Plasmodium-infected red blood cells Nanomedicine 10 2014 1719 1728
    • (2014) Nanomedicine , vol.10 , pp. 1719-1728
    • Marques, J.1    Moles, E.2    Urbán, P.3    Prohens, R.4    Busquets, M.A.5    Sevrin, C.6
  • 53
    • 14144250911 scopus 로고    scopus 로고
    • Recent advances with liposomes as pharmaceutical carriers
    • V.P. Torchilin Recent advances with liposomes as pharmaceutical carriers Nat. Rev. Drug Discov. 4 2005 145 160
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 145-160
    • Torchilin, V.P.1
  • 54
    • 77949878932 scopus 로고    scopus 로고
    • Drug delivery by red blood cells: Vascular carriers designed by Mother Nature
    • V.R. Muzykantov Drug delivery by red blood cells: vascular carriers designed by Mother Nature Expert Opin. Drug Deliv. 7 2010 403 427
    • (2010) Expert Opin. Drug Deliv. , vol.7 , pp. 403-427
    • Muzykantov, V.R.1
  • 56
    • 48349083908 scopus 로고    scopus 로고
    • The red blood cell: Structure and function
    • F. A. Davis Company Philadelphia, PA
    • D.M. Harmening The red blood cell: structure and function Clinical Hematology and Fundamentals of Hemostasis 1996 F. A. Davis Company Philadelphia, PA 54 70
    • (1996) Clinical Hematology and Fundamentals of Hemostasis , pp. 54-70
    • Harmening, D.M.1
  • 57
    • 0031026824 scopus 로고    scopus 로고
    • Membrane fusion with cationic liposomes: Effects of target membrane lipid composition
    • A.L. Bailey, and P.R. Cullis Membrane fusion with cationic liposomes: effects of target membrane lipid composition Biochemistry 36 1997 1628 1634
    • (1997) Biochemistry , vol.36 , pp. 1628-1634
    • Bailey, A.L.1    Cullis, P.R.2
  • 58
    • 84880519949 scopus 로고    scopus 로고
    • Membrane fusion induced by small molecules and ions
    • S. Mondal Roy, and M. Sarkar Membrane fusion induced by small molecules and ions J. Lipids 2011 2011 528784
    • (2011) J. Lipids , vol.2011 , pp. 528784
    • Mondal Roy, S.1    Sarkar, M.2
  • 60
    • 84865961670 scopus 로고    scopus 로고
    • Modeling the release kinetics of poorly water-soluble drug molecules from liposomal nanocarriers
    • S. Loew, A. Fahr, and S. May Modeling the release kinetics of poorly water-soluble drug molecules from liposomal nanocarriers J. Drug Deliv. 2011 2011 376548
    • (2011) J. Drug Deliv. , vol.2011 , pp. 376548
    • Loew, S.1    Fahr, A.2    May, S.3
  • 61
    • 24644453083 scopus 로고    scopus 로고
    • Transfer of lipophilic drugs between liposomal membranes and biological interfaces: Consequences for drug delivery
    • A. Fahr, P.V. Hoogevest, S. May, N. Bergstrand, and S. Leigh Transfer of lipophilic drugs between liposomal membranes and biological interfaces: consequences for drug delivery Eur. J. Pharm. Sci. 26 2005 251 265
    • (2005) Eur. J. Pharm. Sci. , vol.26 , pp. 251-265
    • Fahr, A.1    Hoogevest, P.V.2    May, S.3    Bergstrand, N.4    Leigh, S.5
  • 62
    • 0020554441 scopus 로고
    • Plasma membrane-mediated leakage of liposomes induced by interaction with murine thymocytic leukemia cells
    • H. Kercret, J. Chiovetti, M.W. Fountain, and J.P. Segrest Plasma membrane-mediated leakage of liposomes induced by interaction with murine thymocytic leukemia cells Biochim. Biophys. Acta Biomembr. 733 1983 65 74
    • (1983) Biochim. Biophys. Acta Biomembr. , vol.733 , pp. 65-74
    • Kercret, H.1    Chiovetti, J.2    Fountain, M.W.3    Segrest, J.P.4
  • 63
    • 0017830215 scopus 로고
    • Disintegration of phosphatidylcholine liposomes in plasma as a result of interaction with high-density lipoproteins
    • G. Scherphof, F. Roerdink, M. Waite, and J. Parks Disintegration of phosphatidylcholine liposomes in plasma as a result of interaction with high-density lipoproteins Biochim. Biophys. Acta Gen. Subj. 542 1978 296 307
    • (1978) Biochim. Biophys. Acta Gen. Subj. , vol.542 , pp. 296-307
    • Scherphof, G.1    Roerdink, F.2    Waite, M.3    Parks, J.4
  • 64
    • 0032574726 scopus 로고    scopus 로고
    • Phospholipid composition of the mammalian red cell membrane can be rationalized by a superlattice model
    • J.A. Virtanen, K.H. Cheng, and P. Somerharju Phospholipid composition of the mammalian red cell membrane can be rationalized by a superlattice model Proc. Natl. Acad. Sci. U. S. A. 95 1998 4964 4969
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4964-4969
    • Virtanen, J.A.1    Cheng, K.H.2    Somerharju, P.3


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