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Volumn 39, Issue 1, 2014, Pages 8-16

Cell-penetrating peptides mediated protein cross-membrane delivery and its use in bacterial vector vaccine

Author keywords

Antigen delivery; Bacterial vector vaccine; Cell penetrating peptides; Edwardsiella tarda

Indexed keywords

BACTERIAL ANTIGEN; BACTERIAL VACCINE; CELL PENETRATING PEPTIDE; ESCHERICHIA COLI PROTEIN; LYSIS PROTEIN, E COLI; RECOMBINANT VACCINE;

EID: 84899937970     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2014.04.003     Document Type: Article
Times cited : (19)

References (52)
  • 1
    • 84875950308 scopus 로고    scopus 로고
    • Utilizing Salmonella for antigen delivery.the aims and benefits of bacterial delivered vaccination
    • Kong W., Clark-Curtiss J., Curtiss I.R. Utilizing Salmonella for antigen delivery.the aims and benefits of bacterial delivered vaccination. Expert Rev Vaccines 2013, 12(4):345-347.
    • (2013) Expert Rev Vaccines , vol.12 , Issue.4 , pp. 345-347
    • Kong, W.1    Clark-Curtiss, J.2    Curtiss, I.R.3
  • 3
    • 31544455254 scopus 로고    scopus 로고
    • Rational design of Salmonella-based vaccination strategies
    • Spreng S., Dietrich G., Weidinger G. Rational design of Salmonella-based vaccination strategies. Methods 2006, 38(2):133-143.
    • (2006) Methods , vol.38 , Issue.2 , pp. 133-143
    • Spreng, S.1    Dietrich, G.2    Weidinger, G.3
  • 4
    • 0035422682 scopus 로고    scopus 로고
    • Can a 'flawless' live vector vaccine strain be engineered?
    • Galen J., Levine M. Can a 'flawless' live vector vaccine strain be engineered?. Trends Microbiol 2001, 9(8):372-376.
    • (2001) Trends Microbiol , vol.9 , Issue.8 , pp. 372-376
    • Galen, J.1    Levine, M.2
  • 5
    • 79959391563 scopus 로고    scopus 로고
    • Iron-regulated lysis of recombinant Escherichia coli in host releases protective antigen and confers biological containment
    • Guan L., Mu W., Champeimont J., Wang Q., Wu H., Xiao J., et al. Iron-regulated lysis of recombinant Escherichia coli in host releases protective antigen and confers biological containment. Infect Immun 2011, 79(7):2608-2618.
    • (2011) Infect Immun , vol.79 , Issue.7 , pp. 2608-2618
    • Guan, L.1    Mu, W.2    Champeimont, J.3    Wang, Q.4    Wu, H.5    Xiao, J.6
  • 7
    • 13844256697 scopus 로고    scopus 로고
    • Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer
    • Wadia J.S., Dowdy S.F. Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer. Adv Drug Deliv Rev 2005, 57(4):579-596.
    • (2005) Adv Drug Deliv Rev , vol.57 , Issue.4 , pp. 579-596
    • Wadia, J.S.1    Dowdy, S.F.2
  • 8
    • 38349174536 scopus 로고    scopus 로고
    • On the biomedical promise of cell penetrating peptides.limits versus prospects
    • Foerg C., Merkle H.P. On the biomedical promise of cell penetrating peptides.limits versus prospects. JPharm Sci 2008, 97(1):144-162.
    • (2008) JPharm Sci , vol.97 , Issue.1 , pp. 144-162
    • Foerg, C.1    Merkle, H.P.2
  • 9
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cell-penetrating peptides for medical and biological applications
    • Fonseca S.B., Pereira M.P., Kelley S.O. Recent advances in the use of cell-penetrating peptides for medical and biological applications. Adv Drug Deliv Rev 2009, 61(11):953-964.
    • (2009) Adv Drug Deliv Rev , vol.61 , Issue.11 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 10
    • 77958153239 scopus 로고    scopus 로고
    • Invivo biodistribution and efficacy of peptide mediated delivery
    • Järver P., Mäger I., Langel Ü. Invivo biodistribution and efficacy of peptide mediated delivery. Trends Pharmacol Sci 2010, 31(11):528-535.
    • (2010) Trends Pharmacol Sci , vol.31 , Issue.11 , pp. 528-535
    • Järver, P.1    Mäger, I.2    Langel, Ü.3
  • 11
    • 77958151183 scopus 로고    scopus 로고
    • Amembrane penetrating multiple antigen peptide (MAP) incorporating ovalbumin CD8 epitope induces potent immune responses in mice
    • Brooks N.A., Pouniotis D.S., Sheng K.C., Apostolopoulos V., Pietersz G.A. Amembrane penetrating multiple antigen peptide (MAP) incorporating ovalbumin CD8 epitope induces potent immune responses in mice. Biochim Biophys Acta 2010, 1798(12):2286-2295.
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.12 , pp. 2286-2295
    • Brooks, N.A.1    Pouniotis, D.S.2    Sheng, K.C.3    Apostolopoulos, V.4    Pietersz, G.A.5
  • 12
    • 0036498564 scopus 로고    scopus 로고
    • Dendritic cells transduced with protein antigens induce cytotoxic lymphocytes and elicit antitumor immunity
    • Shibagaki N., Udey M.C. Dendritic cells transduced with protein antigens induce cytotoxic lymphocytes and elicit antitumor immunity. JImmunol 2002, 168(5):2393-2401.
    • (2002) JImmunol , vol.168 , Issue.5 , pp. 2393-2401
    • Shibagaki, N.1    Udey, M.C.2
  • 14
    • 33645069928 scopus 로고    scopus 로고
    • Delivery of tumor associated antigens to antigen presenting cells using penetratin induces potent immune responses
    • Apostolopoulos V., Pouniotis D.S., van Maanen P.J., Andriessen R.W., Lodding J., Xing P.X., et al. Delivery of tumor associated antigens to antigen presenting cells using penetratin induces potent immune responses. Vaccine 2006, 24(16):3191-3202.
    • (2006) Vaccine , vol.24 , Issue.16 , pp. 3191-3202
    • Apostolopoulos, V.1    Pouniotis, D.S.2    van Maanen, P.J.3    Andriessen, R.W.4    Lodding, J.5    Xing, P.X.6
  • 15
    • 0142135117 scopus 로고    scopus 로고
    • Waterborne iron acquisition by a freshwater teleost fish, zebrafish Danio rerio
    • Bury N.R., Grosell M. Waterborne iron acquisition by a freshwater teleost fish, zebrafish Danio rerio. JExp Biol 2003, 206:3529-3535.
    • (2003) JExp Biol , vol.206 , pp. 3529-3535
    • Bury, N.R.1    Grosell, M.2
  • 16
    • 0027263277 scopus 로고
    • Iron acquisition in microbial pathogenesis
    • Payne S.M. Iron acquisition in microbial pathogenesis. Trends Microbiol 1993, 1:66-69.
    • (1993) Trends Microbiol , vol.1 , pp. 66-69
    • Payne, S.M.1
  • 17
    • 0028327173 scopus 로고
    • Fur regulon in gram-negative bacteria.identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay
    • Stojiljkovic I., Baumler A.J., Hantke K. Fur regulon in gram-negative bacteria.identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay. JMol Biol 1994, 236:531-545.
    • (1994) JMol Biol , vol.236 , pp. 531-545
    • Stojiljkovic, I.1    Baumler, A.J.2    Hantke, K.3
  • 18
    • 43949176579 scopus 로고
    • Pathogenesis of Gram-negative bacterial infections in warmwater fish
    • Thune R.L., Stanley L.A., Cooper R.K. Pathogenesis of Gram-negative bacterial infections in warmwater fish. Annu Rev Fish Dis 1993, 3:37-68.
    • (1993) Annu Rev Fish Dis , vol.3 , pp. 37-68
    • Thune, R.L.1    Stanley, L.A.2    Cooper, R.K.3
  • 20
    • 84861182116 scopus 로고    scopus 로고
    • Edwardsiella tarda flagellar protein FlgD.a protective immunogen against edwardsiellosis
    • Zhang M., Wu H., Li X., Yang M., Chen T., Wang Q., et al. Edwardsiella tarda flagellar protein FlgD.a protective immunogen against edwardsiellosis. Vaccine 2012, 30(26):3849-3856.
    • (2012) Vaccine , vol.30 , Issue.26 , pp. 3849-3856
    • Zhang, M.1    Wu, H.2    Li, X.3    Yang, M.4    Chen, T.5    Wang, Q.6
  • 21
    • 0030904245 scopus 로고    scopus 로고
    • Atruncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vivés E., Brodin P., Lebleu B. Atruncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. JBiol Chem 1997, 272(25):16010-16017.
    • (1997) JBiol Chem , vol.272 , Issue.25 , pp. 16010-16017
    • Vivés, E.1    Brodin, P.2    Lebleu, B.3
  • 22
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D., Joliot A.H., Chassaing G., Prochiantz A. The third helix of the Antennapedia homeodomain translocates through biological membranes. JBiol Chem 1994, 269(14):10444-10450.
    • (1994) JBiol Chem , vol.269 , Issue.14 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 23
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott G., O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 1997, 88(2):223-233.
    • (1997) Cell , vol.88 , Issue.2 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 24
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
    • Elmquist A., Lindgren M., Bartfai T., Langel Ü. VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions. Exp Cell Res 2001, 269(2):237-244.
    • (2001) Exp Cell Res , vol.269 , Issue.2 , pp. 237-244
    • Elmquist, A.1    Lindgren, M.2    Bartfai, T.3    Langel, Ü.4
  • 25
    • 24644512176 scopus 로고    scopus 로고
    • Nontoxic membrane translocation peptide from protamine, low molecular weight protamine (LMWP), for enhanced intracellular protein delivery.invitro and invivo study
    • Park Y.J., Chang L.C., Liang J.F., Moon C., Chung C.P., Yang V.C. Nontoxic membrane translocation peptide from protamine, low molecular weight protamine (LMWP), for enhanced intracellular protein delivery.invitro and invivo study. FASEB J 2005, 19:1555-1557.
    • (2005) FASEB J , vol.19 , pp. 1555-1557
    • Park, Y.J.1    Chang, L.C.2    Liang, J.F.3    Moon, C.4    Chung, C.P.5    Yang, V.C.6
  • 26
    • 0032564315 scopus 로고    scopus 로고
    • Translocation of human calcitonin in respiratory nasal epithelium is associated with self-assembly in lipid membrane
    • Schmidt M.C., Rothen-Rutishauser B., Rist B., Beck-Sickinger A., Wunderli-Allenspach H., Rubas W. Translocation of human calcitonin in respiratory nasal epithelium is associated with self-assembly in lipid membrane. Biochemistry 1998, 37(47):16582-16590.
    • (1998) Biochemistry , vol.37 , Issue.47 , pp. 16582-16590
    • Schmidt, M.C.1    Rothen-Rutishauser, B.2    Rist, B.3    Beck-Sickinger, A.4    Wunderli-Allenspach, H.5    Rubas, W.6
  • 27
    • 0035204427 scopus 로고    scopus 로고
    • Apeptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris M.C., Depollier J., Mery J., Heitz F., Divita G. Apeptide carrier for the delivery of biologically active proteins into mammalian cells. Nat Biotechnol 2001, 19(12):1173-1176.
    • (2001) Nat Biotechnol , vol.19 , Issue.12 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 28
    • 0030804766 scopus 로고    scopus 로고
    • Anew peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris M.C., Vidal P., Chaloin L., Heitz F., Divita G. Anew peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res 1997, 25(14):2730-2736.
    • (1997) Nucleic Acids Res , vol.25 , Issue.14 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, L.3    Heitz, F.4    Divita, G.5
  • 29
    • 0030890748 scopus 로고    scopus 로고
    • Design, synthesis and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers
    • Wyman T.B., Nicol F., Zelphati O., Scaria P.V., Plank C., Szoka F.C. Design, synthesis and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers. Biochemistry 1997, 36(10):3008-3017.
    • (1997) Biochemistry , vol.36 , Issue.10 , pp. 3008-3017
    • Wyman, T.B.1    Nicol, F.2    Zelphati, O.3    Scaria, P.V.4    Plank, C.5    Szoka, F.C.6
  • 30
    • 77958153489 scopus 로고    scopus 로고
    • Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery
    • Yu H.H., Nakase I., Pujals S., Hirose H., Tanaka G., Katayama S., et al. Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery. Biochim Biophys Acta 2010, 1798(12):2249-2257.
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.12 , pp. 2249-2257
    • Yu, H.H.1    Nakase, I.2    Pujals, S.3    Hirose, H.4    Tanaka, G.5    Katayama, S.6
  • 31
    • 0030589158 scopus 로고    scopus 로고
    • Towards membrane protein design.pH-sensitive topology of histidine-containing polypeptides
    • Bechinger B. Towards membrane protein design.pH-sensitive topology of histidine-containing polypeptides. JMol Biol 1996, 263(5):768-775.
    • (1996) JMol Biol , vol.263 , Issue.5 , pp. 768-775
    • Bechinger, B.1
  • 32
    • 14744268846 scopus 로고    scopus 로고
    • Pathogenesis and inflammatory response to Edwardsiella tarda infection in the zebra fish
    • Pressley M.E., Phelan P.R., Witten P.E., Mellon M.T., Kim C.H. Pathogenesis and inflammatory response to Edwardsiella tarda infection in the zebra fish. Dev Comp Immunol 2005, 29(6):501-513.
    • (2005) Dev Comp Immunol , vol.29 , Issue.6 , pp. 501-513
    • Pressley, M.E.1    Phelan, P.R.2    Witten, P.E.3    Mellon, M.T.4    Kim, C.H.5
  • 33
    • 84883609896 scopus 로고    scopus 로고
    • Chemically and biologically synthesized CPP-modified gelonin for enhanced anti-tumor activity
    • Shin M.C., Zhang J., David A.E., Trommer W.E., Kwon Y.M., Min K.A., et al. Chemically and biologically synthesized CPP-modified gelonin for enhanced anti-tumor activity. JControl Release 2013, 172(1):169-178.
    • (2013) JControl Release , vol.172 , Issue.1 , pp. 169-178
    • Shin, M.C.1    Zhang, J.2    David, A.E.3    Trommer, W.E.4    Kwon, Y.M.5    Min, K.A.6
  • 34
    • 6344222029 scopus 로고    scopus 로고
    • Transduction of the TAT-FLIP fusion protein results in transient resistance to Fas-induced apoptosis invivo
    • Krautwald S., Ziegler E., Tiede K., Pust R., Kunzendorf U. Transduction of the TAT-FLIP fusion protein results in transient resistance to Fas-induced apoptosis invivo. JBiol Chem 2004, 279(42):44005-44011.
    • (2004) JBiol Chem , vol.279 , Issue.42 , pp. 44005-44011
    • Krautwald, S.1    Ziegler, E.2    Tiede, K.3    Pust, R.4    Kunzendorf, U.5
  • 35
    • 80855131664 scopus 로고    scopus 로고
    • Whole protein and defined CD8(+) and CD4(+) peptides linked to penetratin targets both MHC class I and II antigen presentation pathways
    • Pouniotis D.S., Esparon S., Apostolopoulos V., Pietersz G.A. Whole protein and defined CD8(+) and CD4(+) peptides linked to penetratin targets both MHC class I and II antigen presentation pathways. Immunol Cell Biol 2011, 89(8):904-913.
    • (2011) Immunol Cell Biol , vol.89 , Issue.8 , pp. 904-913
    • Pouniotis, D.S.1    Esparon, S.2    Apostolopoulos, V.3    Pietersz, G.A.4
  • 36
    • 79959365312 scopus 로고    scopus 로고
    • Mechanisms of cellular uptake of cell-penetrating peptides
    • Madani F., Lindberg S., Langel U., Futaki S., Gräslund A. Mechanisms of cellular uptake of cell-penetrating peptides. JBiophys 2011, 2011:414729.
    • (2011) JBiophys , vol.2011 , pp. 414729
    • Madani, F.1    Lindberg, S.2    Langel, U.3    Futaki, S.4    Gräslund, A.5
  • 37
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia J.S., Stan R.V., Dowdy S.F. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 2004, 10(3):310-315.
    • (2004) Nat Med , vol.10 , Issue.3 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 38
    • 79952009756 scopus 로고    scopus 로고
    • Intracellular delivery of quantum dots mediated by a histidine- and arginine-rich HR9 cell-penetrating peptide through the direct membrane translocation mechanism
    • Liu B.R., Huang Y.W., Winiarz J.G., Chiang H.J., Lee H.J. Intracellular delivery of quantum dots mediated by a histidine- and arginine-rich HR9 cell-penetrating peptide through the direct membrane translocation mechanism. Biomaterials 2011, 32(13):3520-3537.
    • (2011) Biomaterials , vol.32 , Issue.13 , pp. 3520-3537
    • Liu, B.R.1    Huang, Y.W.2    Winiarz, J.G.3    Chiang, H.J.4    Lee, H.J.5
  • 39
    • 21244446692 scopus 로고    scopus 로고
    • Tat mammaglobin fusion protein transduced dendritic cells stimulate mammaglobin-specific CD4 and CD8 T cells
    • Viehl C.T., Tanaka Y., Chen T., Frey D.M., Tran A., Fleming T.P., et al. Tat mammaglobin fusion protein transduced dendritic cells stimulate mammaglobin-specific CD4 and CD8 T cells. Breast Cancer Res Treat 2005, 91(3):271-278.
    • (2005) Breast Cancer Res Treat , vol.91 , Issue.3 , pp. 271-278
    • Viehl, C.T.1    Tanaka, Y.2    Chen, T.3    Frey, D.M.4    Tran, A.5    Fleming, T.P.6
  • 40
    • 33645070548 scopus 로고    scopus 로고
    • Penetratin tandemly linked to a CTL peptide induces anti-tumour T-cell responses via a cross-presentation pathway
    • Pouniotis D.S., Apostolopoulos V., Pietersz G.A. Penetratin tandemly linked to a CTL peptide induces anti-tumour T-cell responses via a cross-presentation pathway. Immunology 2006, 117(3):329-339.
    • (2006) Immunology , vol.117 , Issue.3 , pp. 329-339
    • Pouniotis, D.S.1    Apostolopoulos, V.2    Pietersz, G.A.3
  • 41
    • 84855360127 scopus 로고    scopus 로고
    • LAH4 enhances CD8+ T cell immunity of protein/peptide-based vaccines
    • Zhang T.T., Kang T.H., Ma B., Xu Y., Hung C.F., Wu T.C. LAH4 enhances CD8+ T cell immunity of protein/peptide-based vaccines. Vaccine 2012, 30(4):784-793.
    • (2012) Vaccine , vol.30 , Issue.4 , pp. 784-793
    • Zhang, T.T.1    Kang, T.H.2    Ma, B.3    Xu, Y.4    Hung, C.F.5    Wu, T.C.6
  • 42
    • 33746111184 scopus 로고    scopus 로고
    • Polyarginine-mediated protein delivery to dendritic cells presents antigen more efficiently onto MHC class I and class II and elicits superior antitumor immunity
    • Mitsui H., Inozume T., Kitamura R., Shibagaki N., Shimada S. Polyarginine-mediated protein delivery to dendritic cells presents antigen more efficiently onto MHC class I and class II and elicits superior antitumor immunity. JInvest Dermatol 2006, 126(8):1804-1812.
    • (2006) JInvest Dermatol , vol.126 , Issue.8 , pp. 1804-1812
    • Mitsui, H.1    Inozume, T.2    Kitamura, R.3    Shibagaki, N.4    Shimada, S.5
  • 43
    • 63949083004 scopus 로고    scopus 로고
    • AT7 RNA polymerase-dependent gene expression system for Bacillus megaterium
    • Gamer M., Fröde D., Biedendieck R., Stammen S., Jahn D. AT7 RNA polymerase-dependent gene expression system for Bacillus megaterium. Appl Microbiol Biotechnol 2009, 82(6):1195-1203.
    • (2009) Appl Microbiol Biotechnol , vol.82 , Issue.6 , pp. 1195-1203
    • Gamer, M.1    Fröde, D.2    Biedendieck, R.3    Stammen, S.4    Jahn, D.5
  • 44
    • 33646876799 scopus 로고    scopus 로고
    • Immunogenicity of Salmonella vector vaccines expressing SBR of Streptococcus mutans under the control of a T7-nirB (dual) promoter system
    • Salam M.A., Katz J., Zhang P., Hajishengallis G., Michalek S.M. Immunogenicity of Salmonella vector vaccines expressing SBR of Streptococcus mutans under the control of a T7-nirB (dual) promoter system. Vaccine 2006, 24(23):5003-5015.
    • (2006) Vaccine , vol.24 , Issue.23 , pp. 5003-5015
    • Salam, M.A.1    Katz, J.2    Zhang, P.3    Hajishengallis, G.4    Michalek, S.M.5
  • 45
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal.environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal.environmental regulation of Salmonella virulence. Cell 1996, 84(1):165-174.
    • (1996) Cell , vol.84 , Issue.1 , pp. 165-174
    • García Véscovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 46
    • 81255187782 scopus 로고    scopus 로고
    • Anovel invivo inducible expression system in Edwardsiella tarda for potential application in bacterial polyvalence vaccine
    • Mu W., Guan L., Yan Y., Liu Q., Zhang Y. Anovel invivo inducible expression system in Edwardsiella tarda for potential application in bacterial polyvalence vaccine. Fish Shellfish Immunol 2011, 31(6):1097-1105.
    • (2011) Fish Shellfish Immunol , vol.31 , Issue.6 , pp. 1097-1105
    • Mu, W.1    Guan, L.2    Yan, Y.3    Liu, Q.4    Zhang, Y.5
  • 47
    • 61349162436 scopus 로고    scopus 로고
    • Evaluation of recombinant invasive, non-pathogenic Escherichia coli as a vaccine vector against the intracellular pathogen, Brucella
    • Harms J.S., Durward M.A., Magnani D.M., Splitter G.A. Evaluation of recombinant invasive, non-pathogenic Escherichia coli as a vaccine vector against the intracellular pathogen, Brucella. JImmune Based Ther Vaccines 2009, 7:1.
    • (2009) JImmune Based Ther Vaccines , vol.7 , pp. 1
    • Harms, J.S.1    Durward, M.A.2    Magnani, D.M.3    Splitter, G.A.4
  • 49
    • 83155164600 scopus 로고    scopus 로고
    • Bacterial ghosts as carriers of protein subunit and DNA-encoded antigens for vaccine applications
    • Muhammad A., Champeimont J., Mayr U.B., Lubitz W., Kudela P. Bacterial ghosts as carriers of protein subunit and DNA-encoded antigens for vaccine applications. Expert Rev Vaccines 2012, 11(1):97-116.
    • (2012) Expert Rev Vaccines , vol.11 , Issue.1 , pp. 97-116
    • Muhammad, A.1    Champeimont, J.2    Mayr, U.B.3    Lubitz, W.4    Kudela, P.5
  • 50
    • 0037073664 scopus 로고    scopus 로고
    • Bacterial ghosts as vaccine candidates for veterinary applications
    • Jalava K., Hensel A., Szostak M., Resch S., Lubitz W. Bacterial ghosts as vaccine candidates for veterinary applications. JControl Release 2002, 85(1-3):17-25.
    • (2002) JControl Release , vol.85 , Issue.1-3 , pp. 17-25
    • Jalava, K.1    Hensel, A.2    Szostak, M.3    Resch, S.4    Lubitz, W.5
  • 52
    • 27644544112 scopus 로고    scopus 로고
    • Protection of tilapia (Oreochromis mosambicus) from edwardsiellosis by vaccination with Edwardsiella tarda ghosts
    • Kwon S.R., Nam Y.K., Kim S.K., Kim K.H. Protection of tilapia (Oreochromis mosambicus) from edwardsiellosis by vaccination with Edwardsiella tarda ghosts. Fish Shellfish Immunol 2006, 20(4):621-626.
    • (2006) Fish Shellfish Immunol , vol.20 , Issue.4 , pp. 621-626
    • Kwon, S.R.1    Nam, Y.K.2    Kim, S.K.3    Kim, K.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.