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Volumn 19, Issue 6, 2008, Pages 613-619

Antibodies for the treatment of bacterial infections: current experience and future prospects

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; MONOCLONAL ANTIBODIES;

EID: 57049154860     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2008.10.002     Document Type: Review
Times cited : (85)

References (51)
  • 1
    • 44449113837 scopus 로고    scopus 로고
    • Bactericidal action of a complement-independent antibody against relapsing fever Borrelia resides in its variable region
    • LaRocca T.J., Katona L.I., Thanassi D.G., and Benach J.L. Bactericidal action of a complement-independent antibody against relapsing fever Borrelia resides in its variable region. J Immunol 180 (2008) 6222-6228
    • (2008) J Immunol , vol.180 , pp. 6222-6228
    • LaRocca, T.J.1    Katona, L.I.2    Thanassi, D.G.3    Benach, J.L.4
  • 2
    • 0034223369 scopus 로고    scopus 로고
    • In vitro activity of monoclonal and recombinant yeast killer toxin-like antibodies against antibiotic-resistant gram-positive cocci
    • Conti S., Magliani W., Arseni S., Dieci E., Frazzi R., Salati A., Varaldo P.E., and Polonelli L. In vitro activity of monoclonal and recombinant yeast killer toxin-like antibodies against antibiotic-resistant gram-positive cocci. Mol Med 6 (2000) 613-619
    • (2000) Mol Med , vol.6 , pp. 613-619
    • Conti, S.1    Magliani, W.2    Arseni, S.3    Dieci, E.4    Frazzi, R.5    Salati, A.6    Varaldo, P.E.7    Polonelli, L.8
  • 5
    • 35148861151 scopus 로고    scopus 로고
    • Antibody for the prevention of neonatal noscocomial staphylococcal infection: a review of the literature
    • Weisman L.E. Antibody for the prevention of neonatal noscocomial staphylococcal infection: a review of the literature. Arch Pediatr 14 Suppl 1 (2007) S31-S34
    • (2007) Arch Pediatr , vol.14 , Issue.SUPPL. 1
    • Weisman, L.E.1
  • 6
    • 33747775021 scopus 로고    scopus 로고
    • Phase II randomized, double blind, placebo-controlled, safety, pharmacokinetics, pharmacodynamics, and clinical activity study in very low birth weight (VLBW) neonates of BSYX-A110, an anti-staphylococcal monoclonal antibody for the prevention of staphylococcal infection
    • (Abstract)
    • Thackray H., Lassiter H., and Walsh B. Phase II randomized, double blind, placebo-controlled, safety, pharmacokinetics, pharmacodynamics, and clinical activity study in very low birth weight (VLBW) neonates of BSYX-A110, an anti-staphylococcal monoclonal antibody for the prevention of staphylococcal infection. Pediatr Res 59 (2006) 3724 (Abstract)
    • (2006) Pediatr Res , vol.59 , pp. 3724
    • Thackray, H.1    Lassiter, H.2    Walsh, B.3
  • 8
  • 10
    • 50849133950 scopus 로고    scopus 로고
    • Good effect of IgY against Pseudomonas aeruginosa infections in cystic fibrosis patients
    • Nilsson E., Larsson A., Olesen H.V., Wejåker P.E., and Kollberg H. Good effect of IgY against Pseudomonas aeruginosa infections in cystic fibrosis patients. Pediatr Pulmonol 43 (2008) 892-899
    • (2008) Pediatr Pulmonol , vol.43 , pp. 892-899
    • Nilsson, E.1    Larsson, A.2    Olesen, H.V.3    Wejåker, P.E.4    Kollberg, H.5
  • 11
    • 0035077840 scopus 로고    scopus 로고
    • Human monoclonal antibodies against Pseudomonas aeruginosa lipopolysaccharide derived from transgenic mice containing megabase human immunoglobulin loci are opsonic and protective against fatal pseudomonas sepsis
    • Hemachandra S., Kamboj K., Copfer J., Pier G., Green L.L., and Schreiber J.R. Human monoclonal antibodies against Pseudomonas aeruginosa lipopolysaccharide derived from transgenic mice containing megabase human immunoglobulin loci are opsonic and protective against fatal pseudomonas sepsis. Infect Immun 69 (2001) 2223-2229
    • (2001) Infect Immun , vol.69 , pp. 2223-2229
    • Hemachandra, S.1    Kamboj, K.2    Copfer, J.3    Pier, G.4    Green, L.L.5    Schreiber, J.R.6
  • 12
    • 17144363627 scopus 로고    scopus 로고
    • Multi-valent human monoclonal antibody preparation against Pseudomonas aeruginosa derived from transgenic mice containing human immunoglobulin loci is protective against fatal pseudomonas sepsis caused by multiple serotypes
    • Lai Z., Kimmel R., Petersen S., Thomas S., Pier G., Bezabeh B., Luo R., and Schreiber J.R. Multi-valent human monoclonal antibody preparation against Pseudomonas aeruginosa derived from transgenic mice containing human immunoglobulin loci is protective against fatal pseudomonas sepsis caused by multiple serotypes. Vaccine 23 (2005) 3264-3271
    • (2005) Vaccine , vol.23 , pp. 3264-3271
    • Lai, Z.1    Kimmel, R.2    Petersen, S.3    Thomas, S.4    Pier, G.5    Bezabeh, B.6    Luo, R.7    Schreiber, J.R.8
  • 13
    • 0028984469 scopus 로고
    • Biologic activities of antibodies to the neutral-polysaccharide component of the Pseudomonas aeruginosa lipopolysaccharide are blocked by O side chains and mucoid exopolysaccharide (alginate)
    • Hatano K., Goldberg J.B., and Pier G.B. Biologic activities of antibodies to the neutral-polysaccharide component of the Pseudomonas aeruginosa lipopolysaccharide are blocked by O side chains and mucoid exopolysaccharide (alginate). Infect Immun 63 (1995) 21-26
    • (1995) Infect Immun , vol.63 , pp. 21-26
    • Hatano, K.1    Goldberg, J.B.2    Pier, G.B.3
  • 14
    • 0025611267 scopus 로고
    • Generation and characterization of murine antiflagellum monoclonal antibodies that are protective against lethal challenge with Pseudomonas aeruginosa
    • Rosok M.J., Stebbins M.R., Connelly K., Lostrom M.E., and Siadak A.W. Generation and characterization of murine antiflagellum monoclonal antibodies that are protective against lethal challenge with Pseudomonas aeruginosa. Infect Immun 58 (1990) 3819-3828
    • (1990) Infect Immun , vol.58 , pp. 3819-3828
    • Rosok, M.J.1    Stebbins, M.R.2    Connelly, K.3    Lostrom, M.E.4    Siadak, A.W.5
  • 15
    • 0029112591 scopus 로고
    • Mucoid Pseudomonas aeruginosa growing in a biofilm in vitro are killed by opsonic antibodies to the mucoid exopolysaccharide capsule but not by antibodies produced during chronic lung infection in cystic fibrosis patients
    • Meluleni G.J., Grout M., Evans D.J., and Pier G.B. Mucoid Pseudomonas aeruginosa growing in a biofilm in vitro are killed by opsonic antibodies to the mucoid exopolysaccharide capsule but not by antibodies produced during chronic lung infection in cystic fibrosis patients. J Immunol 155 (1995) 2029-2038
    • (1995) J Immunol , vol.155 , pp. 2029-2038
    • Meluleni, G.J.1    Grout, M.2    Evans, D.J.3    Pier, G.B.4
  • 16
    • 34548471954 scopus 로고    scopus 로고
    • Capsular polysaccharide masks clumping factor A-mediated adherence of Staphylococcus aureus to fibrinogen and platelets
    • Risley A.L., Loughman A., Cywes-Bentley C., Foster T.J., and Lee J.C. Capsular polysaccharide masks clumping factor A-mediated adherence of Staphylococcus aureus to fibrinogen and platelets. J Infect Dis 196 (2007) 919-927
    • (2007) J Infect Dis , vol.196 , pp. 919-927
    • Risley, A.L.1    Loughman, A.2    Cywes-Bentley, C.3    Foster, T.J.4    Lee, J.C.5
  • 18
    • 38349048514 scopus 로고    scopus 로고
    • Complement evasion by human pathogens
    • A review of the multiple mechanisms used by bacteria to interfere with complement activation.
    • Lambris J.D., Ricklin D., and Geisbrecht B.V. Complement evasion by human pathogens. Nat Rev Microbiol 6 (2008) 132-142. A review of the multiple mechanisms used by bacteria to interfere with complement activation.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 132-142
    • Lambris, J.D.1    Ricklin, D.2    Geisbrecht, B.V.3
  • 20
    • 0021239746 scopus 로고
    • Proteins of the cystic fibrosis respiratory tract. Fragmented immunoglobulin G opsonic antibody causing defective opsonophagocytosis
    • Fick Jr. R.B., Naegel G.P., Squier S.U., Wood R.E., Gee J.B., and Reynolds H.Y. Proteins of the cystic fibrosis respiratory tract. Fragmented immunoglobulin G opsonic antibody causing defective opsonophagocytosis. J Clin Invest 74 (1984) 236-248
    • (1984) J Clin Invest , vol.74 , pp. 236-248
    • Fick Jr., R.B.1    Naegel, G.P.2    Squier, S.U.3    Wood, R.E.4    Gee, J.B.5    Reynolds, H.Y.6
  • 21
    • 0021912870 scopus 로고
    • IgG proteolytic activity of Pseudomonas aeruginosa in cystic fibrosis
    • Fick Jr. R.B., Baltimore R.S., Squier S.U., and Reynolds H.Y. IgG proteolytic activity of Pseudomonas aeruginosa in cystic fibrosis. J Infect Dis 151 (1985) 589-598
    • (1985) J Infect Dis , vol.151 , pp. 589-598
    • Fick Jr., R.B.1    Baltimore, R.S.2    Squier, S.U.3    Reynolds, H.Y.4
  • 22
    • 0032479154 scopus 로고    scopus 로고
    • Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa
    • Engel L.S., Hill J.M., Caballero A.R., Green L.C., and O'Callaghan R.J. Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa. J Biol Chem 273 (1998) 16792-16797
    • (1998) J Biol Chem , vol.273 , pp. 16792-16797
    • Engel, L.S.1    Hill, J.M.2    Caballero, A.R.3    Green, L.C.4    O'Callaghan, R.J.5
  • 24
    • 0033008431 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa secretory product pyocyanin inactivates alpha1 protease inhibitor: implications for the pathogenesis of cystic fibrosis lung disease
    • Britigan B.E., Railsback M.A., and Cox C.D. The Pseudomonas aeruginosa secretory product pyocyanin inactivates alpha1 protease inhibitor: implications for the pathogenesis of cystic fibrosis lung disease. Infect Immun 67 (1999) 1207-1212
    • (1999) Infect Immun , vol.67 , pp. 1207-1212
    • Britigan, B.E.1    Railsback, M.A.2    Cox, C.D.3
  • 25
    • 0036070620 scopus 로고    scopus 로고
    • Variation in extracellular protease production among clinical isolates of Staphylococcus aureus due to different levels of expression of the protease repressor sarA
    • Karlsson A., and Arvidson S. Variation in extracellular protease production among clinical isolates of Staphylococcus aureus due to different levels of expression of the protease repressor sarA. Infect Immun 70 (2002) 4239-4246
    • (2002) Infect Immun , vol.70 , pp. 4239-4246
    • Karlsson, A.1    Arvidson, S.2
  • 28
    • 33746649058 scopus 로고    scopus 로고
    • Comparative antibody-mediated phagocytosis of Staphylococcus epidermidis cells grown in a biofilm or in the planktonic state
    • Cerca N., Jefferson K.K., Oliveira R., Pier G.B., and Azeredo J. Comparative antibody-mediated phagocytosis of Staphylococcus epidermidis cells grown in a biofilm or in the planktonic state. Infect Immun 74 (2006) 4849-4855
    • (2006) Infect Immun , vol.74 , pp. 4849-4855
    • Cerca, N.1    Jefferson, K.K.2    Oliveira, R.3    Pier, G.B.4    Azeredo, J.5
  • 29
    • 34447249875 scopus 로고    scopus 로고
    • Molecular basis for preferential protective efficacy of antibodies directed to the poorly acetylated form of staphylococcal poly-N-acetyl-beta-(1-6)-glucosamine
    • Cerca N., Jefferson K.K., Maira-Litrán T., Pier D.B., Kelly-Quintos C., Goldmann D.A., Azeredo J., and Pier G.B. Molecular basis for preferential protective efficacy of antibodies directed to the poorly acetylated form of staphylococcal poly-N-acetyl-beta-(1-6)-glucosamine. Infect Immun 75 (2007) 3406-3413
    • (2007) Infect Immun , vol.75 , pp. 3406-3413
    • Cerca, N.1    Jefferson, K.K.2    Maira-Litrán, T.3    Pier, D.B.4    Kelly-Quintos, C.5    Goldmann, D.A.6    Azeredo, J.7    Pier, G.B.8
  • 31
    • 4644328672 scopus 로고    scopus 로고
    • Quorum sensing and bacterial cross-talk in biotechnology
    • March J.C., and Bentley W.E. Quorum sensing and bacterial cross-talk in biotechnology. Curr Opin Biotechnol 15 (2004) 495-502
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 495-502
    • March, J.C.1    Bentley, W.E.2
  • 34
    • 40849114311 scopus 로고    scopus 로고
    • The quorum quenching antibody RS2-1G9 protects macrophages from the cytotoxic effects of the Pseudomonas aeruginosa quorum sensing signalling molecule N-3-oxo-dodecanoyl-homoserine lactone
    • Kaufmann G.F., Park J., Mee J.M., Ulevitch R.J., and Janda K.D. The quorum quenching antibody RS2-1G9 protects macrophages from the cytotoxic effects of the Pseudomonas aeruginosa quorum sensing signalling molecule N-3-oxo-dodecanoyl-homoserine lactone. Mol Immunol 45 (2008) 2710-2714
    • (2008) Mol Immunol , vol.45 , pp. 2710-2714
    • Kaufmann, G.F.1    Park, J.2    Mee, J.M.3    Ulevitch, R.J.4    Janda, K.D.5
  • 36
    • 57049148080 scopus 로고    scopus 로고
    • Babin M, Ou Y, Roschke V, Yu A, Subramanian M, Choi G: Protection against inhalation anthrax-induced lethality by a human monoclonal antibody to protective antigen in rabbits and cynomolgus monkeys. In 43rd Interscience Conference on Antimicrobial Agents and Chemotherapy 2003, (Abstract # 3836).
    • Babin M, Ou Y, Roschke V, Yu A, Subramanian M, Choi G: Protection against inhalation anthrax-induced lethality by a human monoclonal antibody to protective antigen in rabbits and cynomolgus monkeys. In 43rd Interscience Conference on Antimicrobial Agents and Chemotherapy 2003, (Abstract # 3836).
  • 38
    • 19944432972 scopus 로고    scopus 로고
    • A high-affinity monoclonal antibody to anthrax protective antigen passively protects rabbits before and after aerosolized Bacillus anthracis spore challenge
    • Mohamed N., Clagett M., Li J., Jones S., Pincus S., D'Alia G., Nardone L., Babin M., Spitalny G., and Casey L. A high-affinity monoclonal antibody to anthrax protective antigen passively protects rabbits before and after aerosolized Bacillus anthracis spore challenge. Infect Immun 73 (2005) 795-802
    • (2005) Infect Immun , vol.73 , pp. 795-802
    • Mohamed, N.1    Clagett, M.2    Li, J.3    Jones, S.4    Pincus, S.5    D'Alia, G.6    Nardone, L.7    Babin, M.8    Spitalny, G.9    Casey, L.10
  • 39
  • 42
    • 0346814070 scopus 로고    scopus 로고
    • The Type III secretion system of Gram-negative bacteria: a potential therapeutic target?
    • This review provides a detailed description of the needle-like type III secretion systems used for the injection of exotoxins by many Gram-negative bacteria.
    • Müller S., Feldman M.F., and Cornelis G.R. The Type III secretion system of Gram-negative bacteria: a potential therapeutic target?. Expert Opin Ther Targets 5 (2001) 327-339. This review provides a detailed description of the needle-like type III secretion systems used for the injection of exotoxins by many Gram-negative bacteria.
    • (2001) Expert Opin Ther Targets , vol.5 , pp. 327-339
    • Müller, S.1    Feldman, M.F.2    Cornelis, G.R.3
  • 43
    • 0034769748 scopus 로고    scopus 로고
    • Prevalence of type III secretion genes in clinical and environmental isolates of Pseudomonas aeruginosa
    • Feltman H., Schulert G., Khan S., Jain M., Peterson L., and Hauser A.R. Prevalence of type III secretion genes in clinical and environmental isolates of Pseudomonas aeruginosa. Microbiology 147 (2001) 2659-2669
    • (2001) Microbiology , vol.147 , pp. 2659-2669
    • Feltman, H.1    Schulert, G.2    Khan, S.3    Jain, M.4    Peterson, L.5    Hauser, A.R.6
  • 44
    • 0036191393 scopus 로고    scopus 로고
    • Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa
    • Hauser A.R., Cobb E., Bodi M., Mariscal D., Vallés J., Engel J.N., and Rello J. Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa. Crit Care Med 30 (2002) 521-528
    • (2002) Crit Care Med , vol.30 , pp. 521-528
    • Hauser, A.R.1    Cobb, E.2    Bodi, M.3    Mariscal, D.4    Vallés, J.5    Engel, J.N.6    Rello, J.7
  • 47
    • 0034103142 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa cystic fibrosis isolates induce rapid, type III secretion-dependent, but ExoU-independent, oncosis of macrophages and polymorphonuclear neutrophils
    • Dacheux D., Toussaint B., Richard M., Brochier G., Croize J., and Attree I. Pseudomonas aeruginosa cystic fibrosis isolates induce rapid, type III secretion-dependent, but ExoU-independent, oncosis of macrophages and polymorphonuclear neutrophils. Infect Immun 68 (2000) 2916-2924
    • (2000) Infect Immun , vol.68 , pp. 2916-2924
    • Dacheux, D.1    Toussaint, B.2    Richard, M.3    Brochier, G.4    Croize, J.5    Attree, I.6
  • 50
    • 0026692957 scopus 로고
    • What went wrong with Centoxin?
    • This brief review describes some of the potential pitfalls of antibody development in the field of infectious disease.
    • Edgington S. What went wrong with Centoxin?. Biotechnology 10 (1992) 617. This brief review describes some of the potential pitfalls of antibody development in the field of infectious disease.
    • (1992) Biotechnology , vol.10 , pp. 617
    • Edgington, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.