메뉴 건너뛰기




Volumn 15, Issue 2, 2007, Pages 63-69

Secreted bacterial phospholipase A2 enzymes: better living through phospholipolysis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; PHOSPHOLIPASE A2; PROTEIN EXOU; PROTEIN SLAA; UNCLASSIFIED DRUG;

EID: 33846688692     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2006.12.003     Document Type: Article
Times cited : (90)

References (64)
  • 1
    • 0042665762 scopus 로고    scopus 로고
    • 2 as multivalent mediators of inflammatory and allergic disorders
    • 2 as multivalent mediators of inflammatory and allergic disorders. Int. Arch. Allergy Immunol. 131 (2003) 153-163
    • (2003) Int. Arch. Allergy Immunol. , vol.131 , pp. 153-163
    • Granata, F.1
  • 2
    • 33645243918 scopus 로고    scopus 로고
    • Phospholipase and proteinase activities of clinical isolates of Candida from immunocompromised patients
    • Kumar C.P., et al. Phospholipase and proteinase activities of clinical isolates of Candida from immunocompromised patients. Mycopathologia 161 (2006) 213-218
    • (2006) Mycopathologia , vol.161 , pp. 213-218
    • Kumar, C.P.1
  • 3
    • 0035179848 scopus 로고    scopus 로고
    • Extracellular phospholipase activity is a virulence factor for Cryptococcus neoformans
    • Cox G.M., et al. Extracellular phospholipase activity is a virulence factor for Cryptococcus neoformans. Mol. Microbiol. 39 (2001) 166-175
    • (2001) Mol. Microbiol. , vol.39 , pp. 166-175
    • Cox, G.M.1
  • 4
    • 33646148472 scopus 로고    scopus 로고
    • Phospholipase B activity enhances adhesion of Cryptococcus neoformans to a human lung epithelial cell line
    • Ganendren R., et al. Phospholipase B activity enhances adhesion of Cryptococcus neoformans to a human lung epithelial cell line. Microbes Infect. 8 (2006) 1006-1015
    • (2006) Microbes Infect. , vol.8 , pp. 1006-1015
    • Ganendren, R.1
  • 5
    • 14844334897 scopus 로고    scopus 로고
    • A surface phospholipase is involved in the migration of plasmodium sporozoites through cells
    • Bhanot P., et al. A surface phospholipase is involved in the migration of plasmodium sporozoites through cells. J. Biol. Chem. 280 (2005) 6752-6760
    • (2005) J. Biol. Chem. , vol.280 , pp. 6752-6760
    • Bhanot, P.1
  • 6
    • 1342281416 scopus 로고    scopus 로고
    • 2-like lytic factor of Trichomonas vaginalis
    • 2-like lytic factor of Trichomonas vaginalis. Infect. Immun. 72 (2004) 1284-1290
    • (2004) Infect. Immun. , vol.72 , pp. 1284-1290
    • Lubick, K.J.1    Burgess, D.E.2
  • 7
    • 14944352775 scopus 로고    scopus 로고
    • Clostridium perfringens α-toxin: characterization and mode of action
    • Sakurai J., et al. Clostridium perfringens α-toxin: characterization and mode of action. J. Biochem. (Tokyo) 136 (2004) 569-574
    • (2004) J. Biochem. (Tokyo) , vol.136 , pp. 569-574
    • Sakurai, J.1
  • 8
    • 0020452225 scopus 로고
    • Phospholipase C (heat-labile hemolysin) of Pseudomonas aeruginosa: purification and preliminary characterization
    • Berka R.M., and Vasil M.L. Phospholipase C (heat-labile hemolysin) of Pseudomonas aeruginosa: purification and preliminary characterization. J. Bacteriol. 152 (1982) 239-245
    • (1982) J. Bacteriol. , vol.152 , pp. 239-245
    • Berka, R.M.1    Vasil, M.L.2
  • 9
    • 0020463923 scopus 로고
    • Cloning of a phosphate-regulated hemolysin gene (phospholipase C) from Pseudomonas aeruginosa
    • Vasil M.L., et al. Cloning of a phosphate-regulated hemolysin gene (phospholipase C) from Pseudomonas aeruginosa. J. Bacteriol. 152 (1982) 431-440
    • (1982) J. Bacteriol. , vol.152 , pp. 431-440
    • Vasil, M.L.1
  • 10
    • 0021838092 scopus 로고
    • Cytolytic and phospholipase C activity in Legionella species
    • Baine W.B. Cytolytic and phospholipase C activity in Legionella species. J. Gen. Microbiol. 131 (1985) 1383-1391
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1383-1391
    • Baine, W.B.1
  • 11
    • 0027231710 scopus 로고
    • Bacterial phospholipases C
    • Titball R.W. Bacterial phospholipases C. Microbiol. Rev. 57 (1993) 347-366
    • (1993) Microbiol. Rev. , vol.57 , pp. 347-366
    • Titball, R.W.1
  • 12
    • 0015237762 scopus 로고
    • A membrane-bound phospholipase A1 purified from Escherichia coli
    • Scandella C.J., and Kornberg A. A membrane-bound phospholipase A1 purified from Escherichia coli. Biochemistry 10 (1971) 4447-4456
    • (1971) Biochemistry , vol.10 , pp. 4447-4456
    • Scandella, C.J.1    Kornberg, A.2
  • 13
    • 0033951375 scopus 로고    scopus 로고
    • Outer-membrane phospholipase A: known structure, unknown biological function
    • Dekker N. Outer-membrane phospholipase A: known structure, unknown biological function. Mol. Microbiol. 35 (2000) 711-717
    • (2000) Mol. Microbiol. , vol.35 , pp. 711-717
    • Dekker, N.1
  • 14
    • 0034739438 scopus 로고    scopus 로고
    • Bacterial phospholipase A: structure and function of an integral membrane phospholipase
    • Snijder H.J., and Dijkstra B.W. Bacterial phospholipase A: structure and function of an integral membrane phospholipase. Biochim. Biophys. Acta 1488 (2000) 91-101
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 91-101
    • Snijder, H.J.1    Dijkstra, B.W.2
  • 15
    • 0035179671 scopus 로고    scopus 로고
    • Phase variation in the Helicobacter pylori phospholipase A gene and its role in acid adaptation
    • Tannaes T., et al. Phase variation in the Helicobacter pylori phospholipase A gene and its role in acid adaptation. Infect. Immun. 69 (2001) 7334-7340
    • (2001) Infect. Immun. , vol.69 , pp. 7334-7340
    • Tannaes, T.1
  • 16
    • 0033944637 scopus 로고    scopus 로고
    • Lipid profiles of Helicobacter pylori colony variants
    • Tannaes T., et al. Lipid profiles of Helicobacter pylori colony variants. APMIS 108 (2000) 349-356
    • (2000) APMIS , vol.108 , pp. 349-356
    • Tannaes, T.1
  • 17
    • 0030943538 scopus 로고    scopus 로고
    • Colony variation of Helicobacter pylori: pathogenic potential is correlated to cell wall lipid composition
    • Bukholm G., et al. Colony variation of Helicobacter pylori: pathogenic potential is correlated to cell wall lipid composition. Scand. J. Gastroenterol. 32 (1997) 445-454
    • (1997) Scand. J. Gastroenterol. , vol.32 , pp. 445-454
    • Bukholm, G.1
  • 18
    • 33646816018 scopus 로고    scopus 로고
    • Phospholipase A in Gram-negative bacteria and its role in pathogenesis
    • Istivan T.S., and Coloe P.J. Phospholipase A in Gram-negative bacteria and its role in pathogenesis. Microbiology 152 (2006) 1263-1274
    • (2006) Microbiology , vol.152 , pp. 1263-1274
    • Istivan, T.S.1    Coloe, P.J.2
  • 19
    • 0037162559 scopus 로고    scopus 로고
    • Genome sequence of a serotype M3 strain of group A Streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence
    • Beres S.B., et al. Genome sequence of a serotype M3 strain of group A Streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 10078-10083
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10078-10083
    • Beres, S.B.1
  • 20
    • 33744728373 scopus 로고    scopus 로고
    • Acquisition and evolution of the exoU locus in Pseudomonas aeruginosa
    • Kulasekara B.R., et al. Acquisition and evolution of the exoU locus in Pseudomonas aeruginosa. J. Bacteriol. 188 (2006) 4037-4050
    • (2006) J. Bacteriol. , vol.188 , pp. 4037-4050
    • Kulasekara, B.R.1
  • 21
    • 19644371239 scopus 로고    scopus 로고
    • Pathogen-host interactions in Pseudomonas aeruginosa pneumonia
    • Sadikot R.T., et al. Pathogen-host interactions in Pseudomonas aeruginosa pneumonia. Am. J. Respir. Crit. Care Med. 171 (2005) 1209-1223
    • (2005) Am. J. Respir. Crit. Care Med. , vol.171 , pp. 1209-1223
    • Sadikot, R.T.1
  • 22
    • 0041440107 scopus 로고    scopus 로고
    • Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates: evidence for a possible association between O serotypes and exo genes
    • Berthelot P., et al. Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates: evidence for a possible association between O serotypes and exo genes. J. Infect. Dis. 188 (2003) 512-518
    • (2003) J. Infect. Dis. , vol.188 , pp. 512-518
    • Berthelot, P.1
  • 23
    • 0034769748 scopus 로고    scopus 로고
    • Prevalence of type III secretion genes in clinical and environmental isolates of Pseudomonas aeruginosa
    • Feltman H., et al. 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
  • 24
    • 0035877065 scopus 로고    scopus 로고
    • Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections
    • Roy-Burman A., et al. Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections. J. Infect. Dis. 183 (2001) 1767-1774
    • (2001) J. Infect. Dis. , vol.183 , pp. 1767-1774
    • Roy-Burman, A.1
  • 25
    • 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., et al. 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
  • 26
    • 4444342607 scopus 로고    scopus 로고
    • ExoU is a potent intracellular phospholipase
    • Sato H., and Frank D.W. ExoU is a potent intracellular phospholipase. Mol. Microbiol. 53 (2004) 1279-1290
    • (2004) Mol. Microbiol. , vol.53 , pp. 1279-1290
    • Sato, H.1    Frank, D.W.2
  • 27
    • 0033916705 scopus 로고    scopus 로고
    • Acquisition of expression of the Pseudomonas aeruginosa ExoU cytotoxin leads to increased bacterial virulence in a murine model of acute pneumonia and systemic spread
    • Allewelt M., et al. Acquisition of expression of the Pseudomonas aeruginosa ExoU cytotoxin leads to increased bacterial virulence in a murine model of acute pneumonia and systemic spread. Infect. Immun. 68 (2000) 3998-4004
    • (2000) Infect. Immun. , vol.68 , pp. 3998-4004
    • Allewelt, M.1
  • 28
    • 0030868998 scopus 로고    scopus 로고
    • ExoU expression by Pseudomonas aeruginosa correlates with acute cytotoxicity and epithelial injury
    • Finck-Barbancon V., et al. ExoU expression by Pseudomonas aeruginosa correlates with acute cytotoxicity and epithelial injury. Mol. Microbiol. 25 (1997) 547-557
    • (1997) Mol. Microbiol. , vol.25 , pp. 547-557
    • Finck-Barbancon, V.1
  • 29
    • 0031917203 scopus 로고    scopus 로고
    • PepA, a secreted protein of Pseudomonas aeruginosa, is necessary for cytotoxicity and virulence
    • Hauser A.R., et al. PepA, a secreted protein of Pseudomonas aeruginosa, is necessary for cytotoxicity and virulence. Mol. Microbiol. 27 (1998) 807-818
    • (1998) Mol. Microbiol. , vol.27 , pp. 807-818
    • Hauser, A.R.1
  • 30
    • 0032699215 scopus 로고    scopus 로고
    • Pathogenesis of septic shock in Pseudomonas aeruginosa pneumonia
    • Kurahashi K., et al. Pathogenesis of septic shock in Pseudomonas aeruginosa pneumonia. J. Clin. Invest. 104 (1999) 743-750
    • (1999) J. Clin. Invest. , vol.104 , pp. 743-750
    • Kurahashi, K.1
  • 31
    • 8544233545 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU
    • Pankhaniya R.R., et al. Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU. Crit. Care Med. 32 (2004) 2293-2299
    • (2004) Crit. Care Med. , vol.32 , pp. 2293-2299
    • Pankhaniya, R.R.1
  • 32
    • 9244236027 scopus 로고    scopus 로고
    • Relative contributions of Pseudomonas aeruginosa ExoU, ExoS, and ExoT to virulence in the lung
    • Shaver C.M., and Hauser A.R. Relative contributions of Pseudomonas aeruginosa ExoU, ExoS, and ExoT to virulence in the lung. Infect. Immun. 72 (2004) 6969-6977
    • (2004) Infect. Immun. , vol.72 , pp. 6969-6977
    • Shaver, C.M.1    Hauser, A.R.2
  • 34
    • 0038376087 scopus 로고    scopus 로고
    • The mechanism of action of the Pseudomonas aeruginosa-encoded type III cytotoxin, ExoU
    • Sato H., et al. The mechanism of action of the Pseudomonas aeruginosa-encoded type III cytotoxin, ExoU. EMBO J. 22 (2003) 2959-2969
    • (2003) EMBO J. , vol.22 , pp. 2959-2969
    • Sato, H.1
  • 35
    • 13244295376 scopus 로고    scopus 로고
    • Characterization of phospholipase activity of the Pseudomonas aeruginosa type III cytotoxin
    • Sato H., et al. Characterization of phospholipase activity of the Pseudomonas aeruginosa type III cytotoxin. ExoU. J. Bacteriol. 187 (2005) 1192-1195
    • (2005) ExoU. J. Bacteriol. , vol.187 , pp. 1192-1195
    • Sato, H.1
  • 36
    • 33748672064 scopus 로고    scopus 로고
    • Identification of superoxide dismutase as a cofactor for the pseudomonas type III toxin, ExoU
    • Sato H., et al. Identification of superoxide dismutase as a cofactor for the pseudomonas type III toxin, ExoU. Biochemistry 45 (2006) 10368-10375
    • (2006) Biochemistry , vol.45 , pp. 10368-10375
    • Sato, H.1
  • 37
    • 33646374906 scopus 로고    scopus 로고
    • A C-terminal domain targets the Pseudomonas aeruginosa cytotoxin ExoU to the plasma membrane of host cells
    • Rabin S.D., et al. A C-terminal domain targets the Pseudomonas aeruginosa cytotoxin ExoU to the plasma membrane of host cells. Infect. Immun. 74 (2006) 2552-2561
    • (2006) Infect. Immun. , vol.74 , pp. 2552-2561
    • Rabin, S.D.1
  • 38
    • 33745621121 scopus 로고    scopus 로고
    • Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin
    • Stirling F.R., et al. Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin. Cell. Microbiol. 8 (2006) 1294-1309
    • (2006) Cell. Microbiol. , vol.8 , pp. 1294-1309
    • Stirling, F.R.1
  • 39
    • 0028339812 scopus 로고
    • 2+-independent catalytic domain
    • 2+-independent catalytic domain. J. Biol. Chem. 269 (1994) 18239-18249
    • (1994) J. Biol. Chem. , vol.269 , pp. 18239-18249
    • Nalefski, E.A.1
  • 40
    • 28044449929 scopus 로고    scopus 로고
    • Eicosanoid-mediated proinflammatory activity of Pseudomonas aeruginosa ExoU
    • Saliba A.M., et al. Eicosanoid-mediated proinflammatory activity of Pseudomonas aeruginosa ExoU. Cell. Microbiol. 7 (2005) 1811-1822
    • (2005) Cell. Microbiol. , vol.7 , pp. 1811-1822
    • Saliba, A.M.1
  • 41
    • 1542616971 scopus 로고    scopus 로고
    • Lysophospholipase A activity of Pseudomonas aeruginosa type III secretory toxin ExoU
    • Tamura M., et al. Lysophospholipase A activity of Pseudomonas aeruginosa type III secretory toxin ExoU. Biochem. Biophys. Res. Commun. 316 (2004) 323-331
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 323-331
    • Tamura, M.1
  • 42
    • 0141668951 scopus 로고    scopus 로고
    • Effector ExoU from the type III secretion system is an important modulator of gene expression in lung epithelial cells in response to Pseudomonas aeruginosa infection
    • McMorran B., et al. Effector ExoU from the type III secretion system is an important modulator of gene expression in lung epithelial cells in response to Pseudomonas aeruginosa infection. Infect. Immun. 71 (2003) 6035-6044
    • (2003) Infect. Immun. , vol.71 , pp. 6035-6044
    • McMorran, B.1
  • 43
    • 33745590720 scopus 로고    scopus 로고
    • 2-terminal kinase pathway and increases human epithelial interleukin-8 production
    • 2-terminal kinase pathway and increases human epithelial interleukin-8 production. Infect. Immun. 74 (2006) 4104-4113
    • (2006) Infect. Immun. , vol.74 , pp. 4104-4113
    • Cuzick, A.1
  • 44
    • 27144468026 scopus 로고    scopus 로고
    • The global burden of group A streptococcal diseases
    • Carapetis J.R., et al. The global burden of group A streptococcal diseases. Lancet Infect. Dis. 5 (2005) 685-694
    • (2005) Lancet Infect. Dis. , vol.5 , pp. 685-694
    • Carapetis, J.R.1
  • 45
    • 0036266169 scopus 로고    scopus 로고
    • Dissemination of the phage-associated novel superantigen gene speL in recent invasive and noninvasive Streptococcus pyogenes M3/T3 isolates in Japan
    • Ikebe T., et al. Dissemination of the phage-associated novel superantigen gene speL in recent invasive and noninvasive Streptococcus pyogenes M3/T3 isolates in Japan. Infect. Immun. 70 (2002) 3227-3233
    • (2002) Infect. Immun. , vol.70 , pp. 3227-3233
    • Ikebe, T.1
  • 46
    • 8544255579 scopus 로고    scopus 로고
    • Analysis of a novel prophage-encoded group A Streptococcus extracellular phospholipase A(2)
    • Nagiec M.J., et al. Analysis of a novel prophage-encoded group A Streptococcus extracellular phospholipase A(2). J. Biol. Chem. 279 (2004) 45909-45918
    • (2004) J. Biol. Chem. , vol.279 , pp. 45909-45918
    • Nagiec, M.J.1
  • 47
    • 0345714705 scopus 로고    scopus 로고
    • Prophage induction and expression of prophage-encoded virulence factors in group A Streptococcus serotype M3 strain MGAS315
    • Banks D.J., et al. Prophage induction and expression of prophage-encoded virulence factors in group A Streptococcus serotype M3 strain MGAS315. Infect. Immun. 71 (2003) 7079-7086
    • (2003) Infect. Immun. , vol.71 , pp. 7079-7086
    • Banks, D.J.1
  • 48
    • 23344444773 scopus 로고    scopus 로고
    • Growth characteristics of and virulence factor production by group A Streptococcus during cultivation in human saliva
    • Shelburne III S.A., et al. Growth characteristics of and virulence factor production by group A Streptococcus during cultivation in human saliva. Infect. Immun. 73 (2005) 4723-4731
    • (2005) Infect. Immun. , vol.73 , pp. 4723-4731
    • Shelburne III, S.A.1
  • 50
    • 13444279883 scopus 로고    scopus 로고
    • Extracellular deoxyribonuclease made by group A Streptococcus assists pathogenesis by enhancing evasion of the innate immune response
    • Sumby P., et al. Extracellular deoxyribonuclease made by group A Streptococcus assists pathogenesis by enhancing evasion of the innate immune response. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1679-1684
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1679-1684
    • Sumby, P.1
  • 51
    • 21144443961 scopus 로고    scopus 로고
    • Longitudinal analysis of the group A Streptococcus transcriptome in experimental pharyngitis in cynomolgus macaques
    • Virtaneva K., et al. Longitudinal analysis of the group A Streptococcus transcriptome in experimental pharyngitis in cynomolgus macaques. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 9014-9019
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9014-9019
    • Virtaneva, K.1
  • 52
    • 0037162025 scopus 로고    scopus 로고
    • Lysophospholipids and their G protein-coupled receptors in inflammation and immunity
    • Graler M.H., and Goetzl E.J. Lysophospholipids and their G protein-coupled receptors in inflammation and immunity. Biochim. Biophys. Acta 1582 (2002) 168-174
    • (2002) Biochim. Biophys. Acta , vol.1582 , pp. 168-174
    • Graler, M.H.1    Goetzl, E.J.2
  • 53
    • 21844457949 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and its receptors: an autocrine and paracrine network
    • Rosen H., and Goetzl E.J. Sphingosine 1-phosphate and its receptors: an autocrine and paracrine network. Nat. Rev. Immunol. 5 (2005) 560-570
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 560-570
    • Rosen, H.1    Goetzl, E.J.2
  • 54
    • 0036250816 scopus 로고    scopus 로고
    • The platelet-activating factor signaling system and its regulators in syndromes of inflammation and thrombosis
    • Zimmerman G.A., et al. The platelet-activating factor signaling system and its regulators in syndromes of inflammation and thrombosis. Crit. Care Med. 30 (2002) S294-S301
    • (2002) Crit. Care Med. , vol.30
    • Zimmerman, G.A.1
  • 55
    • 0035976575 scopus 로고    scopus 로고
    • Prostaglandins and leukotrienes: advances in eicosanoid biology
    • Funk C.D. Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 294 (2001) 1871-1875
    • (2001) Science , vol.294 , pp. 1871-1875
    • Funk, C.D.1
  • 56
    • 0034943516 scopus 로고    scopus 로고
    • Mixed messages: modulation of inflammation and immune responses by prostaglandins and thromboxanes
    • Tilley S.L., et al. Mixed messages: modulation of inflammation and immune responses by prostaglandins and thromboxanes. J. Clin. Invest. 108 (2001) 15-23
    • (2001) J. Clin. Invest. , vol.108 , pp. 15-23
    • Tilley, S.L.1
  • 57
    • 20144370418 scopus 로고    scopus 로고
    • The impact of eicosanoids on the crosstalk between innate and adaptive immunity: the key roles of dendritic cells
    • Harizi H., and Gualde N. The impact of eicosanoids on the crosstalk between innate and adaptive immunity: the key roles of dendritic cells. Tissue Antigens 65 (2005) 507-514
    • (2005) Tissue Antigens , vol.65 , pp. 507-514
    • Harizi, H.1    Gualde, N.2
  • 58
    • 0035431876 scopus 로고    scopus 로고
    • 2 is required for parvovirus infectivity
    • 2 is required for parvovirus infectivity. Dev. Cell 1 (2001) 291-302
    • (2001) Dev. Cell , vol.1 , pp. 291-302
    • Zadori, Z.1
  • 59
    • 28044448698 scopus 로고    scopus 로고
    • Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry
    • Farr G.A., et al. Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17148-17153
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17148-17153
    • Farr, G.A.1
  • 60
    • 0031872389 scopus 로고    scopus 로고
    • Phospholipase A of Yersinia enterocolitica contributes to pathogenesis in a mouse model
    • Schmiel D.H., et al. Phospholipase A of Yersinia enterocolitica contributes to pathogenesis in a mouse model. Infect. Immun. 66 (1998) 3941-3951
    • (1998) Infect. Immun. , vol.66 , pp. 3941-3951
    • Schmiel, D.H.1
  • 61
    • 0035544036 scopus 로고    scopus 로고
    • 2 as a pathogenic mechanism in a model of cell injury by typhus and spotted fever group rickettsiae
    • 2 as a pathogenic mechanism in a model of cell injury by typhus and spotted fever group rickettsiae. Am. J. Trop. Med. Hyg. 65 (2001) 936-942
    • (2001) Am. J. Trop. Med. Hyg. , vol.65 , pp. 936-942
    • Walker, D.H.1
  • 62
    • 3042669280 scopus 로고    scopus 로고
    • Characterization of a haemolytic phospholipase A(2) activity in clinical isolates of Campylobacter concisus
    • Istivan T.S., et al. Characterization of a haemolytic phospholipase A(2) activity in clinical isolates of Campylobacter concisus. J. Med. Microbiol. 53 (2004) 483-493
    • (2004) J. Med. Microbiol. , vol.53 , pp. 483-493
    • Istivan, T.S.1
  • 63
    • 33646949950 scopus 로고    scopus 로고
    • Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells
    • VanRheenen S.M., et al. Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells. Infect. Immun. 74 (2006) 3597-3606
    • (2006) Infect. Immun. , vol.74 , pp. 3597-3606
    • VanRheenen, S.M.1
  • 64
    • 0037022589 scopus 로고    scopus 로고
    • The human pathogen Pseudomonas aeruginosa utilizes conserved virulence pathways to infect the social amoeba Dictyostelium discoideum
    • Pukatzki S., et al. The human pathogen Pseudomonas aeruginosa utilizes conserved virulence pathways to infect the social amoeba Dictyostelium discoideum. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 3159-3164
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3159-3164
    • Pukatzki, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.