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Volumn 199, Issue 10, 2004, Pages 1379-1390

Mannose-binding lectin-deficient mice are susceptible to infection with Staphylococcus aureus

Author keywords

Infection; Innate immunity; Mannose binding lectin; MBL; Neutropenia

Indexed keywords

MANNOSE BINDING PROTEIN;

EID: 2542420995     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.20032207     Document Type: Article
Times cited : (244)

References (73)
  • 1
    • 0024955886 scopus 로고
    • Approaching the asymptote: Evolution and revolution in immunology
    • Janeway, C.A. 1989. Approaching the asymptote: evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 54:1-13.
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 2
    • 0031936951 scopus 로고    scopus 로고
    • Innate immunity: The blossoming of innate immunity
    • Ezekowitz, R.A.B., and J. Hoffmann. 1998. Innate immunity: the blossoming of innate immunity (editorial overview). Curr. Opin. Immunol. 10:9-11.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 9-11
    • Ezekowitz, R.A.B.1    Hoffmann, J.2
  • 4
    • 0028205777 scopus 로고
    • Lipopolysaccharide-binding protein and CD14 in the lipopolysaccharide-dependent activation of cells
    • Tobias, P.S., and R.J. Ulevitch. 1994. Lipopolysaccharide-binding protein and CD14 in the lipopolysaccharide-dependent activation of cells. Chest. 105:48s-50s.
    • (1994) Chest , vol.105
    • Tobias, P.S.1    Ulevitch, R.J.2
  • 5
    • 0037136421 scopus 로고    scopus 로고
    • Collectins and ficolins: Sugar pattern recognition molecules of the mammalian innate immune system
    • Lu, J., C. Teh, U. Kishore, and K.B. Reid. 2002. Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system. Biochim. Biophys. Acta. 1572:387-400.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 387-400
    • Lu, J.1    Teh, C.2    Kishore, U.3    Reid, K.B.4
  • 6
    • 0041534400 scopus 로고    scopus 로고
    • Collections and ficolins: Humoral lectins of the innate immune defense
    • Holmskov, U., S. Thiel, and J.C. Jensenius. 2003. Collections and ficolins: humoral lectins of the innate immune defense. Annu. Rev. Immunol. 21:547-578.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 547-578
    • Holmskov, U.1    Thiel, S.2    Jensenius, J.C.3
  • 7
    • 0032191166 scopus 로고    scopus 로고
    • The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity
    • Fraser, I.P., H. Koziel, and R.A. Ezekowitz. 1998. The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity. Semin. Immunol. 10:363-372.
    • (1998) Semin. Immunol. , vol.10 , pp. 363-372
    • Fraser, I.P.1    Koziel, H.2    Ezekowitz, R.A.3
  • 8
    • 0027976024 scopus 로고
    • Collectins: Collagenous C-type lectins of the innate immune defense system
    • Holmskov, U., R. Malhotra, R.B. Sim, and J.C. Jensenius. 1994. Collectins: collagenous C-type lectins of the innate immune defense system. Immunol. Today. 15:67-74.
    • (1994) Immunol. Today , vol.15 , pp. 67-74
    • Holmskov, U.1    Malhotra, R.2    Sim, R.B.3    Jensenius, J.C.4
  • 9
    • 0034521609 scopus 로고    scopus 로고
    • Mannose-binding lectin: Structure, function, genetics and disease associations
    • Turner, M.W., and R.M. Hamvas. 2000. Mannose-binding lectin: structure, function, genetics and disease associations. Rev. Immunogenet. 2:305-322.
    • (2000) Rev. Immunogenet. , vol.2 , pp. 305-322
    • Turner, M.W.1    Hamvas, R.M.2
  • 11
    • 0023645042 scopus 로고
    • Serum lectin with known structure activates complement through the classical pathway
    • Ikeda, K., T. Sannoh, N. Kawasaki, T. Kawasaki, and I. Yamashina. 1987. Serum lectin with known structure activates complement through the classical pathway. J. Biol. Chem. 262:7451-7454.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7451-7454
    • Ikeda, K.1    Sannoh, T.2    Kawasaki, N.3    Kawasaki, T.4    Yamashina, I.5
  • 12
    • 0022844505 scopus 로고
    • Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
    • Drickamer, K., M.S. Dordal, and L. Reynolds. 1986. Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J. Biol. Chem. 261:6878-6887.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6878-6887
    • Drickamer, K.1    Dordal, M.S.2    Reynolds, L.3
  • 13
    • 0024553735 scopus 로고
    • The human mannose-binding protein functions as an opsonin
    • Kuhlman, M., K. Joiner, and R.A. Ezekowitz. 1989. The human mannose-binding protein functions as an opsonin. J. Exp. Med. 169:1733-1745.
    • (1989) J. Exp. Med. , vol.169 , pp. 1733-1745
    • Kuhlman, M.1    Joiner, K.2    Ezekowitz, R.A.3
  • 14
    • 0024446048 scopus 로고
    • Association of low levels of mannan-binding protein with a common defect of opsonisation
    • Super, M., S. Thiel, J. Lu, R.J. Levinsky, and M.W. Turner. 1989. Association of low levels of mannan-binding protein with a common defect of opsonisation. Lancet. 2:1236-1239.
    • (1989) Lancet , vol.2 , pp. 1236-1239
    • Super, M.1    Thiel, S.2    Lu, J.3    Levinsky, R.J.4    Turner, M.W.5
  • 16
    • 0032531088 scopus 로고    scopus 로고
    • Different molecular events result in low protein levels of mannan-binding lectin in populations from southeast Africa and South America
    • Madsen, H.O., M.L. Satz, B. Hogh, A. Svejgaard, and P. Garred. 1998. Different molecular events result in low protein levels of mannan-binding lectin in populations from southeast Africa and South America. J. Immunol. 161:3169-3175.
    • (1998) J. Immunol. , vol.161 , pp. 3169-3175
    • Madsen, H.O.1    Satz, M.L.2    Hogh, B.3    Svejgaard, A.4    Garred, P.5
  • 18
    • 0029045792 scopus 로고
    • Interplay between promoter and structural gene variants control basal serum level of mannan-binding protein
    • Madsen, H.O., P. Garred, S. Thiel, J.A. Kurtzhals, L.U. Lamm, L.P. Ryder, and A. Svejgaard. 1995. Interplay between promoter and structural gene variants control basal serum level of mannan-binding protein. J. Immunol. 155:3013-3020.
    • (1995) J. Immunol. , vol.155 , pp. 3013-3020
    • Madsen, H.O.1    Garred, P.2    Thiel, S.3    Kurtzhals, J.A.4    Lamm, L.U.5    Ryder, L.P.6    Svejgaard, A.7
  • 19
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and cd91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden, C.A., A. deCathelineau, P.R. Hoffmann, D. Bratton, B. Ghebrehiwet, V.A. Fadok, and P.M. Henson. 2001. C1q and mannose binding lectin engagement of cell surface calreticulin and cd91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 194:781-796.
    • (2001) J. Exp. Med. , vol.194 , pp. 781-796
    • Ogden, C.A.1    DeCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 20
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
    • erratum published 3:103
    • Sheriff, S., C.Y. Chang, and R.A. Ezekowitz. 1994. Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil. Nat. Struct. Biol. 1:789-794. (erratum published 3:103).
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.3
  • 21
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis, W.I., M.E. Taylor, and K. Drickamer. 1998. The C-type lectin superfamily in the immune system. Immunol. Rev. 163:19-34.
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 22
    • 0026445745 scopus 로고
    • Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease
    • Matsushita, M., and T. Fujita. 1992. Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease. J. Exp. Med. 176:1497-1502.
    • (1992) J. Exp. Med. , vol.176 , pp. 1497-1502
    • Matsushita, M.1    Fujita, T.2
  • 25
    • 0037108372 scopus 로고    scopus 로고
    • Enhancement of complement activation and opsonophagocytosis by complexes of mannose-binding lectin with mannose-binding lectin-associated serine protease after binding to Staphylococcus aureus
    • Neth, O., D.L. Jack, M. Johnson, NJ. Klein, and M.W. Turner. 2002. Enhancement of complement activation and opsonophagocytosis by complexes of mannose-binding lectin with mannose-binding lectin-associated serine protease after binding to Staphylococcus aureus. J. Immunol. 169:4430-4436.
    • (2002) J. Immunol. , vol.169 , pp. 4430-4436
    • Neth, O.1    Jack, D.L.2    Johnson, M.3    Klein, N.J.4    Turner, M.W.5
  • 26
    • 0025095417 scopus 로고
    • Association of low levels of mannan-binding protein with a common defect of opsonisation
    • Super, M., R.J. Levinsky, M.W. Turner, S. Thiel, and J. Lu. 1990. Association of low levels of mannan-binding protein with a common defect of opsonisation. Clin. Exp. Immunol. 79:144-150.
    • (1990) Clin. Exp. Immunol. , vol.79 , pp. 144-150
    • Super, M.1    Levinsky, R.J.2    Turner, M.W.3    Thiel, S.4    Lu, J.5
  • 27
    • 0034658391 scopus 로고    scopus 로고
    • Pivotal role of the CC chemokine, macrophage-derived chemokine, in the innate immune response
    • Matsukawa, A., C.M. Hogaboam, N.W. Lukacs, P.M. Lincoln, H.L. Evanoff, and S.L. Kunkel. 2000. Pivotal role of the CC chemokine, macrophage-derived chemokine, in the innate immune response. J. Immunol. 164:5362-5368.
    • (2000) J. Immunol. , vol.164 , pp. 5362-5368
    • Matsukawa, A.1    Hogaboam, C.M.2    Lukacs, N.W.3    Lincoln, P.M.4    Evanoff, H.L.5    Kunkel, S.L.6
  • 29
    • 0033650448 scopus 로고    scopus 로고
    • Collectins and collectin receptors in innate immunity
    • Holmskov, U.L. 2000. Collectins and collectin receptors in innate immunity. APMIS Suppl. 100:1-59.
    • (2000) APMIS Suppl. , vol.100 , pp. 1-59
    • Holmskov, U.L.1
  • 30
    • 0030784825 scopus 로고    scopus 로고
    • Immunomodulatory functions of surfactant
    • Wright, J.R. 1997. Immunomodulatory functions of surfactant. Physiol. Rev. 77:931-962.
    • (1997) Physiol. Rev. , vol.77 , pp. 931-962
    • Wright, J.R.1
  • 31
    • 0025166114 scopus 로고
    • CD14 serves as the cellular receptor for complexes of lipopolysaccharide with lipopolysaccharide binding protein
    • Wright, S.D., R.A. Ramons, P.S. Tobias, RJ. Ulevitch, and J.C. Mathison. 1990. CD14 serves as the cellular receptor for complexes of lipopolysaccharide with lipopolysaccharide binding protein. Science. 249:1431-1433.
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramons, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 33
    • 0038393077 scopus 로고    scopus 로고
    • Cellular versus humoral immunology: A century-long dispute
    • Silverstein, A.M. 2003. Cellular versus humoral immunology: a century-long dispute. Nat. Immunol. 4:425-428.
    • (2003) Nat. Immunol. , vol.4 , pp. 425-428
    • Silverstein, A.M.1
  • 34
    • 0037108521 scopus 로고    scopus 로고
    • Neutrophil influx in response to a peritoneal infection with Salmonella is delayed in lipopolysaccharide-binding protein or CD14-deficient mice
    • Yang, K.K., B.G. Domer, U. Merkel, B. Ryffel, C. Schutt, D. Golenbock, M.W. Freeman, R.S. Jack, J. Fierer, M.A. Swancutt, et al. 2002. Neutrophil influx in response to a peritoneal infection with Salmonella is delayed in lipopolysaccharide-binding protein or CD14-deficient mice. J. Immunol. 169:4475-4480.
    • (2002) J. Immunol. , vol.169 , pp. 4475-4480
    • Yang, K.K.1    Domer, B.G.2    Merkel, U.3    Ryffel, B.4    Schutt, C.5    Golenbock, D.6    Freeman, M.W.7    Jack, R.S.8    Fierer, J.9    Swancutt, M.A.10
  • 35
    • 0037097521 scopus 로고    scopus 로고
    • The role of lipopolysaccharide binding protein in resistance to Salmonella infections in mice
    • Fierer, J., M.A. Swancutt, D. Heumann, and D. Golenbock. 2002. The role of lipopolysaccharide binding protein in resistance to Salmonella infections in mice. J. Immunol. 168:6396-6403.
    • (2002) J. Immunol. , vol.168 , pp. 6396-6403
    • Fierer, J.1    Swancutt, M.A.2    Heumann, D.3    Golenbock, D.4
  • 36
    • 0026453082 scopus 로고
    • Diallelic polymorphism may explain variations of the blood concentration of mannan-binding protein in Eskimos, but not in black Africans
    • Garred, P., H.O. Madsen, J.A. Kurtzhals, L.U. Lamm, S. Thiel, A.S. Hey, and A. Svejgaard. 1992. Diallelic polymorphism may explain variations of the blood concentration of mannan-binding protein in Eskimos, but not in black Africans. Eur. J. Immunogenet. 19:403-412.
    • (1992) Eur. J. Immunogenet. , vol.19 , pp. 403-412
    • Garred, P.1    Madsen, H.O.2    Kurtzhals, J.A.3    Lamm, L.U.4    Thiel, S.5    Hey, A.S.6    Svejgaard, A.7
  • 37
    • 0030986151 scopus 로고    scopus 로고
    • Mannose-binding protein gene mutations are associated with childhood infection in a consecutive hospital series
    • Summerfield, J.A., M. Sumiya, M. Levin, and M.W. Turner. 1997. Mannose-binding protein gene mutations are associated with childhood infection in a consecutive hospital series. BMJ. 314:1229-1232.
    • (1997) BMJ , vol.314 , pp. 1229-1232
    • Summerfield, J.A.1    Sumiya, M.2    Levin, M.3    Turner, M.W.4
  • 38
    • 0035949119 scopus 로고    scopus 로고
    • Association between deficiency of mannose-binding lectin and severe infections after chemotherapy
    • Peterslund, N.A., C. Koch, J.C. Jensenius, and S. Thiel. 2001. Association between deficiency of mannose-binding lectin and severe infections after chemotherapy. Lancet. 358:637-638.
    • (2001) Lancet , vol.358 , pp. 637-638
    • Peterslund, N.A.1    Koch, C.2    Jensenius, J.C.3    Thiel, S.4
  • 39
    • 0031720252 scopus 로고    scopus 로고
    • Mannose-binding lectin (MBL) in health and disease
    • Turner, M.W. 1998. Mannose-binding lectin (MBL) in health and disease. Immunobiology. 199:327-339.
    • (1998) Immunobiology , vol.199 , pp. 327-339
    • Turner, M.W.1
  • 40
    • 0002862044 scopus 로고
    • Ante-antibody immunity
    • Ezekowitz, R.A.B. 1991. Ante-antibody immunity. Curr. Biol. 1:60-62.
    • (1991) Curr. Biol. , vol.1 , pp. 60-62
    • Ezekowitz, R.A.B.1
  • 41
    • 0029840182 scopus 로고    scopus 로고
    • Characterization of two mannose-binding protein cDNAs from rhesus monkey (Macaca mulatta): Structure and evolutionary implications
    • Mogues, T., T. Ota, A.I. Tauber, and K.N. Sastry. 1996. Characterization of two mannose-binding protein cDNAs from rhesus monkey (Macaca mulatta): structure and evolutionary implications. Glycobiology. 6:543-550.
    • (1996) Glycobiology , vol.6 , pp. 543-550
    • Mogues, T.1    Ota, T.2    Tauber, A.I.3    Sastry, K.N.4
  • 43
    • 0034162548 scopus 로고    scopus 로고
    • Purification and characterization of two mannan-binding lectins from mouse serum
    • Hansen, S., S. Thiel, A. Willis, U. Holmskov, and J.C. Jensenius. 2000. Purification and characterization of two mannan-binding lectins from mouse serum. J. Immunol. 164:2610-2618.
    • (2000) J. Immunol. , vol.164 , pp. 2610-2618
    • Hansen, S.1    Thiel, S.2    Willis, A.3    Holmskov, U.4    Jensenius, J.C.5
  • 44
    • 0025906415 scopus 로고
    • Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins
    • Lee, R.T., Y. Ichikawa, M. Fay, K. Drickamer, M.C. Shao, and Y.C. Lee. 1991. Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins. J. Biol. Chem. 266:4810-4815.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4810-4815
    • Lee, R.T.1    Ichikawa, Y.2    Fay, M.3    Drickamer, K.4    Shao, M.C.5    Lee, Y.C.6
  • 45
    • 0030069340 scopus 로고    scopus 로고
    • Structural analysis of monosaccharide recognition by rat liver mannose-binding protein
    • Ng, K.K., K. Drickamer, and W.I. Weis. 1996. Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. J. Biol. Chem. 271:663-674.
    • (1996) J. Biol. Chem. , vol.271 , pp. 663-674
    • Ng, K.K.1    Drickamer, K.2    Weis, W.I.3
  • 47
    • 0036888862 scopus 로고    scopus 로고
    • Disseminated candidiasis and hepatic malarial infection in mannose-binding-lectin-A-deficient mice
    • Lee, S.J., G. Gonzalez-Aseguinolaza, and M.C. Nussenzweig. 2002. Disseminated candidiasis and hepatic malarial infection in mannose-binding-lectin-A-deficient mice. Mol. Cell. Biol. 22:8199-8203.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8199-8203
    • Lee, S.J.1    Gonzalez-Aseguinolaza, G.2    Nussenzweig, M.C.3
  • 50
    • 0036891025 scopus 로고    scopus 로고
    • Age-related trends in pathogen frequency and antimicrobial susceptibility of bloodstream isolates in North America: SENTRY Antimicrobial Surveillance Program, 1997-2000
    • Diekema, D.J., M.A. Pfaller, R.N. Jones, F.J. Schmitz, J. Smayevsky, J. Bell, and M. Beach. 2002. Age-related trends in pathogen frequency and antimicrobial susceptibility of bloodstream isolates in North America: SENTRY Antimicrobial Surveillance Program, 1997-2000. Int. J. Antimicrob. Agents. 20:412-418.
    • (2002) Int. J. Antimicrob. Agents , vol.20 , pp. 412-418
    • Diekema, D.J.1    Pfaller, M.A.2    Jones, R.N.3    Schmitz, F.J.4    Smayevsky, J.5    Bell, J.6    Beach, M.7
  • 52
    • 0344688312 scopus 로고    scopus 로고
    • Is methicillin-resistant Staphylococcus aureus more virulent than methicillin-susceptible S. aureus? A comparative cohort study of British patients with nosocomial infection and bacteremia
    • Melzer, M., S.J. Eykyn, W.R. Gransden, and S. Chinn. 2003. Is methicillin-resistant Staphylococcus aureus more virulent than methicillin-susceptible S. aureus? A comparative cohort study of British patients with nosocomial infection and bacteremia. Clin. Infect. Dis. 37:1453-1460.
    • (2003) Clin. Infect. Dis. , vol.37 , pp. 1453-1460
    • Melzer, M.1    Eykyn, S.J.2    Gransden, W.R.3    Chinn, S.4
  • 54
    • 0029240468 scopus 로고
    • Characterization of murine mannose-binding protein genes Mb12 and Mb12 reveals features common to other collectin genes
    • Sastry, R., J.S. Wang, D.C. Brown, R.A. Ezekowitz, A.I. Tauber, and K.N. Sastry. 1995. Characterization of murine mannose-binding protein genes Mb12 and Mb12 reveals features common to other collectin genes. Mamm. Genome. 6:103-110.
    • (1995) Mamm. Genome , vol.6 , pp. 103-110
    • Sastry, R.1    Wang, J.S.2    Brown, D.C.3    Ezekowitz, R.A.4    Tauber, A.I.5    Sastry, K.N.6
  • 56
    • 0023233214 scopus 로고
    • Virulence studies, in mice, of transposon-induced mutants of Staphylococcus aureus differing in capsule size
    • Lee, J.C., M.J. Betley, C.A. Hopkins, N.E. Perez, and G.B. Pier. 1987. Virulence studies, in mice, of transposon-induced mutants of Staphylococcus aureus differing in capsule size. J. Infect. Dis. 156:741-750.
    • (1987) J. Infect. Dis. , vol.156 , pp. 741-750
    • Lee, J.C.1    Betley, M.J.2    Hopkins, C.A.3    Perez, N.E.4    Pier, G.B.5
  • 57
    • 0030863413 scopus 로고    scopus 로고
    • Protective efficacy of antibodies to the Staphylococcus aureus type 5 capsular polysaccharide in a modified model of endocarditis in rats
    • Lee, J.C., J.S. Park, S.E. Shepherd, V. Carey, and A. Fattom. 1997. Protective efficacy of antibodies to the Staphylococcus aureus type 5 capsular polysaccharide in a modified model of endocarditis in rats. Infect. Immun. 65:4146-4151.
    • (1997) Infect. Immun. , vol.65 , pp. 4146-4151
    • Lee, J.C.1    Park, J.S.2    Shepherd, S.E.3    Carey, V.4    Fattom, A.5
  • 58
    • 0034043676 scopus 로고    scopus 로고
    • Monitoring bioluminescent Staphylococcus aureus infections in living mice using a novel luxABCDE construct
    • Francis, K.P., D. Joh, C. Bellinger-Kawahara, M.J. Hawkinson, T.F. Purchio, and P.R. Contag. 2000. Monitoring bioluminescent Staphylococcus aureus infections in living mice using a novel luxABCDE construct. Infect. Immun. 68:3594-3600.
    • (2000) Infect. Immun. , vol.68 , pp. 3594-3600
    • Francis, K.P.1    Joh, D.2    Bellinger-Kawahara, C.3    Hawkinson, M.J.4    Purchio, T.F.5    Contag, P.R.6
  • 59
    • 0036368807 scopus 로고    scopus 로고
    • Rapid control of wound infections by targeted photodynamic therapy monitored by in vivo bioluminescence imaging
    • Hamblin, M.R., D.A. O'Donnell, N. Murthy, C.H. Contag, and T. Hasan. 2002. Rapid control of wound infections by targeted photodynamic therapy monitored by in vivo bioluminescence imaging. Photochem. Photobiol. 75:51-57.
    • (2002) Photochem. Photobiol. , vol.75 , pp. 51-57
    • Hamblin, M.R.1    O'Donnell, D.A.2    Murthy, N.3    Contag, C.H.4    Hasan, T.5
  • 60
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet, M., P. Manfruelli, A. Pearson, B. Mathey-Prevot, and R.A. Ezekowitz. 2002. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature. 416:644-648.
    • (2002) Nature , vol.416 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 61
    • 0037306528 scopus 로고    scopus 로고
    • Availability of complement bound to Staphylococcus aureus to interact with membrane complement receptors influences efficiency of phagocytosis
    • Cunnion, K.M., H.M. Zhang, and M.M. Frank. 2003. Availability of complement bound to Staphylococcus aureus to interact with membrane complement receptors influences efficiency of phagocytosis. Infect. Immun. 71:656-662.
    • (2003) Infect. Immun. , vol.71 , pp. 656-662
    • Cunnion, K.M.1    Zhang, H.M.2    Frank, M.M.3
  • 62
    • 0033789588 scopus 로고    scopus 로고
    • Role of neutrophil leukocytes in cutaneous infection caused by Staphylococcus aureus
    • Molne, L., M. Verdrengh, and A. Tarkowski. 2000. Role of neutrophil leukocytes in cutaneous infection caused by Staphylococcus aureus. Infect. Immun. 68:6162-6167.
    • (2000) Infect. Immun. , vol.68 , pp. 6162-6167
    • Molne, L.1    Verdrengh, M.2    Tarkowski, A.3
  • 63
    • 0035949107 scopus 로고    scopus 로고
    • Deficiency of mannose-binding lectin and burden of infection in children with malignancy: A prospective study
    • Neth, O., I. Hann, M.W. Turner, and N.J. Klein. 2001. Deficiency of mannose-binding lectin and burden of infection in children with malignancy: a prospective study. Lancet. 358:614-618.
    • (2001) Lancet , vol.358 , pp. 614-618
    • Neth, O.1    Hann, I.2    Turner, M.W.3    Klein, N.J.4
  • 64
    • 0037093083 scopus 로고    scopus 로고
    • Mannose-binding lectin gene polymorphisms are associated with major infection following allogeneic hemopoietic stem cell transplantation
    • Mullighan, C.G., S. Heatley, K. Doherty, F. Szabo, A. Grigg, T.P. Hughes, A.P. Schwarer, J. Szer, B.D. Tait, L. Bik To, et al. 2002. Mannose-binding lectin gene polymorphisms are associated with major infection following allogeneic hemopoietic stem cell transplantation. Blood. 99:3524-3529.
    • (2002) Blood , vol.99 , pp. 3524-3529
    • Mullighan, C.G.1    Heatley, S.2    Doherty, K.3    Szabo, F.4    Grigg, A.5    Hughes, T.P.6    Schwarer, A.P.7    Szer, J.8    Tait, B.D.9    Bik To, L.10
  • 66
    • 0034598314 scopus 로고    scopus 로고
    • Protection from lethal Gram-positive infection by macrophage scavenger receptor-dependent phagocytosis
    • Thomas, C.A., Y. Li, T. Kodama, H. Suzuki, S.C. Silverstein, and J. El Khoury. 2000. Protection from lethal Gram-positive infection by macrophage scavenger receptor-dependent phagocytosis. J. Exp. Med. 191:147-156.
    • (2000) J. Exp. Med. , vol.191 , pp. 147-156
    • Thomas, C.A.1    Li, Y.2    Kodama, T.3    Suzuki, H.4    Silverstein, S.C.5    El Khoury, J.6
  • 67
    • 0033564947 scopus 로고    scopus 로고
    • Protection by group II phospholipase A2 against Staphylococcus aureus
    • Laine, V.J., D.S. Grass, and T.J. Nevalainen. 1999. Protection by group II phospholipase A2 against Staphylococcus aureus. J. Immunol. 162:7402-7408.
    • (1999) J. Immunol. , vol.162 , pp. 7402-7408
    • Laine, V.J.1    Grass, D.S.2    Nevalainen, T.J.3
  • 69
  • 70
    • 0042766499 scopus 로고    scopus 로고
    • The major cold shock gene, cspA, is involved in the susceptibility of Staphylococcus aureus to an antimicrobial peptide of human cathepsin G
    • Katzif, S., D. Danavall, S. Bowers, J.T. Balthazar, and W.M. Shafer. 2003. The major cold shock gene, cspA, is involved in the susceptibility of Staphylococcus aureus to an antimicrobial peptide of human cathepsin G. Infect. Immun. 71:4304-4312.
    • (2003) Infect. Immun. , vol.71 , pp. 4304-4312
    • Katzif, S.1    Danavall, D.2    Bowers, S.3    Balthazar, J.T.4    Shafer, W.M.5
  • 71
    • 0027425143 scopus 로고
    • Killing of Staphylococcus aureus by tumor necrosis factor-alpha-activated neutrophils. The role of serum opsonins, integrin receptors, respiratory burst, and degranulation
    • Ferrante, A., A.J. Martin, E.J. Bates, D.H. Goh, D.P. Harvey, D. Parsons, D.A. Rathjen, G. Russ, and J.M. Dayer. 1993. Killing of Staphylococcus aureus by tumor necrosis factor-alpha-activated neutrophils. The role of serum opsonins, integrin receptors, respiratory burst, and degranulation. J. Immunol. 151:4821-4828.
    • (1993) J. Immunol. , vol.151 , pp. 4821-4828
    • Ferrante, A.1    Martin, A.J.2    Bates, E.J.3    Goh, D.H.4    Harvey, D.P.5    Parsons, D.6    Rathjen, D.A.7    Russ, G.8    Dayer, J.M.9
  • 72
    • 0025884387 scopus 로고
    • Characterization of the major neutrophil-stimulating activity present in culture medium conditioned by Staphylococcus aureus-stimulated mononuclear leukocytes
    • Bates, E.J., A. Ferrante, and L.J. Beard. 1991. Characterization of the major neutrophil-stimulating activity present in culture medium conditioned by Staphylococcus aureus-stimulated mononuclear leukocytes. Immunology. 72:448-450.
    • (1991) Immunology , vol.72 , pp. 448-450
    • Bates, E.J.1    Ferrante, A.2    Beard, L.J.3


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