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Volumn 33, Issue 4, 2009, Pages 489-498

IrAM-An α2-macroglobulin from the hard tick Ixodes ricinus: Characterization and function in phagocytosis of a potential pathogen Chryseobacterium indologenes

Author keywords

Chryseobacterium indologenes; Innate immunity; Ixodes ricinus; Phagocytosis; Thioester proteins; 2 Macroglobulin

Indexed keywords

ALPHA 2 MACROGLOBULIN; DOUBLE STRANDED RNA; MESSENGER RNA; METHYLAMINE; THIOESTER; 1,10 PHENANTHROLINE; 1,10-PHENANTHROLINE; METALLOPROTEINASE; PHENANTHROLINE DERIVATIVE;

EID: 58649085263     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2008.09.011     Document Type: Article
Times cited : (76)

References (47)
  • 1
    • 0036160153 scopus 로고    scopus 로고
    • How drosophila combats microbial infection: a model to study innate immunity and host-pathogen interactions
    • Tzou P., De Gregorio E., and Lemaitre B. How drosophila combats microbial infection: a model to study innate immunity and host-pathogen interactions. Curr Opin Microbiol 5 (2002) 102-110
    • (2002) Curr Opin Microbiol , vol.5 , pp. 102-110
    • Tzou, P.1    De Gregorio, E.2    Lemaitre, B.3
  • 2
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., and Lee B.L. Recent advances in the innate immunity of invertebrate animals. J Biochem Mol Biol 38 (2005) 128-150
    • (2005) J Biochem Mol Biol , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 3
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of drosophila
    • Hoffmann J.A. The immune response of drosophila. Nature 426 (2003) 33-38
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffmann, J.A.1
  • 4
    • 6044227865 scopus 로고    scopus 로고
    • Immune responses and parasite transmission in blood-feeding insects
    • Lehane M.J., Aksoy S., and Levashina E. Immune responses and parasite transmission in blood-feeding insects. Trends Parasitol 20 (2004) 433-439
    • (2004) Trends Parasitol , vol.20 , pp. 433-439
    • Lehane, M.J.1    Aksoy, S.2    Levashina, E.3
  • 5
    • 3543017971 scopus 로고    scopus 로고
    • Innate immunity in the malaria vector Anopheles gambiae: comparative and functional genomics
    • Osta M.A., Christophides G.K., Vlachou D., and Kafatos F.C. Innate immunity in the malaria vector Anopheles gambiae: comparative and functional genomics. J Exp Biol 207 (2004) 2551-2563
    • (2004) J Exp Biol , vol.207 , pp. 2551-2563
    • Osta, M.A.1    Christophides, G.K.2    Vlachou, D.3    Kafatos, F.C.4
  • 6
    • 57349131989 scopus 로고    scopus 로고
    • Innate immunity in ticks
    • Taylor D. Innate immunity in ticks. J Acarol Soc Jpn 15 (2006) 109-127
    • (2006) J Acarol Soc Jpn , vol.15 , pp. 109-127
    • Taylor, D.1
  • 7
    • 52049119719 scopus 로고    scopus 로고
    • Molecular characterization and related aspects of the inate immune response in ticks
    • Sonenshine D.E., and Hynes W.L. Molecular characterization and related aspects of the inate immune response in ticks. Front Biosci 13 (2008) 7043-7046
    • (2008) Front Biosci , vol.13 , pp. 7043-7046
    • Sonenshine, D.E.1    Hynes, W.L.2
  • 8
    • 0347262495 scopus 로고    scopus 로고
    • Characterization of an alpha-macroglobulin-like glycoprotein isolated from the plasma of the soft tick Ornithodoros moubata
    • Kopacek P., Weise C., Saravanan T., Vitova K., and Grubhoffer L. Characterization of an alpha-macroglobulin-like glycoprotein isolated from the plasma of the soft tick Ornithodoros moubata. Eur J Biochem 267 (2000) 465-475
    • (2000) Eur J Biochem , vol.267 , pp. 465-475
    • Kopacek, P.1    Weise, C.2    Saravanan, T.3    Vitova, K.4    Grubhoffer, L.5
  • 9
    • 0041707780 scopus 로고    scopus 로고
    • Molecular cloning, structure and bait region splice variants of alpha2-macroglobulin from the soft tick Ornithodoros moubata
    • Saravanan T., Weise C., Sojka D., and Kopacek P. Molecular cloning, structure and bait region splice variants of alpha2-macroglobulin from the soft tick Ornithodoros moubata. Insect Biochem Mol Biol 33 (2003) 841-851
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 841-851
    • Saravanan, T.1    Weise, C.2    Sojka, D.3    Kopacek, P.4
  • 10
    • 0346157328 scopus 로고    scopus 로고
    • Thioester-containing proteins and insect immunity
    • Blandin S., and Levashina E.A. Thioester-containing proteins and insect immunity. Mol Immunol 40 (2004) 903-908
    • (2004) Mol Immunol , vol.40 , pp. 903-908
    • Blandin, S.1    Levashina, E.A.2
  • 11
    • 0034633786 scopus 로고    scopus 로고
    • Constitutive expression of a complement-like protein in toll and JAK gain-of-function mutants of drosophila
    • Lagueux M., Perrodou E., Levashina E.A., Capovilla M., and Hoffmann J.A. Constitutive expression of a complement-like protein in toll and JAK gain-of-function mutants of drosophila. Proc Natl Acad Sci 97 (2000) 11427-11432
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 11427-11432
    • Lagueux, M.1    Perrodou, E.2    Levashina, E.A.3    Capovilla, M.4    Hoffmann, J.A.5
  • 13
    • 0035831034 scopus 로고    scopus 로고
    • Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae
    • Levashina E.A., Moita L.F., Blandin S., Vriend G., Lagueux M., and Kafatos F.C. Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell 104 (2001) 709-718
    • (2001) Cell , vol.104 , pp. 709-718
    • Levashina, E.A.1    Moita, L.F.2    Blandin, S.3    Vriend, G.4    Lagueux, M.5    Kafatos, F.C.6
  • 14
    • 1542328964 scopus 로고    scopus 로고
    • Complement-like protein TEP1 is a determinant of vectorial capacity in the malaria vector Anopheles gambiae
    • Blandin S., Shiao S.H., Moita L.F., Janse C.J., Waters A.P., Kafatos F.C., et al. Complement-like protein TEP1 is a determinant of vectorial capacity in the malaria vector Anopheles gambiae. Cell 11 (2004) 661-670
    • (2004) Cell , vol.11 , pp. 661-670
    • Blandin, S.1    Shiao, S.H.2    Moita, L.F.3    Janse, C.J.4    Waters, A.P.5    Kafatos, F.C.6
  • 15
    • 44649105254 scopus 로고    scopus 로고
    • Antimalarial responses in Anopheles gambiae: From a complement-like protein to a complement-like pathway
    • Blandin S.A., Marois E., and Levashina E.A. Antimalarial responses in Anopheles gambiae: From a complement-like protein to a complement-like pathway. Cell Host Microb 3 (2008) 364-374
    • (2008) Cell Host Microb , vol.3 , pp. 364-374
    • Blandin, S.A.1    Marois, E.2    Levashina, E.A.3
  • 16
    • 0033374691 scopus 로고    scopus 로고
    • Pathogen-tick-host interactions: Borrelia burgdorferi and TBE virus
    • Nuttall P.A. Pathogen-tick-host interactions: Borrelia burgdorferi and TBE virus. Zentralbl Bakteriol 289 (1999) 492-505
    • (1999) Zentralbl Bakteriol , vol.289 , pp. 492-505
    • Nuttall, P.A.1
  • 17
    • 58649121539 scopus 로고    scopus 로고
    • A comparison of Chryseobacterium indologenes pathogenicity to the soft tick Ornithodoros moubata and hard tick Ixodes ricinus
    • Buresova V., Franta Z., and Kopacek P. A comparison of Chryseobacterium indologenes pathogenicity to the soft tick Ornithodoros moubata and hard tick Ixodes ricinus. J Invertebr Pathol 3 (2006) 96-104
    • (2006) J Invertebr Pathol , vol.3 , pp. 96-104
    • Buresova, V.1    Franta, Z.2    Kopacek, P.3
  • 18
    • 0033117543 scopus 로고    scopus 로고
    • Purification and characterization of a metalloprotease from Chryseobacterium indologenes Ix9 a and determination of the amino acid specificity with electrospray mass spectrometry
    • Venter H., Osthoff G., and Litthauer D. Purification and characterization of a metalloprotease from Chryseobacterium indologenes Ix9 a and determination of the amino acid specificity with electrospray mass spectrometry. Protein Expr Purif 15 (1999) 282-295
    • (1999) Protein Expr Purif , vol.15 , pp. 282-295
    • Venter, H.1    Osthoff, G.2    Litthauer, D.3
  • 22
    • 33751538306 scopus 로고    scopus 로고
    • Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity
    • Grunclova L., Horn M., Vancova M., Sojka D., Franta Z., Mares M., et al. Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity. Biol Chem 387 (2006) 1635-1644
    • (2006) Biol Chem , vol.387 , pp. 1635-1644
    • Grunclova, L.1    Horn, M.2    Vancova, M.3    Sojka, D.4    Franta, Z.5    Mares, M.6
  • 23
    • 0029556818 scopus 로고
    • The prophenoloxidase from the wax moth Galleria mellonella: purification and characterization of the proenzyme
    • Kopacek P., Weise C., and Götz P. The prophenoloxidase from the wax moth Galleria mellonella: purification and characterization of the proenzyme. Insect Biochem Mol Biol 25 (1995) 1081-1091
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 1081-1091
    • Kopacek, P.1    Weise, C.2    Götz, P.3
  • 24
    • 1642618154 scopus 로고    scopus 로고
    • Identification of Borrelia bugdorferi sensu stricto. Borrelia garinii and Borrelia afzelii in Ixodes ricinus ticks from Southern Bohemia using monoclonal antibodies
    • Stepanova-Tresova G., Kopecky J., and Kuthejlova M. Identification of Borrelia bugdorferi sensu stricto. Borrelia garinii and Borrelia afzelii in Ixodes ricinus ticks from Southern Bohemia using monoclonal antibodies. Zentbl Bakteriol 289 (1999) 797-806
    • (1999) Zentbl Bakteriol , vol.289 , pp. 797-806
    • Stepanova-Tresova, G.1    Kopecky, J.2    Kuthejlova, M.3
  • 25
    • 0347722697 scopus 로고    scopus 로고
    • Localization of carbohydrate attachment sites and disulfide bridges in Limulus alpha-2-macroglobulin. Evidence for two forms differing primarily in their bait region sequences
    • Husted L.B., Sorensen E.S., Armstrong P.B., Quigley J.P., Kristensen L., and Sottrup-Jensen L. Localization of carbohydrate attachment sites and disulfide bridges in Limulus alpha-2-macroglobulin. Evidence for two forms differing primarily in their bait region sequences. J Biol Chem 277 (2002) 43698-43706
    • (2002) J Biol Chem , vol.277 , pp. 43698-43706
    • Husted, L.B.1    Sorensen, E.S.2    Armstrong, P.B.3    Quigley, J.P.4    Kristensen, L.5    Sottrup-Jensen, L.6
  • 26
    • 0022998261 scopus 로고
    • Primary structure of human alpha 2-macroglobulin. Complete disulfide bridge assignment and localization of two interchain bridges in the dimeric proteinase binding unit
    • Jensen P.E., and Sottrup-Jensen L. Primary structure of human alpha 2-macroglobulin. Complete disulfide bridge assignment and localization of two interchain bridges in the dimeric proteinase binding unit. J Biol Chem 261 (1986) 15863-15869
    • (1986) J Biol Chem , vol.261 , pp. 15863-15869
    • Jensen, P.E.1    Sottrup-Jensen, L.2
  • 27
    • 0023883825 scopus 로고    scopus 로고
    • Structural basis of the binding specificity of the thioester-containing proteins C3, C4, and alpha 2-macroglobulin
    • Dodds A.W., and Law S.K. Structural basis of the binding specificity of the thioester-containing proteins C3, C4, and alpha 2-macroglobulin. Complement 5 (1998) 89-97
    • (1998) Complement , vol.5 , pp. 89-97
    • Dodds, A.W.1    Law, S.K.2
  • 28
    • 0030053692 scopus 로고    scopus 로고
    • The reaction mechanism of the internal thioester in the human complement component C4
    • Dodds A.W., Ren X.D., Willis A.C., and Law S.K. The reaction mechanism of the internal thioester in the human complement component C4. Nature 379 (1996) 177-179
    • (1996) Nature , vol.379 , pp. 177-179
    • Dodds, A.W.1    Ren, X.D.2    Willis, A.C.3    Law, S.K.4
  • 29
    • 0014426266 scopus 로고
    • Molecular alteration of alpha-2-macroglobulin by aliphatic amines
    • Steinbuch M., Pejaudier L., Quentin M., and Martin V. Molecular alteration of alpha-2-macroglobulin by aliphatic amines. Biochim Biophys Acta 154 (1968) 228-231
    • (1968) Biochim Biophys Acta , vol.154 , pp. 228-231
    • Steinbuch, M.1    Pejaudier, L.2    Quentin, M.3    Martin, V.4
  • 31
    • 0020164637 scopus 로고
    • Evolution of alpha 2-macroglobulin. The demonstration in a variety of vertebrate species of a protein resembling human alpha 2-macroglobulin
    • Starkey P.M., and Barrett A.J. Evolution of alpha 2-macroglobulin. The demonstration in a variety of vertebrate species of a protein resembling human alpha 2-macroglobulin. Biochemistry 205 (1982) 91-95
    • (1982) Biochemistry , vol.205 , pp. 91-95
    • Starkey, P.M.1    Barrett, A.J.2
  • 32
    • 0033624298 scopus 로고    scopus 로고
    • Multiple forms of alpha2-macroglobulin from a bony fish, the common carp (Cyprinus carpio): striking sequence diversity in functional sites
    • Mutsuro J., Nakao M., Fujiki K., and Yano T. Multiple forms of alpha2-macroglobulin from a bony fish, the common carp (Cyprinus carpio): striking sequence diversity in functional sites. Immunogenetics 51 (2000) 847-855
    • (2000) Immunogenetics , vol.51 , pp. 847-855
    • Mutsuro, J.1    Nakao, M.2    Fujiki, K.3    Yano, T.4
  • 33
    • 0038754046 scopus 로고    scopus 로고
    • Molecular cloning and structural characterization of the hagfish proteinase inhibitor of the alpha-2-macroglobulin family
    • Idiris A., Ohtsubo K., Yoza K., Osada T., Nakamichi N., Matsumura T., et al. Molecular cloning and structural characterization of the hagfish proteinase inhibitor of the alpha-2-macroglobulin family. J Protein Chem 22 (2003) 89-98
    • (2003) J Protein Chem , vol.22 , pp. 89-98
    • Idiris, A.1    Ohtsubo, K.2    Yoza, K.3    Osada, T.4    Nakamichi, N.5    Matsumura, T.6
  • 34
    • 0022364933 scopus 로고
    • A homologue of alpha 2-macroglobulin purified from the hemolymph of the horseshoe crab Limulus polyphemus
    • Quigley J.P., and Armstrong P.B. A homologue of alpha 2-macroglobulin purified from the hemolymph of the horseshoe crab Limulus polyphemus. J Biol Chem 260 (1985) 12715-12719
    • (1985) J Biol Chem , vol.260 , pp. 12715-12719
    • Quigley, J.P.1    Armstrong, P.B.2
  • 35
    • 33748758437 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (alpha2-M) from the haemocytes of tiger shrimp Penaeus monodon
    • Lin Y.C., Vaseeharan B., Ko C.F., Chiou T.T., and Chen J.C. Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (alpha2-M) from the haemocytes of tiger shrimp Penaeus monodon. Mol Immunol 44 (2007) 1065-1074
    • (2007) Mol Immunol , vol.44 , pp. 1065-1074
    • Lin, Y.C.1    Vaseeharan, B.2    Ko, C.F.3    Chiou, T.T.4    Chen, J.C.5
  • 36
    • 33646384915 scopus 로고    scopus 로고
    • Proteases and protease inhibitors: a balance of activities in host-pathogen interaction
    • Armstrong P.B. Proteases and protease inhibitors: a balance of activities in host-pathogen interaction. Immunobiology 21 (2006) 263-281
    • (2006) Immunobiology , vol.21 , pp. 263-281
    • Armstrong, P.B.1
  • 37
    • 0023243153 scopus 로고
    • 2-macroglobulin and chicken egg white ovomacroglobulin
    • 2-macroglobulin and chicken egg white ovomacroglobulin. J Biochem 101 (1987) 199-205
    • (1987) J Biochem , vol.101 , pp. 199-205
    • Molla, A.1    Oda, T.2    Maeda, H.3
  • 38
    • 0040370656 scopus 로고    scopus 로고
    • Protein GRAB of Streptococcus pyrogenes regulates proteolysis at the bacterial surface by binding alpha2-macroglobulin
    • Rasmussen M., Müller H.P., and Björck L. Protein GRAB of Streptococcus pyrogenes regulates proteolysis at the bacterial surface by binding alpha2-macroglobulin. J Biol Chem 274 (1999) 15336-15344
    • (1999) J Biol Chem , vol.274 , pp. 15336-15344
    • Rasmussen, M.1    Müller, H.P.2    Björck, L.3
  • 39
    • 0029988928 scopus 로고    scopus 로고
    • Inhibition of cysteine proteinase from Schistosoma mansoni larvae by alpha-macroglobulin from the plasma of Biomphalaria glabrata
    • Fryer S.E., Bender R.C., and Bayne C.J. Inhibition of cysteine proteinase from Schistosoma mansoni larvae by alpha-macroglobulin from the plasma of Biomphalaria glabrata. J Parasitol 82 (1996) 343-347
    • (1996) J Parasitol , vol.82 , pp. 343-347
    • Fryer, S.E.1    Bender, R.C.2    Bayne, C.J.3
  • 40
    • 21644480464 scopus 로고    scopus 로고
    • Identification of immune genes in grass carp Ctenopharyngodon idella in response to infection of the parasitic copepod Sinergasilus major
    • Chang M.X., Nie P., Liu G.Y., Song Y., and Gao Q. Identification of immune genes in grass carp Ctenopharyngodon idella in response to infection of the parasitic copepod Sinergasilus major. Parasitol Res 96 (2005) 224-229
    • (2005) Parasitol Res , vol.96 , pp. 224-229
    • Chang, M.X.1    Nie, P.2    Liu, G.Y.3    Song, Y.4    Gao, Q.5
  • 41
    • 0030941617 scopus 로고    scopus 로고
    • Natural anti-proteases in rainbow trout, Oncorhynchus mykiss and brook charr, Salvelinus fontinalis and the in vitro neutralization of fish alpha 2-macroglobulin by the metalloprotease from the pathogenic haemoflagellate, Cryptobia salmositica
    • Zuo X., and Woo P.T. Natural anti-proteases in rainbow trout, Oncorhynchus mykiss and brook charr, Salvelinus fontinalis and the in vitro neutralization of fish alpha 2-macroglobulin by the metalloprotease from the pathogenic haemoflagellate, Cryptobia salmositica. Parasitology 114 (1997) 375-381
    • (1997) Parasitology , vol.114 , pp. 375-381
    • Zuo, X.1    Woo, P.T.2
  • 42
    • 37349042309 scopus 로고    scopus 로고
    • Differential transcription of multiple forms of alpha-2-macroglobulin in carp (Cyprinus carpio) infected with parasites
    • Onara D.F., Forlenza M., Gonzalez S.F., Rakus KŁ, Pilarczyk A., Irnazarow I., et al. Differential transcription of multiple forms of alpha-2-macroglobulin in carp (Cyprinus carpio) infected with parasites. Dev Comp Immunol 32 (2008) 339-347
    • (2008) Dev Comp Immunol , vol.32 , pp. 339-347
    • Onara, D.F.1    Forlenza, M.2    Gonzalez, S.F.3    Rakus KŁ4    Pilarczyk, A.5    Irnazarow, I.6
  • 44
    • 31144437860 scopus 로고    scopus 로고
    • Identification of drosophila gene products required for phagocytosis of Candida albicans
    • Stroschein-Stevenson S.L., Foley E., O'Farrell P.H., and Johnson A.D. Identification of drosophila gene products required for phagocytosis of Candida albicans. PLoS Biol 4 (2005) e4
    • (2005) PLoS Biol , vol.4
    • Stroschein-Stevenson, S.L.1    Foley, E.2    O'Farrell, P.H.3    Johnson, A.D.4
  • 45
    • 21844475827 scopus 로고    scopus 로고
    • In vivo identification of novel regulators and conserved pathways of phagocytosis in A. gambiae
    • Moita L.F., Wang-Sattler R., Michel K., Zimmermann T., Blandin S., Levashina E.A., et al. In vivo identification of novel regulators and conserved pathways of phagocytosis in A. gambiae. Immunity 23 (2005) 65-73
    • (2005) Immunity , vol.23 , pp. 65-73
    • Moita, L.F.1    Wang-Sattler, R.2    Michel, K.3    Zimmermann, T.4    Blandin, S.5    Levashina, E.A.6
  • 46
    • 0025666455 scopus 로고
    • Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor
    • Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O., and Sottrup-Jensen L. Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor. FEBS Lett 276 (1990) 151-155
    • (1990) FEBS Lett , vol.276 , pp. 151-155
    • Kristensen, T.1    Moestrup, S.K.2    Gliemann, J.3    Bendtsen, L.4    Sand, O.5    Sottrup-Jensen, L.6
  • 47
    • 0034517884 scopus 로고    scopus 로고
    • High protease activity of Chryseobacterium indologenes isolates associated with invasive infection
    • Pan H.J., Teng L.J., Chen Y.C., Hsueh P.R., Yang P.C., Ho S.W., et al. High protease activity of Chryseobacterium indologenes isolates associated with invasive infection. J Microbiol Immunol Infect 33 (2000) 223-226
    • (2000) J Microbiol Immunol Infect , vol.33 , pp. 223-226
    • Pan, H.J.1    Teng, L.J.2    Chen, Y.C.3    Hsueh, P.R.4    Yang, P.C.5    Ho, S.W.6


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