메뉴 건너뛰기




Volumn 158, Issue 1, 2011, Pages 90-98

Involvement of apolipophorin III in antibacterial defense of Galleria mellonella larvae

Author keywords

Apolipophorin III; Galleria mellonella; IEF SDS PAGE; Innate immunity; LIVE DEAD staining

Indexed keywords

APOLIPOPHORIN III; INSECT PROTEIN; UNCLASSIFIED DRUG;

EID: 78649630851     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2010.10.001     Document Type: Article
Times cited : (78)

References (48)
  • 1
    • 41149127811 scopus 로고    scopus 로고
    • Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets
    • Adamo S.A., Roberts J.L., Easy R.H., Ross N.W. Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets. J. Exp. Biol. 2008, 211:531-538.
    • (2008) J. Exp. Biol. , vol.211 , pp. 531-538
    • Adamo, S.A.1    Roberts, J.L.2    Easy, R.H.3    Ross, N.W.4
  • 2
    • 53149116721 scopus 로고    scopus 로고
    • Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation, and prolong survival upon infection in insects
    • Altincicek B., Stötzel S., Wygrecka M., Preisner K.T., Vilcinskas A. Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation, and prolong survival upon infection in insects. J. Immunol. 2008, 181:2705-2712.
    • (2008) J. Immunol. , vol.181 , pp. 2705-2712
    • Altincicek, B.1    Stötzel, S.2    Wygrecka, M.3    Preisner, K.T.4    Vilcinskas, A.5
  • 3
    • 15944373508 scopus 로고    scopus 로고
    • Apolipophorin III is a substrate for protease IV from Pseudomonas aeruginosa
    • Andrejko M., Cytryńska M., Jakubowicz T. Apolipophorin III is a substrate for protease IV from Pseudomonas aeruginosa. FEMS Microbiol. Lett. 2005, 243:331-337.
    • (2005) FEMS Microbiol. Lett. , vol.243 , pp. 331-337
    • Andrejko, M.1    Cytryńska, M.2    Jakubowicz, T.3
  • 4
    • 36849047229 scopus 로고    scopus 로고
    • Changes in Galleria mellonella apolipophorin III level during Pseudomonas aeruginosa infection
    • Andrejko M., Mizerska-Dudka M., Jakubowicz T. Changes in Galleria mellonella apolipophorin III level during Pseudomonas aeruginosa infection. J. Invertebr. Pathol. 2008, 97:14-19.
    • (2008) J. Invertebr. Pathol. , vol.97 , pp. 14-19
    • Andrejko, M.1    Mizerska-Dudka, M.2    Jakubowicz, T.3
  • 5
    • 0016435787 scopus 로고
    • Characterization of lipopolysaccharides from Escherichia coli K-12 mutants
    • Boman H.G., Monner D.A. Characterization of lipopolysaccharides from Escherichia coli K-12 mutants. J. Bacteriol. 1975, 121:455-464.
    • (1975) J. Bacteriol. , vol.121 , pp. 455-464
    • Boman, H.G.1    Monner, D.A.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0022501235 scopus 로고
    • Apolipophorin III in locusts: purification and characterization
    • Chino H., Yazawa M. Apolipophorin III in locusts: purification and characterization. J. Lipid Res. 1986, 27:377-385.
    • (1986) J. Lipid Res. , vol.27 , pp. 377-385
    • Chino, H.1    Yazawa, M.2
  • 9
    • 0035988708 scopus 로고    scopus 로고
    • Purification and characterization of apolipophorin III from immune hemolymph of Heliotis virescens pupae
    • Chung K.T., Ourth D.D. Purification and characterization of apolipophorin III from immune hemolymph of Heliotis virescens pupae. Comp. Biochem. Physiol. B 2002, 132:505-514.
    • (2002) Comp. Biochem. Physiol. B , vol.132 , pp. 505-514
    • Chung, K.T.1    Ourth, D.D.2
  • 10
    • 33846794525 scopus 로고    scopus 로고
    • Purification and characterization of eight peptides from Galleria mellonella immune hemolymph
    • Cytryńska M., Mak P., Zdybicka-Barabas A., Suder P., Jakubowicz T. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. Peptides 2007, 28:533-546.
    • (2007) Peptides , vol.28 , pp. 533-546
    • Cytryńska, M.1    Mak, P.2    Zdybicka-Barabas, A.3    Suder, P.4    Jakubowicz, T.5
  • 11
    • 33745228788 scopus 로고    scopus 로고
    • Studies on the role of protein kinase A in humoral immune response of Galleria mellonella larvae
    • Cytryńska M., Zdybicka-Barabas A., Jakubowicz T. Studies on the role of protein kinase A in humoral immune response of Galleria mellonella larvae. J. Insect Physiol. 2006, 52:744-753.
    • (2006) J. Insect Physiol. , vol.52 , pp. 744-753
    • Cytryńska, M.1    Zdybicka-Barabas, A.2    Jakubowicz, T.3
  • 12
    • 0035009726 scopus 로고    scopus 로고
    • Localization of injected apolipophorin III in vivo - new insights into the immune activation process directed by this protein
    • Dettloff M., Kaiser B., Wiesner A. Localization of injected apolipophorin III in vivo - new insights into the immune activation process directed by this protein. J. Insect Physiol. 2001, 47:789-797.
    • (2001) J. Insect Physiol. , vol.47 , pp. 789-797
    • Dettloff, M.1    Kaiser, B.2    Wiesner, A.3
  • 13
    • 0035213499 scopus 로고    scopus 로고
    • Lipophorin of lower density is formed during immune responses in the lepidopteran insect Galleria mellonella
    • Dettloff M., Wittwer D., Weise C., Wiesner A. Lipophorin of lower density is formed during immune responses in the lepidopteran insect Galleria mellonella. Cell Tissue Res. 2001, 306:449-458.
    • (2001) Cell Tissue Res. , vol.306 , pp. 449-458
    • Dettloff, M.1    Wittwer, D.2    Weise, C.3    Wiesner, A.4
  • 14
    • 0031252949 scopus 로고    scopus 로고
    • Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae)
    • Dunphy G., Halwani A. Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae). J. Insect Physiol. 1997, 43:1023-1029.
    • (1997) J. Insect Physiol. , vol.43 , pp. 1023-1029
    • Dunphy, G.1    Halwani, A.2
  • 15
    • 0032754032 scopus 로고    scopus 로고
    • Apolipophorin III in Galleria mellonella potentiates hemolymph lytic activity
    • Halwani A.E., Dunphy G.B. Apolipophorin III in Galleria mellonella potentiates hemolymph lytic activity. Dev. Comp. Immunol. 1999, 23:563-570.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 563-570
    • Halwani, A.E.1    Dunphy, G.B.2
  • 16
    • 0034521485 scopus 로고    scopus 로고
    • Apolipophorin-III and the interactions of lipoteichoic acids with the immediate immune responses of Galleria mellonella
    • Halwani A.E., Niven D.F., Dunphy G.B. Apolipophorin-III and the interactions of lipoteichoic acids with the immediate immune responses of Galleria mellonella. J. Invertebr. Pathol. 2000, 76:233-241.
    • (2000) J. Invertebr. Pathol. , vol.76 , pp. 233-241
    • Halwani, A.E.1    Niven, D.F.2    Dunphy, G.B.3
  • 18
    • 0031610767 scopus 로고    scopus 로고
    • Hemagglutinating properties of apolipophorin III from the hemolymph of Galleria mellonella larvae
    • Iimura Y., Ishikawa H., Yamamoto K., Sehnal F. Hemagglutinating properties of apolipophorin III from the hemolymph of Galleria mellonella larvae. Archiv. Insect Biochem. Physiol. 1998, 38:119-125.
    • (1998) Archiv. Insect Biochem. Physiol. , vol.38 , pp. 119-125
    • Iimura, Y.1    Ishikawa, H.2    Yamamoto, K.3    Sehnal, F.4
  • 19
    • 0024526129 scopus 로고
    • Structure and glycosylation of lipoteichoic acids in Bacillus strains
    • Iwasaki H., Shimada A., Yokoyama K., Ito E. Structure and glycosylation of lipoteichoic acids in Bacillus strains. J. Bacteriol. 1989, 171:424-429.
    • (1989) J. Bacteriol. , vol.171 , pp. 424-429
    • Iwasaki, H.1    Shimada, A.2    Yokoyama, K.3    Ito, E.4
  • 20
    • 0029132680 scopus 로고
    • Haemolymph immune proteins protect the insect body cavity from invading bacteria
    • Jarosz J. Haemolymph immune proteins protect the insect body cavity from invading bacteria. Comp. Biochem. Physiol. C. 1995, 111:213-220.
    • (1995) Comp. Biochem. Physiol. C. , vol.111 , pp. 213-220
    • Jarosz, J.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 277:680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0023511413 scopus 로고
    • Copper staining: a five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels
    • Lee C., Levin A., Branton D. Copper staining: a five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 1987, 166:308-312.
    • (1987) Anal. Biochem. , vol.166 , pp. 308-312
    • Lee, C.1    Levin, A.2    Branton, D.3
  • 25
    • 33746309850 scopus 로고    scopus 로고
    • Tyrosine fluorescence analysis of apolipophorin III - lipopolysaccharide interaction
    • Leon L.J., Pratt C.C., Vasquez L.J., Weers P.M.M. Tyrosine fluorescence analysis of apolipophorin III - lipopolysaccharide interaction. Archiv. Biochem. Biophys. 2006, 452:38-45.
    • (2006) Archiv. Biochem. Biophys. , vol.452 , pp. 38-45
    • Leon, L.J.1    Pratt, C.C.2    Vasquez, L.J.3    Weers, P.M.M.4
  • 26
    • 33645400827 scopus 로고    scopus 로고
    • Recognition and inactivation of LPS by lipophorin particles
    • Ma G., Hay D., Li D., Asgari S., Schmidt O. Recognition and inactivation of LPS by lipophorin particles. Dev. Comp. Immunol. 2006, 30:619-626.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 619-626
    • Ma, G.1    Hay, D.2    Li, D.3    Asgari, S.4    Schmidt, O.5
  • 27
    • 0034575124 scopus 로고    scopus 로고
    • Apolipoprotein E: far more than a lipid transport protein
    • Mahley R.W., Rall S.C. Apolipoprotein E: far more than a lipid transport protein. Annu. Rev. Genomics Hum. Genet. 2000, 01:507-537.
    • (2000) Annu. Rev. Genomics Hum. Genet. , vol.1 , pp. 507-537
    • Mahley, R.W.1    Rall, S.C.2
  • 28
    • 0015102016 scopus 로고
    • Ampicillin-resistant mutants of Escherichia coli K-12 with lipopolysaccharide alterations affecting mating ability and susceptibility to sex-specific bacteriophages
    • Monner D.A., Jonsson S., Boman H.G. Ampicillin-resistant mutants of Escherichia coli K-12 with lipopolysaccharide alterations affecting mating ability and susceptibility to sex-specific bacteriophages. J. Bacteriol. 1971, 107:420-432.
    • (1971) J. Bacteriol. , vol.107 , pp. 420-432
    • Monner, D.A.1    Jonsson, S.2    Boman, H.G.3
  • 29
    • 0037967636 scopus 로고    scopus 로고
    • Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens
    • Mullen L., Goldsworthy G. Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens. Insect Biochem. Mol. Biol. 2003, 33:661-670.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 661-670
    • Mullen, L.1    Goldsworthy, G.2
  • 30
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in Gram-positive bacteria
    • Neuhaus F.C., Baddiley J. A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in Gram-positive bacteria. Microbiol. Mol. Biol. Rev. 2003, 67:686-723.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 31
    • 0035949656 scopus 로고    scopus 로고
    • Insect immune activation by apolipophorin III is correlated with the lipid-binding properties of this protein
    • Niere M., Dettloff M., Maier T., Ziegler M., Wiesner A. Insect immune activation by apolipophorin III is correlated with the lipid-binding properties of this protein. Biochemistry 2001, 40:11502-11508.
    • (2001) Biochemistry , vol.40 , pp. 11502-11508
    • Niere, M.1    Dettloff, M.2    Maier, T.3    Ziegler, M.4    Wiesner, A.5
  • 33
    • 4344699934 scopus 로고    scopus 로고
    • Effects of two hemolymph proteins on humoral defense reactions in the wax moth, Galleria mellonella
    • Park S.Y., Kim C.H., Jeong W.H., Lee J.H., Seo S.J., Han Y.S., Lee I.H. Effects of two hemolymph proteins on humoral defense reactions in the wax moth, Galleria mellonella. Dev. Comp. Immunol. 2005, 29:43-51.
    • (2005) Dev. Comp. Immunol. , vol.29 , pp. 43-51
    • Park, S.Y.1    Kim, C.H.2    Jeong, W.H.3    Lee, J.H.4    Seo, S.J.5    Han, Y.S.6    Lee, I.H.7
  • 34
    • 0016754149 scopus 로고
    • A membrane-associated lipomannan in Micrococci
    • Powell D.A., Duckworth M., Baddiley J. A membrane-associated lipomannan in Micrococci. Biochem. J. 1975, 151:387-397.
    • (1975) Biochem. J. , vol.151 , pp. 387-397
    • Powell, D.A.1    Duckworth, M.2    Baddiley, J.3
  • 35
    • 10044286925 scopus 로고    scopus 로고
    • Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella
    • Pratt C.C., Weers P.M.M. Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella. Biol. Chem. 2004, 385:1113-1119.
    • (2004) Biol. Chem. , vol.385 , pp. 1113-1119
    • Pratt, C.C.1    Weers, P.M.M.2
  • 36
    • 0031687891 scopus 로고    scopus 로고
    • Apolipoprotein E-deficient mice have impaired innate immune responses to Listeria monocytogenes in vivo
    • Roselaar S.E., Daugherty A. Apolipoprotein E-deficient mice have impaired innate immune responses to Listeria monocytogenes in vivo. J. Lipid Res. 1998, 39:1740-1743.
    • (1998) J. Lipid Res. , vol.39 , pp. 1740-1743
    • Roselaar, S.E.1    Daugherty, A.2
  • 37
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100Da
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100Da. Anal. Biochem. 1987, 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 38
    • 55549145013 scopus 로고    scopus 로고
    • Apolipophorin III from Hyphantria cunea shows different anti-oxidant ability against LDL oxidation in the lipid-free and lipid-bound state
    • Seo S.J., Park K.-H., Cho K.-H. Apolipophorin III from Hyphantria cunea shows different anti-oxidant ability against LDL oxidation in the lipid-free and lipid-bound state. Comp. Biochem. Physiol. B 2008, 151:433-439.
    • (2008) Comp. Biochem. Physiol. B , vol.151 , pp. 433-439
    • Seo, S.J.1    Park, K.-H.2    Cho, K.-H.3
  • 39
    • 0025693237 scopus 로고
    • Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily
    • Sun S.-C., Lindström I., Boman H.G., Faye I., Schmidt O. Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science 1990, 250:1729-1732.
    • (1990) Science , vol.250 , pp. 1729-1732
    • Sun, S.-C.1    Lindström, I.2    Boman, H.G.3    Faye, I.4    Schmidt, O.5
  • 40
    • 0025719032 scopus 로고
    • Atypical lipoteichoic acids of Gram-positive bacteria
    • Sutcliffe I.C., Shaw N. Atypical lipoteichoic acids of Gram-positive bacteria. J. Bacterial. 1991, 173:7065-7069.
    • (1991) J. Bacterial. , vol.173 , pp. 7065-7069
    • Sutcliffe, I.C.1    Shaw, N.2
  • 43
    • 33645057448 scopus 로고    scopus 로고
    • Apolipophorin III: role model apolipoprotein
    • Weers P.M.M., Ryan R.O. Apolipophorin III: role model apolipoprotein. Insect Biochem. Mol. Biol. 2006, 36:231-240.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 231-240
    • Weers, P.M.M.1    Ryan, R.O.2
  • 45
    • 0031761879 scopus 로고    scopus 로고
    • Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella
    • Weise C., Franke P., Kopaćek P., Wiesner A. Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella. J. Protein Chem. 1998, 17:633-641.
    • (1998) J. Protein Chem. , vol.17 , pp. 633-641
    • Weise, C.1    Franke, P.2    Kopaćek, P.3    Wiesner, A.4
  • 46
    • 0842300362 scopus 로고    scopus 로고
    • A novel role for an insect apolipoprotein (apolipophorin III) in β-1, 3-glucan pattern recognition and cellular encapsulation reactions
    • Whitten M.M.A., Tew I.F., Lee B.L., Ratcliffe N.A. A novel role for an insect apolipoprotein (apolipophorin III) in β-1, 3-glucan pattern recognition and cellular encapsulation reactions. J. Immunol. 2004, 172:2177-2185.
    • (2004) J. Immunol. , vol.172 , pp. 2177-2185
    • Whitten, M.M.A.1    Tew, I.F.2    Lee, B.L.3    Ratcliffe, N.A.4
  • 47
    • 0030786580 scopus 로고    scopus 로고
    • Isolated apolipophorin III from Galleria mellonella stimulates the immune reactions of this insect
    • Wiesner A., Losen S., Kopaćek P., Weise C., Götz P. Isolated apolipophorin III from Galleria mellonella stimulates the immune reactions of this insect. J. Insect Physiol. 1997, 43:383-391.
    • (1997) J. Insect Physiol. , vol.43 , pp. 383-391
    • Wiesner, A.1    Losen, S.2    Kopaćek, P.3    Weise, C.4    Götz, P.5
  • 48
    • 0036648993 scopus 로고    scopus 로고
    • Apolipophorin-III affects the activity of the haemocytes of Galleria mellonella larvae
    • Zakarian R.J., Dunphy G.B., Albert P.J., Rau M.E. Apolipophorin-III affects the activity of the haemocytes of Galleria mellonella larvae. J. Insect Physiol. 2002, 48:715-723.
    • (2002) J. Insect Physiol. , vol.48 , pp. 715-723
    • Zakarian, R.J.1    Dunphy, G.B.2    Albert, P.J.3    Rau, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.