메뉴 건너뛰기




Volumn 3, Issue 4, 2008, Pages

Vitellogenin functions as a multivalent pattern recognition receptor with an opsonic activity

Author keywords

[No Author keywords available]

Indexed keywords

OPSONIN; PATTERN RECOGNITION RECEPTOR; VITELLOGENIN; LIGAND;

EID: 44849088161     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001940     Document Type: Article
Times cited : (153)

References (48)
  • 1
    • 33846565430 scopus 로고    scopus 로고
    • Apolipocrustacein, formerly vitellogenin, is the major egg yolk precursor protein in decapod crustaceans and is homologous to insect apolipophorin II/I and vertebrate apolipoprotein B
    • Avarre JC, Lubzens E, Babin PJ (2007) Apolipocrustacein, formerly vitellogenin, is the major egg yolk precursor protein in decapod crustaceans and is homologous to insect apolipophorin II/I and vertebrate apolipoprotein B. Bmc Evol Biol 7: 3.
    • (2007) Bmc Evol Biol , vol.7 , pp. 3
    • Avarre, J.C.1    Lubzens, E.2    Babin, P.J.3
  • 3
    • 0032078463 scopus 로고    scopus 로고
    • Molecular characteristics of insect vitellogenins and vitellogenin receptors
    • Sappington TW, Raikhel AS (1998) Molecular characteristics of insect vitellogenins and vitellogenin receptors. Insect Biochem Mol Biol 28: 277-300.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 277-300
    • Sappington, T.W.1    Raikhel, A.S.2
  • 5
    • 0022544506 scopus 로고
    • Expression of the vitellogenin gene in female and male sea urchin
    • Shyu AB, Raff RA, Blumenthal T (1986) Expression of the vitellogenin gene in female and male sea urchin. Proc Natl Acad Sci USA 83: 3865-3869.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3865-3869
    • Shyu, A.B.1    Raff, R.A.2    Blumenthal, T.3
  • 6
    • 0000963379 scopus 로고
    • The vitellogenin of Leucophaea maderate: Synthesis of a large phosphorylated precursor
    • della-Cioppa, G, Engelman F (1987) The vitellogenin of Leucophaea maderate: synthesis of a large phosphorylated precursor. Insect Biochem 17: 401-415.
    • (1987) Insect Biochem , vol.17 , pp. 401-415
    • della-Cioppa, G.1    Engelman, F.2
  • 7
    • 0025288991 scopus 로고
    • Biosynthesis of mosquito vitellogenin
    • Dhadialla TS, Raikhel AS (1990) Biosynthesis of mosquito vitellogenin. J Biol Chem 265: 9924-9933.
    • (1990) J Biol Chem , vol.265 , pp. 9924-9933
    • Dhadialla, T.S.1    Raikhel, A.S.2
  • 9
    • 33645054569 scopus 로고    scopus 로고
    • Downregulation of vitellogenin gene activity increases the gustatory responsiveness of honey bee workers (Apis mellifera)
    • Amdam GV, Norberg K, Page RE, Erber J, Scheiner R (2006) Downregulation of vitellogenin gene activity increases the gustatory responsiveness of honey bee workers (Apis mellifera). Behav Brain Res 169: 201-205.
    • (2006) Behav Brain Res , vol.169 , pp. 201-205
    • Amdam, G.V.1    Norberg, K.2    Page, R.E.3    Erber, J.4    Scheiner, R.5
  • 10
    • 24144451079 scopus 로고    scopus 로고
    • Vitellogenin regulates hormonal dynamics in the worker caste of a eusocial insect
    • Guidugli KR, Nascimento AM, Amdam GV, Barchuk AR, Omholt S, et al. (2005) Vitellogenin regulates hormonal dynamics in the worker caste of a eusocial insect. FEBS Lett 579: 4961-4965.
    • (2005) FEBS Lett , vol.579 , pp. 4961-4965
    • Guidugli, K.R.1    Nascimento, A.M.2    Amdam, G.V.3    Barchuk, A.R.4    Omholt, S.5
  • 11
    • 33947281456 scopus 로고    scopus 로고
    • The gene vitellogenin has multiple coordinating effects on social organization
    • Nelson CM, Ihle KE, Fondrk MK, Page RE, Amdam GV (2007) The gene vitellogenin has multiple coordinating effects on social organization. PLoS Biol 5:0673-0677.
    • (2007) PLoS Biol , vol.5 , pp. 0673-0677
    • Nelson, C.M.1    Ihle, K.E.2    Fondrk, M.K.3    Page, R.E.4    Amdam, G.V.5
  • 12
    • 32244433600 scopus 로고    scopus 로고
    • Reproductive protein protects functionally sterile honey bee workers from oxidative stress
    • Seehuus SC, Norberg K, Gimsa U, Krekling T, Amdam GV (2006) Reproductive protein protects functionally sterile honey bee workers from oxidative stress. PNAS 103: 962-967.
    • (2006) PNAS , vol.103 , pp. 962-967
    • Seehuus, S.C.1    Norberg, K.2    Gimsa, U.3    Krekling, T.4    Amdam, G.V.5
  • 13
    • 0033595808 scopus 로고    scopus 로고
    • Vitellogenin-6 is a major carbonylated.protein in aged nematode, Caenorhabditis elegans
    • Nakamura A, Yasuda K, Adachi H, Sakurai Y, Ishii N, et al. (1999) Vitellogenin-6 is a major carbonylated.protein in aged nematode, Caenorhabditis elegans. Biochem Bioph Res Co 264: 580-583.
    • (1999) Biochem Bioph Res Co , vol.264 , pp. 580-583
    • Nakamura, A.1    Yasuda, K.2    Adachi, H.3    Sakurai, Y.4    Ishii, N.5
  • 14
    • 3142601428 scopus 로고    scopus 로고
    • Amdam GV, Hartfelder K, Norberg K, Hagen A, Omholt SW (2004) Altered physiology in worker honey bees (Hymenoptera: Apidae) infested by the mite Varroa destructor (Acari: Varroidae): a factor in colony loss during over-wintering?. J Econ Entomol 97: 741-747.
    • Amdam GV, Hartfelder K, Norberg K, Hagen A, Omholt SW (2004) Altered physiology in worker honey bees (Hymenoptera: Apidae) infested by the mite Varroa destructor (Acari: Varroidae): a factor in colony loss during over-wintering?. J Econ Entomol 97: 741-747.
  • 15
    • 28944441827 scopus 로고    scopus 로고
    • Vitellogenin is a novel player in defense reactions
    • Shi XD, Zhang SC, Pang QX (2006) Vitellogenin is a novel player in defense reactions. Fish Shellfish Immunol 20: 769-772.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 769-772
    • Shi, X.D.1    Zhang, S.C.2    Pang, Q.X.3
  • 16
  • 17
    • 0036212849 scopus 로고    scopus 로고
    • Janeway CA, Medzhitov R (2002) Innate immune recognition. Annu Rem Immunol 20: 197-216.
    • Janeway CA, Medzhitov R (2002) Innate immune recognition. Annu Rem Immunol 20: 197-216.
  • 18
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway CA (1989) Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harbor Symp Quant Biol 54: 1-13.
    • (1989) Cold Spring Harbor Symp Quant Biol , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 20
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll K, Cerenius L (1998) Role of the prophenoloxidase-activating system in invertebrate immunity. Curr Opin Imummol 10: 23-28.
    • (1998) Curr Opin Imummol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 21
    • 12844260314 scopus 로고
    • Professional and non-professional phagocytes: An introduction
    • Rabinovitch M (1995) Professional and non-professional phagocytes: an introduction. Trends Cell Biol 5: 85-87.
    • (1995) Trends Cell Biol , vol.5 , pp. 85-87
    • Rabinovitch, M.1
  • 22
    • 0036909507 scopus 로고    scopus 로고
    • Signal transduction during Fc receptor-mediated phagocytosis
    • Garcia-Garcia E, Rosales C (2002) Signal transduction during Fc receptor-mediated phagocytosis. J Leukoc Biol 72: 1092-1108.
    • (2002) J Leukoc Biol , vol.72 , pp. 1092-1108
    • Garcia-Garcia, E.1    Rosales, C.2
  • 23
    • 3142551379 scopus 로고    scopus 로고
    • Mini-review: A pivotal role for innate immunity in the clearance of apoptotic cells
    • Roos A, Xu W, Castellano G, Nauta AJ, Garred P, et al. (2004) Mini-review: a pivotal role for innate immunity in the clearance of apoptotic cells. Eur J Immunol 34: 921-929.
    • (2004) Eur J Immunol , vol.34 , pp. 921-929
    • Roos, A.1    Xu, W.2    Castellano, G.3    Nauta, A.J.4    Garred, P.5
  • 24
    • 0037184995 scopus 로고    scopus 로고
    • Pattern recognition receptors: Doubling up for the innate immune responses
    • Gordon S (2002) Pattern recognition receptors: doubling up for the innate immune responses. Cell 111: 927-930.
    • (2002) Cell , vol.111 , pp. 927-930
    • Gordon, S.1
  • 25
    • 0026516931 scopus 로고
    • Function of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin
    • Jomori T, Natori S (1992) Function of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin. FEBS Lett 296: 283-286.
    • (1992) FEBS Lett , vol.296 , pp. 283-286
    • Jomori, T.1    Natori, S.2
  • 26
    • 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 EA, Moita LF, Blandin S, Vriend G, Lagueux M, et al. (2001) Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell 104: 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
  • 27
    • 0037061482 scopus 로고    scopus 로고
    • Functional genemic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet M, Manfruelli P, Pearson A, Mathey-Prevot B, Ezekowitz RA (2002) Functional genemic 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
  • 28
    • 2942547979 scopus 로고    scopus 로고
    • Eggshell and egg yolk proteins in fish: Hepatic proteins for the next generation: oogenetic, population, and evolutionary implications of endocrine disruption
    • Arukwe A, Goksøyr A (2003) Eggshell and egg yolk proteins in fish: hepatic proteins for the next generation: oogenetic, population, and evolutionary implications of endocrine disruption. Comp Hepatol 2: e4.
    • (2003) Comp Hepatol , vol.2
    • Arukwe, A.1    Goksøyr, A.2
  • 30
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O (2006) Pathogen recognition and innate immunity. Cell 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 31
    • 33646370200 scopus 로고    scopus 로고
    • Recognition of pathogens and activation of immune responses in Drosophila and horseshoe crab innate immunity
    • Kurata S, Ariki S, Kawabata S (2006) Recognition of pathogens and activation of immune responses in Drosophila and horseshoe crab innate immunity. Immunobiology 211: 237-249.
    • (2006) Immunobiology , vol.211 , pp. 237-249
    • Kurata, S.1    Ariki, S.2    Kawabata, S.3
  • 32
    • 5144220046 scopus 로고    scopus 로고
    • Infectious non-self recognition in invertebrates: Lessons from Drosophila and other insect models
    • Royet J (2004) Infectious non-self recognition in invertebrates: lessons from Drosophila and other insect models. Mol Immumol 41: 1063-1075.
    • (2004) Mol Immumol , vol.41 , pp. 1063-1075
    • Royet, J.1
  • 33
    • 40049083456 scopus 로고    scopus 로고
    • A shot-form C-type lectin from amphioxus acts as a direct microbial killing protein via interaction with peptidoglycan and glucan
    • Yu Y, Yu Y, Huang H, Feng K, Pan M, et al. (2007) A shot-form C-type lectin from amphioxus acts as a direct microbial killing protein via interaction with peptidoglycan and glucan. J Immunol 179: 8425-8434.
    • (2007) J Immunol , vol.179 , pp. 8425-8434
    • Yu, Y.1    Yu, Y.2    Huang, H.3    Feng, K.4    Pan, M.5
  • 34
    • 0037364965 scopus 로고    scopus 로고
    • Manduca sexta lipopolysaccharide-specific immulectin-2 protects larvae from bacterial infection
    • Yu XQ Kanost MR (2003) Manduca sexta lipopolysaccharide-specific immulectin-2 protects larvae from bacterial infection. Dev Comp Immunol 27: 189-196.
    • (2003) Dev Comp Immunol , vol.27 , pp. 189-196
    • Yu, X.Q.1    Kanost, M.R.2
  • 35
    • 0141495001 scopus 로고    scopus 로고
    • Fungal beta-glucans and mammalian immunity
    • Brown GD, Gordon S (2003) Fungal beta-glucans and mammalian immunity. Immunity 19: 311-315.
    • (2003) Immunity , vol.19 , pp. 311-315
    • Brown, G.D.1    Gordon, S.2
  • 37
    • 0035035528 scopus 로고    scopus 로고
    • Purification and characterization of a putative vitellogenin from the ovary amphioxus (Branchiostoma belcheri tsingtauense)
    • Sun X, Zhang S (2001) Purification and characterization of a putative vitellogenin from the ovary amphioxus (Branchiostoma belcheri tsingtauense). Comp Biochem Physiol B 129: 121-127.
    • (2001) Comp Biochem Physiol B , vol.129 , pp. 121-127
    • Sun, X.1    Zhang, S.2
  • 38
    • 78651153791 scopus 로고
    • Disc electrophoresis-II. Method and application to human serum proteins
    • Davis R (1964) Disc electrophoresis-II. Method and application to human serum proteins. Ann NY Acad Sci 121: 404-427.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, R.1
  • 39
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major potypeptide of the human erythrocyte membrane
    • Fairbanks G, Steck TL, Wallace DFH (1971) Electrophoretic analysis of the major potypeptide of the human erythrocyte membrane. Biochem J 10: 2606-2617.
    • (1971) Biochem J , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallace, D.F.H.3
  • 40
    • 0017644146 scopus 로고
    • Estiadiol-17 beta effects on lipid and on the induction of a yolk precursor in goldfish, Carassius auratus
    • de Vlaming VL, Vodicnik MJ, Bauer G, Marquette T, Evans D (1977) Estiadiol-17 beta effects on lipid and on the induction of a yolk precursor in goldfish, Carassius auratus. Life Sci 20: 1945-1952.
    • (1977) Life Sci , vol.20 , pp. 1945-1952
    • de Vlaming, V.L.1    Vodicnik, M.J.2    Bauer, G.3    Marquette, T.4    Evans, D.5
  • 41
    • 0015890981 scopus 로고
    • Staining of phosphoproteins on acrylamide gel electropherograms
    • Cutting JA, Roth TF (1973) Staining of phosphoproteins on acrylamide gel electropherograms. Anal Biochem 54: 386-394.
    • (1973) Anal Biochem , vol.54 , pp. 386-394
    • Cutting, J.A.1    Roth, T.F.2
  • 42
    • 33750696004 scopus 로고    scopus 로고
    • Zou Y, He L, Huang SH (2006) Identification of a surface protein on human brain microvascular endothelial cells as vimentin interacting with Ercherichia coli\ invasion protein IbeA. Biochem Biophys Res Commun 351: 625-630.
    • Zou Y, He L, Huang SH (2006) Identification of a surface protein on human brain microvascular endothelial cells as vimentin interacting with Ercherichia coli\ invasion protein IbeA. Biochem Biophys Res Commun 351: 625-630.
  • 43
    • 2542457776 scopus 로고    scopus 로고
    • A new method for the screening of solid-phase combinatorial libraries for affinity chromatography
    • Roque AC, Taipa MA, Lowe CR (2004) A new method for the screening of solid-phase combinatorial libraries for affinity chromatography. J Mol Recognit 17: 262-267.
    • (2004) J Mol Recognit , vol.17 , pp. 262-267
    • Roque, A.C.1    Taipa, M.A.2    Lowe, C.R.3
  • 44
    • 0742270922 scopus 로고    scopus 로고
    • β-1,3-Glucan recognition protein-2 (βGRP-2) from Manduca sexta: An acute-phase protein that binds beta-1,3-glucan and lipoteichoic acid to aggregate fungi and bacteria and stimulate prophenoloxidase activation
    • Jiang H, Ma C, Lu ZQ, Kanost MR (2004) β-1,3-Glucan recognition protein-2 (βGRP-2) from Manduca sexta: an acute-phase protein that binds beta-1,3-glucan and lipoteichoic acid to aggregate fungi and bacteria and stimulate prophenoloxidase activation. Insect Biochem Mol Biol 34: 89-100.
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 89-100
    • Jiang, H.1    Ma, C.2    Lu, Z.Q.3    Kanost, M.R.4
  • 45
    • 0035860808 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase by membrane-targeted Raf chimeras is independent of raft localization
    • Chen X, Resh MD (2001) Activation of mitogen-activated protein kinase by membrane-targeted Raf chimeras is independent of raft localization. J Biol Chem 276: 34617-34623.
    • (2001) J Biol Chem , vol.276 , pp. 34617-34623
    • Chen, X.1    Resh, M.D.2
  • 46
    • 0018364137 scopus 로고
    • Ultrastructural study of the teleost fish kidney
    • Zapata A (1979) Ultrastructural study of the teleost fish kidney. Dev Comp Immunol 3: 55-65.
    • (1979) Dev Comp Immunol , vol.3 , pp. 55-65
    • Zapata, A.1
  • 47
    • 0019833679 scopus 로고
    • Lymphoid organs of teleost fist. II. Ultrastructure of renal lymphoid tissue of Rutilus rutilus and Gobio gobio
    • Zapata A (1981) Lymphoid organs of teleost fist. II. Ultrastructure of renal lymphoid tissue of Rutilus rutilus and Gobio gobio. Dev Comp Immunol 5:685-690.
    • (1981) Dev Comp Immunol , vol.5 , pp. 685-690
    • Zapata, A.1
  • 48
    • 0027996785 scopus 로고
    • Adjuvant Quil A improves protection in mice and enhances the opsonic capacity of antisera induced by pneumoccocal polysaccharide conjugate vaccines
    • DeVelasco EA, Dekker HA, Antal P, Jalink KP, van Strijp JA, et al. (1994) Adjuvant Quil A improves protection in mice and enhances the opsonic capacity of antisera induced by pneumoccocal polysaccharide conjugate vaccines. Vaccine 12: 1419-1422.
    • (1994) Vaccine , vol.12 , pp. 1419-1422
    • DeVelasco, E.A.1    Dekker, H.A.2    Antal, P.3    Jalink, K.P.4    van Strijp, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.