메뉴 건너뛰기




Volumn 177, Issue 7, 2006, Pages 4594-4604

Characterization of a novel C-type lectin, Bombyx mori multibinding protein, from the B. mori hemolymph: Mechanism of wide-range microorganism recognition and role in immunity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; BOMBYX MORI MULTIBINDING PROTEIN; COMPLEMENTARY DNA; LECTIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33749147438     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.7.4594     Document Type: Article
Times cited : (128)

References (30)
  • 1
    • 0024955886 scopus 로고
    • Approaching the asymptote: Evolution and revolution in Immunology
    • Janeway, Jr., C. A. 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 Jr., C.A.1
  • 2
    • 0031050034 scopus 로고    scopus 로고
    • Innate immunity: Impact on the adaptive immune response
    • Medzhitov, R., and C. A. Janeway, Jr. 1997. Innate immunity: impact on the adaptive immune response. Curr. Opin. Immunol. 9: 4-9.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 4-9
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 3
    • 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
  • 4
    • 0025784020 scopus 로고
    • Molecular cloning of cDNA for lipopolysaccharide-binding protein from the hemolymph of the American cockroach, Periplaneta americana: Similarity of the protein with animal lectins and its acute phase expression
    • Jomori, T., and S. Natori. 1991. Molecular cloning of cDNA for lipopolysaccharide-binding protein from the hemolymph of the American cockroach, Periplaneta americana: similarity of the protein with animal lectins and its acute phase expression. J. Biol. Chem. 266: 13318-13323.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13318-13323
    • Jomori, T.1    Natori, S.2
  • 5
    • 0026516931 scopus 로고
    • Function of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin
    • Jomori, T., and S. Natori. 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
  • 6
    • 0027520138 scopus 로고
    • A novel role of Periplaneta lectin as an opsonin to recognize 2-keto-3-deoxy octonate residues of bacterial lipopolysaccharides
    • Kawasaki, K., T. Kubo, and S. Natori. 1993. A novel role of Periplaneta lectin as an opsonin to recognize 2-keto-3-deoxy octonate residues of bacterial lipopolysaccharides. Comp. Biochem. Physiol. 106: 675-680.
    • (1993) Comp. Biochem. Physiol. , vol.106 , pp. 675-680
    • Kawasaki, K.1    Kubo, T.2    Natori, S.3
  • 7
    • 0033166017 scopus 로고    scopus 로고
    • Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase
    • Yu, X. Q., Gan, Hong, and M. R. Kanost. 1999. Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase. Insect Biochem. Mol. Biol. 29: 585-597.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 585-597
    • Yu, X.Q.1    Gan, H.2    Kanost, M.R.3
  • 8
    • 0345055811 scopus 로고    scopus 로고
    • Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning
    • Shin, S. W., S. S. Park, D. S. Park, M. G. Kim, S. C. Kim, P. T. Bray, and H. Y. Park. 1998. Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning. Insect Biochem. Mol. Biol. 28: 827-827.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 827-827
    • Shin, S.W.1    Park, S.S.2    Park, D.S.3    Kim, M.G.4    Kim, S.C.5    Bray, P.T.6    Park, H.Y.7
  • 9
    • 0033959641 scopus 로고    scopus 로고
    • Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain
    • Shin, S. W., D. S. Park, S. C. Kim, and H. Y. Park. 2000. Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain. FEBS Lett. 467: 70-74.
    • (2000) FEBS Lett. , vol.467 , pp. 70-74
    • Shin, S.W.1    Park, D.S.2    Kim, S.C.3    Park, H.Y.4
  • 10
    • 0030835326 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding proteins and their involvement in the bacterial clearance from the hemolymph of the silkworm Bombyx mori
    • Koizumi, N., A. Morozumi, M. Imamura, E. Tanaka, H. Iwahana, and R. Sato. 1997. Lipopolysaccharide-binding proteins and their involvement in the bacterial clearance from the hemolymph of the silkworm Bombyx mori. Eur. J. Biochem. 248: 217-224.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 217-224
    • Koizumi, N.1    Morozumi, A.2    Imamura, M.3    Tanaka, E.4    Iwahana, H.5    Sato, R.6
  • 11
    • 0032993577 scopus 로고    scopus 로고
    • The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains
    • Koizumi, N., M. Imamura, T. Kadotani, K. Yaoi, H. Iwahana, and R. Sato. 1999. The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains. FEBS Lett. 443: 139-143.
    • (1999) FEBS Lett. , vol.443 , pp. 139-143
    • Koizumi, N.1    Imamura, M.2    Kadotani, T.3    Yaoi, K.4    Iwahana, H.5    Sato, R.6
  • 13
    • 14844282115 scopus 로고    scopus 로고
    • A novel C-type limmulecitn-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes
    • Yu, X. Q., M. E. Tracy, E. Ling, F. R. Scholz, and T. Trenczek. 2005. A novel C-type limmulecitn-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes. Insect Biochem. Mol. Biol. 35: 285-295.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 285-295
    • Yu, X.Q.1    Tracy, M.E.2    Ling, E.3    Scholz, F.R.4    Trenczek, T.5
  • 15
    • 0034535375 scopus 로고    scopus 로고
    • Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to Gram-negative bacterial
    • Yu, X. Q., and M. R. Kanost. 2000. Immulectin-2, a lipopolysaccharide- specific lectin from an insect, Manduca sexta, is induced in response to Gram-negative bacterial. J. Biol. Chem. 275: 37373-37381.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37373-37381
    • Yu, X.Q.1    Kanost, M.R.2
  • 16
    • 0037364965 scopus 로고    scopus 로고
    • Manduca sexta lipopolysaccharide-specific immulectin-2 protects larvae from bacterial infection
    • Yu, X. Q., and M. R. Kanost. 2003. Manduca sexta lipopolysaccharide- specific immulectin-2 protects larvae from bacterial infection. Dev. Comp. Immunol. 21: 189-196.
    • (2003) Dev. Comp. Immunol. , vol.21 , pp. 189-196
    • Yu, X.Q.1    Kanost, M.R.2
  • 17
    • 2942617149 scopus 로고    scopus 로고
    • Immulectin-2, a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco horn-worm, Manduca sexta
    • Yu, X. Q., and M. R. Kanost. 2004. Immulectin-2, a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco horn-worm, Manduca sexta. Dev. Comp. Immunol. 28: 891-900.
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 891-900
    • Yu, X.Q.1    Kanost, M.R.2
  • 18
    • 0032767780 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein of Bombyx mori participates in a hemocyte-mediated defense reaction against Gram-negative bacteria
    • Koizumi, N., Y. Imai, A. Moroxumi, M. Imamura, T. Kadotani, K. Yaoi, H. Iwahana, and R. Sato. 1999. Lipopolysaccharide-binding protein of Bombyx mori participates in a hemocyte-mediated defense reaction against Gram-negative bacteria. J. Insect Physiol. 45: 853-859.
    • (1999) J. Insect Physiol. , vol.45 , pp. 853-859
    • Koizumi, N.1    Imai, Y.2    Moroxumi, A.3    Imamura, M.4    Kadotani, T.5    Yaoi, K.6    Iwahana, H.7    Sato, R.8
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D. W., S. G. Fischer, M. W. Kirschner, and U. K. Laemmli. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252: 1102-1106.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 21
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25: 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 22
    • 0019876887 scopus 로고
    • Isolation and characterization of a mannan-binding protein form rat liver
    • Mizuno, Y., Y. Kozutsumi, T. Kawasakik, and I. Yamashina. 1981. Isolation and characterization of a mannan-binding protein form rat liver. J. Biol. Chem. 256: 4247-4252.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4247-4252
    • Mizuno, Y.1    Kozutsumi, Y.2    Kawasakik, T.3    Yamashina, I.4
  • 23
    • 0035863454 scopus 로고    scopus 로고
    • Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation
    • Tinari, N., I. Kuwabara, M. E. Huflejt, P. F. Shen, S. Iacobelli, and F. T. Liu. 2001. Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation. Int. J. Cancer 91: 167-172.
    • (2001) Int. J. Cancer , vol.91 , pp. 167-172
    • Tinari, N.1    Kuwabara, I.2    Huflejt, M.E.3    Shen, P.F.4    Iacobelli, S.5    Liu, F.T.6
  • 24
    • 0037136403 scopus 로고    scopus 로고
    • Molecular basis of non-self recognition by the horseshoe crab tachylectins
    • Kawabata, S., and R. Tsuda. 2002. Molecular basis of non-self recognition by the horseshoe crab tachylectins. Biochim. Biophys. Acta 1572: 414-421.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 414-421
    • Kawabata, S.1    Tsuda, R.2
  • 25
    • 0028837355 scopus 로고
    • A human anti-insulin IgG autoantibody apparently arises through clonal selection from an insulin-specific "Germ-Line" natural antibody template
    • Ichiyoshi, Y., M. Zhou, and P. Casali. 1995. A human anti-insulin IgG autoantibody apparently arises through clonal selection from an insulin-specific "Germ-Line" natural antibody template. J. Immunol. 154: 226-238.
    • (1995) J. Immunol. , vol.154 , pp. 226-238
    • Ichiyoshi, Y.1    Zhou, M.2    Casali, P.3
  • 26
    • 0036839682 scopus 로고    scopus 로고
    • Contributions of the N- and C-terminal domains of surfactant protein D to the binding, aggregation, and phagocytic uptake of bacteria
    • Hartshorn, K. L., M. R. White, and E. C. Crouch. 2002. Contributions of the N- and C-terminal domains of surfactant protein D to the binding, aggregation, and phagocytic uptake of bacteria. Infect. Immun. 70: 6129-6139.
    • (2002) Infect. Immun. , vol.70 , pp. 6129-6139
    • Hartshorn, K.L.1    White, M.R.2    Crouch, E.C.3
  • 27
    • 1342303386 scopus 로고    scopus 로고
    • The classical activation pathway of the human complement system is specifically inhibited by calreticulin form Trypanosoma cruzi
    • Ferreira, V., C. Valck, G. Sanchez, A. Gingras, S. Tzima, M. C. Molina, R. Sim, W. Schwaeble, and A. Ferreira. 2004. The classical activation pathway of the human complement system is specifically inhibited by calreticulin form Trypanosoma cruzi. J. Immunol. 172: 3042-3050.
    • (2004) J. Immunol. , vol.172 , pp. 3042-3050
    • Ferreira, V.1    Valck, C.2    Sanchez, G.3    Gingras, A.4    Tzima, S.5    Molina, M.C.6    Sim, R.7    Schwaeble, W.8    Ferreira, A.9
  • 29
    • 0141918816 scopus 로고    scopus 로고
    • The role of mannose-binding lectin in health and disease
    • Turner, M. W. 2003. The role of mannose-binding lectin in health and disease. Immunology 40: 423-429.
    • (2003) Immunology , vol.40 , pp. 423-429
    • Turner, M.W.1
  • 30
    • 0023102338 scopus 로고
    • Contribution of the mannan O side-chains to the adjuvant action of lipopolysaccharides
    • Ohta, M., N. Kido, T. Hasegawa, H. Ito, Y. Fujii, Y. Arakawa, T. Komatsu, and N. Kato. 1986. Contribution of the mannan O side-chains to the adjuvant action of lipopolysaccharides. Immunology 60: 503-507.
    • (1986) Immunology , vol.60 , pp. 503-507
    • Ohta, M.1    Kido, N.2    Hasegawa, T.3    Ito, H.4    Fujii, Y.5    Arakawa, Y.6    Komatsu, T.7    Kato, N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.