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Volumn 79, Issue 1, 2012, Pages 34-43

Primary structure and opsonic activity of an F-lectin from serum of the gilt head bream Sparus aurata (Pisces, Sparidae)

Author keywords

F lectin; hemagglutinins; opsonin; Sparus aurata; teleost

Indexed keywords

ANTIGEN; BACTERIUM; BIOCHEMICAL COMPOSITION; EEL; PERCIFORM; PROKARYOTE; PROTEIN; SERUM;

EID: 84858436449     PISSN: 11250003     EISSN: 17485851     Source Type: Journal    
DOI: 10.1080/11250003.2011.596167     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0030147252 scopus 로고    scopus 로고
    • Lectins as defence in vertebrates and invertebrates
    • Arason, GJ. 1996. Lectins as defence in vertebrates and invertebrates. Fish & Shellfish Immunology, 6: 277-289.
    • (1996) Fish & Shellfish Immunology , vol.6 , pp. 277-289
    • Arason, G.J.1
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • Arnold, K, Bordoli, L, Kopp, J and Schwede, T. 2006. The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics, 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 6
    • 77955087193 scopus 로고    scopus 로고
    • Structure and specificity of a binary tandem domain F-lectin from striped bass (Morone saxatilis)
    • Bianchet, MA, Odom, EW, Vasta, GR and Amzel, LM. 2010. Structure and specificity of a binary tandem domain F-lectin from striped bass (Morone saxatilis). Journal of Molecular Biology, 401: 239-252.
    • (2010) Journal of Molecular Biology , vol.401 , pp. 239-252
    • Bianchet, M.A.1    Odom, E.W.2    Vasta, G.R.3    Amzel, L.M.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford, MM. 1976. A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72: 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0035802281 scopus 로고    scopus 로고
    • A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax
    • Cammarata, M, Vazzana, M, Chinnici, C and Parrinello, N. 2001. A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax. Biochimica et Biophysica Acta, 1528: 196-202.
    • (2001) Biochimica et Biophysica Acta , vol.1528 , pp. 196-202
    • Cammarata, M.1    Vazzana, M.2    Chinnici, C.3    Parrinello, N.4
  • 10
    • 0028168082 scopus 로고
    • P-selectin interacts with a beta 2-integrin to enhance phagocytosis
    • Cooper, D, Butcher, CM, Berndt, MC and Vadas, MA. 1994. P-selectin interacts with a beta 2-integrin to enhance phagocytosis. Journal of Immunology, 153: 3199-3209.
    • (1994) Journal of Immunology , vol.153 , pp. 3199-3209
    • Cooper, D.1    Butcher, C.M.2    Berndt, M.C.3    Vadas, M.A.4
  • 11
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway - Its role in innate immunity and evolution
    • Fujita, T, Matsushita, M and Endo, Y. 2004. The lectin-complement pathway-Its role in innate immunity and evolution. Immunological Reviews, 198: 185-202.
    • (2004) Immunological Reviews , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 12
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N and Peitsch, MC. 1997. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18,: 2714-2723.
    • (1997) Electrophoresis 18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 13
    • 0022928012 scopus 로고
    • Methods for distinguishing ingested from adhering particles
    • Hed, J. 1986. Methods for distinguishing ingested from adhering particles. Methods in Enzymology, 132: 198-204.
    • (1986) Methods in Enzymology , vol.132 , pp. 198-204
    • Hed, J.1
  • 14
    • 0034693055 scopus 로고    scopus 로고
    • Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins
    • Honda, S, Kashiwagi, M, Miyamoto, K, Takei, Y and Hirose, S. 2000. Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins. The Journal of Biological Chemistry, 275: 33151-33157.
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 33151-33157
    • Honda, S.1    Kashiwagi, M.2    Miyamoto, K.3    Takei, Y.4    Hirose, S.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, UK. 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
  • 17
    • 0032186306 scopus 로고    scopus 로고
    • A potentially critical molecule in pathologic processes including neoplasia
    • Listinsky, J, Siegal, P and Listinsky, M. 1998. A potentially critical molecule in pathologic processes including neoplasia. American Journal of Clinical Pathology, 110: 425-440.
    • (1998) American Journal of Clinical Pathology , vol.110 , pp. 425-440
    • Listinsky, J.1    Siegal, P.2    Listinsky, M.3
  • 19
    • 33644981902 scopus 로고    scopus 로고
    • Characterization of a binary tandem domain F-type lectin from Striped Bass (Morone saxatilis)
    • Odom, E and Vasta, GR. 2006. Characterization of a binary tandem domain F-type lectin from Striped Bass (Morone saxatilis). Journal of Biological Chemistry, 281: 1698-1713.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 1698-1713
    • Odom, E.1    Vasta, G.R.2
  • 20
    • 0032966861 scopus 로고    scopus 로고
    • Enhancement of anti-Aeromonas salmonicida activity in Atlantic salmon (Salmo salar) macrophages by a mannose binding lectin
    • Ottinger, CA, Johnson, SC, Ewart, KV, Brown, LL and Ross, NW. 1999. Enhancement of anti-Aeromonas salmonicida activity in Atlantic salmon (Salmo salar) macrophages by a mannose binding lectin. Comparative Biochemistry and Physiology, 123: 53-59.
    • (1999) Comparative Biochemistry and Physiology , vol.123 , pp. 53-59
    • Ottinger, C.A.1    Johnson, S.C.2    Ewart, K.V.3    Brown, L.L.4    Ross, N.W.5
  • 21
    • 83355163630 scopus 로고    scopus 로고
    • A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs
    • Parisi, MG, Cammarata, M, Benenati, G, Salerno, G, Mangano, V, Vizzini, A and Parrinello, N. 2010. A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs. Cell Tissue Research, 341: 279-288.
    • (2010) Cell Tissue Research , vol.341 , pp. 279-288
    • Parisi, M.G.1    Cammarata, M.2    Benenati, G.3    Salerno, G.4    Mangano, V.5    Vizzini, A.6    Parrinello, N.7
  • 23
    • 0030662197 scopus 로고    scopus 로고
    • A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides
    • Saito, T, Hatada, M, Iwanaga, S and Kawabata, S. 1997. A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. Journal of Biological Chemistry, 272: 30703-30708.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30703-30708
    • Saito, T.1    Hatada, M.2    Iwanaga, S.3    Kawabata, S.4
  • 24
    • 67650479198 scopus 로고    scopus 로고
    • F-type lectin from the sea bass (Dicentrarchus labrax): Purification, cDNA cloning, tissue expression and localization, and opsonic activity
    • Salerno, G, Parisi, MG, Parrinello, D, Benenati, G, Vizzini, A, Vazzana, M, Vasta, GR and Cammarata, M. 2009. F-type lectin from the sea bass (Dicentrarchus labrax): Purification, cDNA cloning, tissue expression and localization, and opsonic activity. Fish Shellfish Immunology, 27: 143-153.
    • (2009) Fish Shellfish Immunology , vol.27 , pp. 143-153
    • Salerno, G.1    Parisi, M.G.2    Parrinello, D.3    Benenati, G.4    Vizzini, A.5    Vazzana, M.6    Vasta, G.R.7    Cammarata, M.8
  • 25
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T, Kopp, J, Guex, N and Peitsch, MC. 2003. SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Research, 31: 3381-3385.
    • (2003) Nucleic Acids Research , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 26
    • 7244258916 scopus 로고    scopus 로고
    • History of lectins: From hemagglutinins to biological recognition molecules
    • Sharon, N and Lis, H. 2004. History of lectins: From hemagglutinins to biological recognition molecules. Glycobiology, 14: 53-62.
    • (2004) Glycobiology , vol.14 , pp. 53-62
    • Sharon, N.1    Lis, H.2
  • 28
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, JD, Gibson, TJ, Plewniak, F, Jeanmougin, F and Higgins, DG. 1997. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Research, 25: 4876-4882.
    • (1997) Nucleic Acids Research , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, JD, Higgins, DG and Gibson, TJ. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research, 22: 4673-4680.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0029964034 scopus 로고    scopus 로고
    • Surfactant protein A stimulates phagocytosis of specific pulmonary pathogens by alveolar macrophages
    • Tino, MJ and Wright, JR. 1996. Surfactant protein A stimulates phagocytosis of specific pulmonary pathogens by alveolar macrophages. American Journal of Physiology, 270: 677
    • (1996) American Journal of Physiology , vol.270 , pp. 677
    • Tino, M.J.1    Wright, J.R.2
  • 32
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta, GR. 2009. Roles of galectins in infection. Nature Review Microbiology, 7: 424-438.
    • (2009) Nature Review Microbiology , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 34
    • 67650427267 scopus 로고    scopus 로고
    • Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates
    • Vasta, GR, Ahmed, H and Odom, EW. 2004. Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates. Current Opinion in Structural Biology, 11: 53-62.
    • (2004) Current Opinion in Structural Biology , vol.11 , pp. 53-62
    • Vasta, G.R.1    Ahmed, H.2    Odom, E.W.3
  • 37
    • 77956721412 scopus 로고    scopus 로고
    • The non-specific immune system: Humoral defence
    • In: Iwama G, Nakanishi, editors San Diego, CA: Academic Press
    • Yano, T. 1996. "The non-specific immune system: Humoral defence". In The fish immune system: Organism, pathogen, and environment, Edited by: Iwama, G and Nakanishi. 105-157. San Diego, CA: Academic Press.
    • (1996) The fish immune system: Organism, pathogen, and environment , pp. 105-157
    • Yano, T.1


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