메뉴 건너뛰기




Volumn 4, Issue , 2015, Pages

Molecular interaction between natural IgG and ficolin - Mechanistic insights on adaptive-innate immune crosstalk

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN ANTIBODY COMPLEX; COMPLEMENT COMPONENT C1Q; FICOLIN; HISTIDINE; IMMUNOGLOBULIN G; LECTIN; PEPTIDE FRAGMENT; PROTEIN BINDING;

EID: 84914121582     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep03675     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R. & Janeway Jr, C. A. Innate immunity: the virtues of a nonclonal system of recognition. Cell 91, 295-298 (1997).
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 2
    • 58049220365 scopus 로고    scopus 로고
    • Pattern recognition receptors and control of adaptive immunity
    • Palm, N. W. & Medzhitov, R. Pattern recognition receptors and control of adaptive immunity. Immunological reviews 227, 221-233, doi:10.1111/j.1600-065X.2008.00731.x (2009).
    • (2009) Immunological Reviews , vol.227 , pp. 221-233
    • Palm, N.W.1    Medzhitov, R.2
  • 3
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra, R. et al. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nature medicine 1, 237-243 (1995).
    • (1995) Nature Medicine , vol.1 , pp. 237-243
    • Malhotra, R.1
  • 4
    • 23844468114 scopus 로고    scopus 로고
    • Human serum IgM glycosylation: Identification of glycoforms that can bind to mannan-binding lectin
    • Arnold, J. N. et al. Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin. The Journal of biological chemistry 280, 29080-29087, doi:10.1074/jbc.M504528200 (2005).
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 29080-29087
    • Arnold, J.N.1
  • 5
    • 0038165519 scopus 로고    scopus 로고
    • Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems
    • Royle, L. et al. Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems. J Biol Chem 278, 20140-20153, doi:10.1074/jbc.M301436200 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 20140-20153
    • Royle, L.1
  • 6
    • 1642315560 scopus 로고    scopus 로고
    • Polyreactivity of antibody molecules
    • Notkins, A. L. Polyreactivity of antibody molecules. Trends Immunol 25, 174-179, doi:10.1016/j.it.2004.02.004 (2004).
    • (2004) Trends Immunol , vol.25 , pp. 174-179
    • Notkins, A.L.1
  • 7
    • 33947721996 scopus 로고    scopus 로고
    • The broad antibacterial activity of the natural antibody repertoire is due to polyreactive antibodies
    • Zhou, Z. H. et al. The broad antibacterial activity of the natural antibody repertoire is due to polyreactive antibodies. Cell host & microbe 1, 51-61, doi:10.1016/j.chom.2007.01.002 (2007).
    • (2007) Cell Host & Microbe , vol.1 , pp. 51-61
    • Zhou, Z.H.1
  • 8
    • 0032787091 scopus 로고    scopus 로고
    • Control of early viral and bacterial distribution and disease by natural antibodies
    • Ochsenbein, A. F. et al . Control of early viral and bacterial distribution and disease by natural antibodies. Science 286, 2156-2159 (1999).
    • (1999) Science , vol.286 , pp. 2156-2159
    • Ochsenbein, A.F.1
  • 9
    • 78049313303 scopus 로고    scopus 로고
    • The importance of natural IgM: Scavenger, protector and regulator
    • Ehrenstein, M. R. & Notley, C. A. The importance of natural IgM: scavenger, protector and regulator. Nature reviews. Immunology 10, 778-786, doi:10.1038/nri2849 (2010).
    • (2010) Nature Reviews. Immunology , vol.10 , pp. 778-786
    • Ehrenstein, M.R.1    Notley, C.A.2
  • 10
    • 0013986472 scopus 로고
    • Natural antibodies and the immune response
    • Boyden, S. V. Natural antibodies and the immune response. Advances in immunology 5, 1-28 (1966).
    • (1966) Advances in Immunology , vol.5 , pp. 1-28
    • Boyden, S.V.1
  • 12
    • 84887823108 scopus 로고    scopus 로고
    • Natural IgG antibodies provide innate protection against ficolin-opsonized bacteria
    • Panda, S., Zhang, J., Tan, N. S., Ho, B. & Ding, J. L. Natural IgG antibodies provide innate protection against ficolin-opsonized bacteria. The EMBO journal 32, 2905-2919, doi:10.1038/emboj.2013.199 (2013).
    • (2013) The EMBO Journal , vol.32 , pp. 2905-2919
    • Panda, S.1    Zhang, J.2    Tan, N.S.3    Ho, B.4    Ding, J.L.5
  • 13
    • 0023276640 scopus 로고
    • The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies
    • Galili, U., Buehler, J., Shohet, S. B. & Macher, B. A. The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies. The Journal of experimental medicine 165, 693-704 (1987).
    • (1987) The Journal of Experimental Medicine , vol.165 , pp. 693-704
    • Galili, U.1    Buehler, J.2    Shohet, S.B.3    Macher, B.A.4
  • 15
    • 84887822469 scopus 로고    scopus 로고
    • Protection by natural IgG: A sweet partnership with soluble lectins does the trick!
    • Puga, I. & Cerutti, A. Protection by natural IgG: a sweet partnership with soluble lectins does the trick! The EMBO journal 32, 2897-2899, doi:10.1038/emboj.2013.235 (2013).
    • (2013) The EMBO Journal , vol.32 , pp. 2897-2899
    • Puga, I.1    Cerutti, A.2
  • 16
    • 0024563950 scopus 로고
    • In vivo pH of induced soft-tissue abscesses in diabetic and nondiabetic mice
    • Bessman, A. N., Page, J. & Thomas, L. J. In vivo pH of induced soft-tissue abscesses in diabetic and nondiabetic mice. Diabetes 38, 659-662 (1989).
    • (1989) Diabetes , vol.38 , pp. 659-662
    • Bessman, A.N.1    Page, J.2    Thomas, L.J.3
  • 17
    • 33947682701 scopus 로고    scopus 로고
    • Trauma and aggressive homeostasis management
    • Baranov, D. & Neligan, P. Trauma and aggressive homeostasis management. Anesthesiology clinics 25, 49-63, viii, doi:10.1016/j.atc.2006.11.003 (2007).
    • (2007) Anesthesiology Clinics , vol.25
    • Baranov, D.1    Neligan, P.2
  • 18
    • 34548146026 scopus 로고    scopus 로고
    • Acute kidney injury, hyperosmolality and metabolic acidosis associated with lorazepam
    • Zar, T., Yusufzai, I., Sullivan, A. & Graeber, C. Acute kidney injury, hyperosmolality and metabolic acidosis associated with lorazepam. Nature clinical practice. Nephrology 3, 515-520, doi:10.1038/ncpneph0573 (2007).
    • (2007) Nature Clinical Practice. Nephrology , vol.3 , pp. 515-520
    • Zar, T.1    Yusufzai, I.2    Sullivan, A.3    Graeber, C.4
  • 21
    • 58649108986 scopus 로고    scopus 로고
    • Effects of Staphylococcus aureus-hemolysin A on calcium signalling in immortalized human airway epithelial cells
    • Eichstaedt, S. et al. Effects of Staphylococcus aureus-hemolysin A on calcium signalling in immortalized human airway epithelial cells. Cell calcium 45, 165-176, doi:10.1016/j.ceca.2008.09.001 (2009).
    • (2009) Cell Calcium , vol.45 , pp. 165-176
    • Eichstaedt, S.1
  • 22
    • 59249094527 scopus 로고    scopus 로고
    • Local inflammation induces complement crosstalk which amplifies the antimicrobial response
    • Zhang, J. et al. Local inflammation induces complement crosstalk which amplifies the antimicrobial response. PLoS Pathog 5, e1000282, doi:10.1371/journal.ppat.1000282 (2009).
    • (2009) PLoS Pathog , vol.5 , pp. e1000282
    • Zhang, J.1
  • 23
    • 0025184385 scopus 로고
    • Complement activation induced by human C-reactive protein in mildly acidic conditions
    • Miyazawa, K. & Inoue, K. Complement activation induced by human C-reactive protein in mildly acidic conditions. J Immunol 145, 650-654 (1990).
    • (1990) J Immunol , vol.145 , pp. 650-654
    • Miyazawa, K.1    Inoue, K.2
  • 24
    • 33745686066 scopus 로고    scopus 로고
    • Characterization of acid signaling in rat vagal pulmonary sensory neurons
    • Gu, Q. & Lee, L. Y. Characterization of acid signaling in rat vagal pulmonary sensory neurons. Am J Physiol Lung Cell Mol Physiol 291, L58-65, doi:10.1152/ajplung.00517.2005 (2006).
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.291 , pp. L58-L65
    • Gu, Q.1    Lee, L.Y.2
  • 25
    • 0034508025 scopus 로고    scopus 로고
    • Natural antibodies and complement link innate and acquired immunity
    • Ochsenbein, A. F. & Zinkernagel, R. M. Natural antibodies and complement link innate and acquired immunity. Immunol Today 21, 624-630 (2000).
    • (2000) Immunol Today , vol.21 , pp. 624-630
    • Ochsenbein, A.F.1    Zinkernagel, R.M.2
  • 26
    • 0041534400 scopus 로고    scopus 로고
    • Collections and ficolins: Humoral lectins of the innate immune defense
    • Holmskov, U., Thiel, S. & Jensenius, J. C. Collections and ficolins: humoral lectins of the innate immune defense. Annual review of immunology 21, 547-578, doi:10.1146/annurev.immunol.21.120601.140954 (2003).
    • (2003) Annual Review of Immunology , vol.21 , pp. 547-578
    • Holmskov, U.1    Thiel, S.2    Jensenius, J.C.3
  • 28
    • 0042279172 scopus 로고    scopus 로고
    • Protein analysis by hydrogen exchange mass spectrometry
    • Hoofnagle, A. N., Resing, K. A. & Ahn, N. G. Protein analysis by hydrogen exchange mass spectrometry. Annu Rev Biophys Biomol Struct 32, 1-25, doi:10.1146/annurev.biophys.32.110601.142417 (2003).
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 1-25
    • Hoofnagle, A.N.1    Resing, K.A.2    Ahn, N.G.3
  • 29
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • Mandell, J. G., Falick, A. M. & Komives, E. A. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal Chem 70, 3987-3995 (1998).
    • (1998) Anal Chem , vol.70 , pp. 3987-3995
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 30
    • 0023897194 scopus 로고
    • The binding site for C1q on IgG
    • Duncan, A. R. & Winter, G. The binding site for C1q on IgG. Nature 332, 738-740, doi:10.1038/332738a0 (1988).
    • (1988) Nature , vol.332 , pp. 738-740
    • Duncan, A.R.1    Winter, G.2
  • 31
    • 5444262511 scopus 로고    scopus 로고
    • Toll-like receptor control of the adaptive immune responses
    • Iwasaki, A. & Medzhitov, R. Toll-like receptor control of the adaptive immune responses. Nat Immunol 5, 987-995, doi:10.1038/ni1112 (2004).
    • (2004) Nat Immunol , vol.5 , pp. 987-995
    • Iwasaki, A.1    Medzhitov, R.2
  • 32
    • 78650675408 scopus 로고    scopus 로고
    • Secreted M-ficolin anchors onto monocyte transmembrane G protein-coupled receptor 43 and cross talks with plasma C-reactive protein to mediate immune signaling and regulate host defense
    • Zhang, J. et al. Secreted M-ficolin anchors onto monocyte transmembrane G protein-coupled receptor 43 and cross talks with plasma C-reactive protein to mediate immune signaling and regulate host defense. Journal of immunology 185, 6899-6910, doi:10.4049/jimmunol.1001225 (2010).
    • (2010) Journal of Immunology , vol.185 , pp. 6899-6910
    • Zhang, J.1
  • 33
    • 80052099312 scopus 로고    scopus 로고
    • Pathophysiological condition changes the conformation of a flexible FBG-related protein, switching it from pathogen-recognition to host-interaction
    • Zhang, J., Yang, L., Anand, G. S., Ho, B. & Ding, J. L. Pathophysiological condition changes the conformation of a flexible FBG-related protein, switching it from pathogen-recognition to host-interaction. Biochimie 93, 1710-1719, doi:10.1016/j.biochi.2011.06.003 (2011).
    • (2011) Biochimie , vol.93 , pp. 1710-1719
    • Zhang, J.1    Yang, L.2    Anand, G.S.3    Ho, B.4    Ding, J.L.5
  • 34
    • 66149122619 scopus 로고    scopus 로고
    • Serum levels of ficolin-3 (Hakata antigen) in patients with systemic lupus erythematosus
    • Andersen, T., Munthe-Fog, L., Garred, P. & Jacobsen, S. Serum levels of ficolin-3 (Hakata antigen) in patients with systemic lupus erythematosus. J Rheumatol 36, 757-759, doi:10.3899/jrheum.080361 (2009).
    • (2009) J Rheumatol , vol.36 , pp. 757-759
    • Andersen, T.1    Munthe-Fog, L.2    Garred, P.3    Jacobsen, S.4
  • 35
    • 34548038427 scopus 로고    scopus 로고
    • Identification of a functionally relevant signal peptide of mouse ficolin A
    • Kwon, S. et al. Identification of a functionally relevant signal peptide of mouse ficolin A. Journal of biochemistry and molecular biology 40, 532-538 (2007).
    • (2007) Journal of Biochemistry and Molecular Biology , vol.40 , pp. 532-538
    • Kwon, S.1
  • 36
    • 4744376266 scopus 로고    scopus 로고
    • Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human L-/M-ficolins
    • Endo, Y. et al. Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human L-/M-ficolins. Genomics 84, 737-744, doi:10.1016/j.ygeno.2004.07.006 (2004).
    • (2004) Genomics , vol.84 , pp. 737-744
    • Endo, Y.1
  • 37
    • 30744448647 scopus 로고    scopus 로고
    • Extracellular acidosis induces neutrophil activation by a mechanism dependent on activation of phosphatidylinositol 3-kinase/Akt and ERK pathways
    • Martinez, D. et al. Extracellular acidosis induces neutrophil activation by a mechanism dependent on activation of phosphatidylinositol 3-kinase/Akt and ERK pathways. J Immunol 176, 1163-1171 (2006).
    • (2006) J Immunol , vol.176 , pp. 1163-1171
    • Martinez, D.1
  • 38
    • 43449131563 scopus 로고    scopus 로고
    • Dynamic structural changes during complement C3 activation analyzed by hydrogen/deuterium exchange mass spectrometry
    • Schuster, M. C. et al. Dynamic structural changes during complement C3 activation analyzed by hydrogen/deuterium exchange mass spectrometry. Mol Immunol 45, 3142-3151, doi:10.1016/j.molimm.2008.03.010 (2008).
    • (2008) Mol Immunol , vol.45 , pp. 3142-3151
    • Schuster, M.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.