메뉴 건너뛰기




Volumn 189, Issue 5, 2012, Pages 2478-2487

Human H-ficolin inhibits replication of seasonal and pandemic influenza A viruses

Author keywords

[No Author keywords available]

Indexed keywords

FICOLIN; H FICOLIN; OSELTAMIVIR; RECOMBINANT PROTEIN; SIALIC ACID; UNCLASSIFIED DRUG;

EID: 84865404380     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1103786     Document Type: Article
Times cited : (60)

References (39)
  • 1
    • 34548321364 scopus 로고    scopus 로고
    • Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins
    • Thiel, S. 2007. Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins. Mol. Immunol. 44: 3875-3888.
    • (2007) Mol. Immunol. , vol.44 , pp. 3875-3888
    • Thiel, S.1
  • 3
    • 0033060134 scopus 로고    scopus 로고
    • Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel human lectin secreted into bronchus/alveolus and bile
    • Akaiwa, M., Y. Yae, R. Sugimoto, S. O. Suzuki, T. Iwaki, K. Izuhara, and N. Hamasaki. 1999. Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel human lectin secreted into bronchus/alveolus and bile. J. Histochem. Cytochem. 47: 777-786.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 777-786
    • Akaiwa, M.1    Yae, Y.2    Sugimoto, R.3    Suzuki, S.O.4    Iwaki, T.5    Izuhara, K.6    Hamasaki, N.7
  • 4
    • 84858065747 scopus 로고    scopus 로고
    • Studies of the pattern recognition molecule H-ficolin: Specificity and purification
    • Zacho, R. M., L. Jensen, R. Terp, J. C. Jensenius, and S. Thiel. 2012. Studies of the pattern recognition molecule H-ficolin: specificity and purification. J. Biol. Chem. 287: 8071-8081.
    • (2012) J. Biol. Chem. , vol.287 , pp. 8071-8081
    • Zacho, R.M.1    Jensen, L.2    Terp, R.3    Jensenius, J.C.4    Thiel, S.5
  • 5
    • 79955508081 scopus 로고    scopus 로고
    • Serum concentrations of lectin-pathway components in healthy neonates, children and adults: Mannan-binding lectin (MBL), M-, L-, and H-ficolin, and MBL-associated serine protease-2 (MASP-2)
    • Sallenbach, S., S. Thiel, C. Aebi, M. Otth, S. Bigler, J. C. Jensenius, L. J. Schlapbach, and R. A. Ammann. 2011. Serum concentrations of lectin-pathway components in healthy neonates, children and adults: mannan-binding lectin (MBL), M-, L-, and H-ficolin, and MBL-associated serine protease-2 (MASP-2). Pediatr. Allergy Immunol. 22: 424-430.
    • (2011) Pediatr. Allergy Immunol. , vol.22 , pp. 424-430
    • Sallenbach, S.1    Thiel, S.2    Aebi, C.3    Otth, M.4    Bigler, S.5    Jensenius, J.C.6    Schlapbach, L.J.7    Ammann, R.A.8
  • 6
    • 38949154873 scopus 로고    scopus 로고
    • Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen)
    • Hummelshoj, T., L. M. Fog, H. O. Madsen, R. B. Sim, and P. Garred. 2008. Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen). Mol. Immunol. 45: 1623-1632.
    • (2008) Mol. Immunol. , vol.45 , pp. 1623-1632
    • Hummelshoj, T.1    Fog, L.M.2    Madsen, H.O.3    Sim, R.B.4    Garred, P.5
  • 8
    • 80052566371 scopus 로고    scopus 로고
    • Congenital H-ficolin deficiency in premature infants with severe necrotising enterocolitis
    • Schlapbach, L. J., S. Thiel, U. Kessler, R. A. Ammann, C. Aebi, and J. C. Jensenius. 2011. Congenital H-ficolin deficiency in premature infants with severe necrotising enterocolitis. Gut 60: 1438-1439.
    • (2011) Gut , vol.60 , pp. 1438-1439
    • Schlapbach, L.J.1    Thiel, S.2    Kessler, U.3    Ammann, R.A.4    Aebi, C.5    Jensenius, J.C.6
  • 9
    • 69949118734 scopus 로고    scopus 로고
    • Specifically binding of L-ficolin to N-glycans of HCV envelope glycoproteins E1 and E2 leads to complement activation
    • Liu, J., M. A. Ali, Y. Shi, Y. Zhao, F. Luo, J. Yu, T. Xiang, J. Tang, D. Li, Q. Hu, et al. 2009. Specifically binding of L-ficolin to N-glycans of HCV envelope glycoproteins E1 and E2 leads to complement activation. Cell. Mol. Immunol. 6: 235-244.
    • (2009) Cell. Mol. Immunol. , vol.6 , pp. 235-244
    • Liu, J.1    Ali, M.A.2    Shi, Y.3    Zhao, Y.4    Luo, F.5    Yu, J.6    Xiang, T.7    Tang, J.8    Li, D.9    Hu, Q.10
  • 10
    • 84862796428 scopus 로고    scopus 로고
    • L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo
    • Pan, Q., H. Chen, F. Wang, V. T. Jeza, W. Hou, Y. Zhao, T. Xiang, Y. Zhu, Y. Endo, T. Fujita, and X. L. Zhang. 2012. L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo. J. Innate Immun. 4: 312-324.
    • (2012) J. Innate Immun. , vol.4 , pp. 312-324
    • Pan, Q.1    Chen, H.2    Wang, F.3    Jeza, V.T.4    Hou, W.5    Zhao, Y.6    Xiang, T.7    Zhu, Y.8    Endo, Y.9    Fujita, T.10    Zhang, X.L.11
  • 11
    • 37449027688 scopus 로고    scopus 로고
    • Porcine plasma ficolin binds and reduces infectivity of porcine reproductive and respiratory syndrome virus (PRRSV) in vitro
    • Keirstead, N. D., C. Lee, D. Yoo, A. S. Brooks, and M. A. Hayes. 2008. Porcine plasma ficolin binds and reduces infectivity of porcine reproductive and respiratory syndrome virus (PRRSV) in vitro. Antiviral Res. 77: 28-38.
    • (2008) Antiviral Res. , vol.77 , pp. 28-38
    • Keirstead, N.D.1    Lee, C.2    Yoo, D.3    Brooks, A.S.4    Hayes, M.A.5
  • 12
    • 78650694711 scopus 로고    scopus 로고
    • Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin
    • Chang,W. C., K. L. Hartshorn, M. R. White, P. Moyo, I. C. Michelow, H. Koziel, B. T. Kinane, E. V. Schmidt, T. Fujita, and K. Takahashi. 2011. Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin. Biochem. Pharmacol. 81: 388-395.
    • (2011) Biochem. Pharmacol. , vol.81 , pp. 388-395
    • Chang, W.C.1    Hartshorn, K.L.2    White, M.R.3    Moyo, P.4    Michelow, I.C.5    Koziel, H.6    Kinane, B.T.7    Schmidt, E.V.8    Fujita, T.9    Takahashi, K.10
  • 14
    • 9144249121 scopus 로고    scopus 로고
    • L-ficolin is a pattern recognition molecule specific for acetyl groups
    • Krarup, A., S. Thiel, A. Hansen, T. Fujita, and J. C. Jensenius. 2004. L-ficolin is a pattern recognition molecule specific for acetyl groups. J. Biol. Chem. 279: 47513-47519.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47513-47519
    • Krarup, A.1    Thiel, S.2    Hansen, A.3    Fujita, T.4    Jensenius, J.C.5
  • 16
    • 28344454827 scopus 로고    scopus 로고
    • M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement
    • Frederiksen, P. D., S. Thiel, C. B. Larsen, and J. C. Jensenius. 2005. M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement. Scand. J. Immunol. 62: 462-473.
    • (2005) Scand. J. Immunol. , vol.62 , pp. 462-473
    • Frederiksen, P.D.1    Thiel, S.2    Larsen, C.B.3    Jensenius, J.C.4
  • 17
    • 14244266540 scopus 로고    scopus 로고
    • Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation
    • Kuraya, M., Z. Ming, X. Liu, M. Matsushita, and T. Fujita. 2005. Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation. Immunobiology 209: 689-697.
    • (2005) Immunobiology , vol.209 , pp. 689-697
    • Kuraya, M.1    Ming, Z.2    Liu, X.3    Matsushita, M.4    Fujita, T.5
  • 19
    • 34250204072 scopus 로고    scopus 로고
    • Human neutrophil defensins increase neutrophil uptake of influenza A virus and bacteria and modify virus-induced respiratory burst responses
    • Tecle, T., M. R. White, D. Gantz, E. C. Crouch, and K. L. Hartshorn. 2007. Human neutrophil defensins increase neutrophil uptake of influenza A virus and bacteria and modify virus-induced respiratory burst responses. J. Immunol. 178: 8046-8052.
    • (2007) J. Immunol. , vol.178 , pp. 8046-8052
    • Tecle, T.1    White, M.R.2    Gantz, D.3    Crouch, E.C.4    Hartshorn, K.L.5
  • 20
    • 0033962409 scopus 로고    scopus 로고
    • Enhanced antinfluenza activity of a recombinant pulmonary surfactant protein D and serum conglutinin fusion protein
    • Hartshorn, K., K. Sastry, D. Chang, M. White, and E. Crouch. 2000. Enhanced antinfluenza activity of a recombinant pulmonary surfactant protein D and serum conglutinin fusion protein. Am. J. Physiol. 278: L90-L98.
    • (2000) Am. J. Physiol. , vol.278
    • Hartshorn, K.1    Sastry, K.2    Chang, D.3    White, M.4    Crouch, E.5
  • 21
    • 0031416787 scopus 로고    scopus 로고
    • Mechanisms of anti-influenza activity of surfactant proteins A and D: Comparison with serum collectins
    • Hartshorn, K. L., M. R. White, V. Shepherd, K. Reid, J. C. Jensenius, and E. C. Crouch. 1997. Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins. Am. J. Physiol. 273: L1156-L1166.
    • (1997) Am. J. Physiol. , vol.273
    • Hartshorn, K.L.1    White, M.R.2    Shepherd, V.3    Reid, K.4    Jensenius, J.C.5    Crouch, E.C.6
  • 22
    • 79952621304 scopus 로고    scopus 로고
    • The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding
    • Qi, L., J. C. Kash, V. G. Dugan, B. W. Jagger, Y. F. Lau, Z. M. Sheng, E. C. Crouch, K. L. Hartshorn, and J. K. Taubenberger. 2011. The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding. Virology 412: 426-434.
    • (2011) Virology , vol.412 , pp. 426-434
    • Qi, L.1    Kash, J.C.2    Dugan, V.G.3    Jagger, B.W.4    Lau, Y.F.5    Sheng, Z.M.6    Crouch, E.C.7    Hartshorn, K.L.8    Taubenberger, J.K.9
  • 23
    • 77958149678 scopus 로고    scopus 로고
    • Pandemic H1N1 influenza A viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies
    • Job, E. R., Y. M. Deng, M. D. Tate, B. Bottazzi, E. C. Crouch, M. M. Dean, A. Mantovani, A. G. Brooks, and P. C. Reading. 2010. Pandemic H1N1 influenza A viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies. J. Immunol. 185: 4284-4291.
    • (2010) J. Immunol. , vol.185 , pp. 4284-4291
    • Job, E.R.1    Deng, Y.M.2    Tate, M.D.3    Bottazzi, B.4    Crouch, E.C.5    Dean, M.M.6    Mantovani, A.7    Brooks, A.G.8    Reading, P.C.9
  • 25
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: Evidence from influenza virus infection of mice
    • Reading, P. C., L. S. Morey, E. C. Crouch, and E. M. Anders. 1997. Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice. J. Virol. 71: 8204-8212.
    • (1997) J. Virol. , vol.71 , pp. 8204-8212
    • Reading, P.C.1    Morey, L.S.2    Crouch, E.C.3    Anders, E.M.4
  • 27
    • 30744469116 scopus 로고    scopus 로고
    • Salivary agglutinin and lung scavenger receptor cysteine-rich glycoprotein 340 have broad anti-influenza activities and interactions with surfactant protein D that vary according to donor source and sialylation
    • Hartshorn, K. L., A. Ligtenberg, M. R. White, M. Van Eijk, M. Hartshorn, L. Pemberton, U. Holmskov, and E. Crouch. 2006. Salivary agglutinin and lung scavenger receptor cysteine-rich glycoprotein 340 have broad anti-influenza activities and interactions with surfactant protein D that vary according to donor source and sialylation. Biochem. J. 393: 545-553.
    • (2006) Biochem. J. , vol.393 , pp. 545-553
    • Hartshorn, K.L.1    Ligtenberg, A.2    White, M.R.3    Van Eijk, M.4    Hartshorn, M.5    Pemberton, L.6    Holmskov, U.7    Crouch, E.8
  • 34
    • 0042346137 scopus 로고    scopus 로고
    • Porcine pulmonary collectins show distinct interactions with influenza A viruses: Role of the N-linked oligosaccharides in the carbohydrate recognition domain
    • van Eijk, M., M. R. White, E. C. Crouch, J. J. Batenburg, A. B. Vaandrager, L. M. Van Golde, H. P. Haagsman, and K. L. Hartshorn. 2003. Porcine pulmonary collectins show distinct interactions with influenza A viruses: role of the N-linked oligosaccharides in the carbohydrate recognition domain. J. Immunol. 171: 1431-1440.
    • (2003) J. Immunol. , vol.171 , pp. 1431-1440
    • Van Eijk, M.1    White, M.R.2    Crouch, E.C.3    Batenburg, J.J.4    Vaandrager, A.B.5    Van Golde, L.M.6    Haagsman, H.P.7    Hartshorn, K.L.8
  • 36
    • 36348946320 scopus 로고    scopus 로고
    • Inhibition of hemagglutination activity of influenza A viruses by SP-A1 and SP-A2 variants expressed in CHO cells
    • Mikerov, A. N., M. White, K. Hartshorn, G. Wang, and J. Floros. 2008. Inhibition of hemagglutination activity of influenza A viruses by SP-A1 and SP-A2 variants expressed in CHO cells. Med. Microbiol. Immunol. (Berl.) 197: 9-12.
    • (2008) Med. Microbiol. Immunol. (Berl.) , vol.197 , pp. 9-12
    • Mikerov, A.N.1    White, M.2    Hartshorn, K.3    Wang, G.4    Floros, J.5
  • 37
    • 77953296297 scopus 로고    scopus 로고
    • Role of surfactant protein A and D (SP-A and SP-D) in human antiviral host defense
    • (Schol Ed)
    • Hartshorn, K. L. 2010. Role of surfactant protein A and D (SP-A and SP-D) in human antiviral host defense. Front Biosci (Schol Ed) 2: 527-546 (Schol Ed).
    • (2010) Front Biosci (Schol Ed) , vol.2 , pp. 527-546
    • Hartshorn, K.L.1
  • 38
    • 0034667522 scopus 로고    scopus 로고
    • Mechanism of binding of surfactant protein D to influenza A viruses: Importance of binding to haemagglutinin to antiviral activity
    • Hartshorn, K. L., M. R. White, D. R. Voelker, J. Coburn, K. Zaner, and E. C. Crouch. 2000. Mechanism of binding of surfactant protein D to influenza A viruses: importance of binding to haemagglutinin to antiviral activity. Biochem. J. 351: 449-458.
    • (2000) Biochem. J. , vol.351 , pp. 449-458
    • Hartshorn, K.L.1    White, M.R.2    Voelker, D.R.3    Coburn, J.4    Zaner, K.5    Crouch, E.C.6
  • 39
    • 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., Y. Liu, K. Kanno, M. Takahashi, M. Matsushita, and T. Fujita. 2004. 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.
    • (2004) Genomics , vol.84 , pp. 737-744
    • Endo, Y.1    Liu, Y.2    Kanno, K.3    Takahashi, M.4    Matsushita, M.5    Fujita, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.