메뉴 건너뛰기




Volumn 23, Issue 1, 2017, Pages 77-88

Collectins, H-ficolin and LL-37 reduce influence viral replication in human monocytes and modulate virus-induced cytokine production

Author keywords

antimicrobial peptide; Neutrophil; pandemic; phagocyte; TNF

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; COLLECTIN; CYTOKINE; H FICOLIN; M FICOLIN; MANNOSE BINDING LECTIN; SURFACTANT PROTEIN D; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN; FCN3 PROTEIN, HUMAN; GLYCOPROTEIN; LECTIN; PROTEIN BINDING;

EID: 85006716733     PISSN: 17534259     EISSN: 17534267     Source Type: Journal    
DOI: 10.1177/1753425916678470     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 84914145530 scopus 로고    scopus 로고
    • The amazing innate immune response to influenza A virus infection
    • Tripathi S, White MR, Hartshorn KL,. The amazing innate immune response to influenza A virus infection. Innate Immun 2015; 21: 73-98.
    • (2015) Innate Immun , vol.21 , pp. 73-98
    • Tripathi, S.1    White, M.R.2    Hartshorn, K.L.3
  • 2
    • 84880666005 scopus 로고    scopus 로고
    • Depletion of alveolar macrophages during influenza infection facilitates bacterial superinfections
    • Ghoneim HE, Thomas PG, McCullers JA,. Depletion of alveolar macrophages during influenza infection facilitates bacterial superinfections. J Immunol 2013; 191: 1250-1259.
    • (2013) J Immunol , vol.191 , pp. 1250-1259
    • Ghoneim, H.E.1    Thomas, P.G.2    McCullers, J.A.3
  • 3
    • 80051921486 scopus 로고    scopus 로고
    • Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice
    • Tate MD, Brooks AG, Reading PC,. Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice. J Immunol 2012; 187: 1884-1894.
    • (2012) J Immunol , vol.187 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 4
    • 42449095509 scopus 로고    scopus 로고
    • Alveolar macrophages are indispensable for controlling influenza viruses in lungs of pigs
    • Kim HM, Lee YW, Lee KJ, et al. Alveolar macrophages are indispensable for controlling influenza viruses in lungs of pigs. J Virol 2008; 82: 4265-4274.
    • (2008) J Virol , vol.82 , pp. 4265-4274
    • Kim, H.M.1    Lee, Y.W.2    Lee, K.J.3
  • 5
    • 84899878076 scopus 로고    scopus 로고
    • Recombinant human mannose-binding lectin dampens human alveolar macrophage inflammatory responses to influenza A virus in vitro
    • Epub ahead of print 7 January 2014
    • Nelson B, Zhou X, White M, et al. Recombinant human mannose-binding lectin dampens human alveolar macrophage inflammatory responses to influenza A virus in vitro. J Leukoc Biol. Epub ahead of print 7 January 2014.
    • J Leukoc Biol
    • Nelson, B.1    Zhou, X.2    White, M.3
  • 6
    • 79960862858 scopus 로고    scopus 로고
    • Critical role of serpinB1 in regulating inflammatory responses in pulmonary influenza infection
    • Gong D, Farley K, White M, et al. Critical role of serpinB1 in regulating inflammatory responses in pulmonary influenza infection. J Infect Dis 2011; 204: 592-600.
    • (2011) J Infect Dis , vol.204 , pp. 592-600
    • Gong, D.1    Farley, K.2    White, M.3
  • 7
    • 79251534355 scopus 로고    scopus 로고
    • CCR2-antagonist prophylaxis reduces pulmonary immune pathology and markedly improves survival during influenza infection
    • Lin KL, Sweeney S, Kang BD, et al. CCR2-antagonist prophylaxis reduces pulmonary immune pathology and markedly improves survival during influenza infection. J Immunol 2011; 186: 508-515.
    • (2011) J Immunol , vol.186 , pp. 508-515
    • Lin, K.L.1    Sweeney, S.2    Kang, B.D.3
  • 8
    • 42149083307 scopus 로고    scopus 로고
    • CCR2 + monocyte-derived dendritic cells and exudate macrophages produce influenza-induced pulmonary immune pathology and mortality
    • Lin KL, Suzuki Y, Nakano H, et al. CCR2 + monocyte-derived dendritic cells and exudate macrophages produce influenza-induced pulmonary immune pathology and mortality. J Immunol 2008; 180: 2562-2572.
    • (2008) J Immunol , vol.180 , pp. 2562-2572
    • Lin, K.L.1    Suzuki, Y.2    Nakano, H.3
  • 9
    • 62549085229 scopus 로고    scopus 로고
    • Early and sustained innate immune response defines pathology and death in nonhuman primates infected by highly pathogenic influenza virus
    • Baskin CR, Bielefeldt-Ohmann H, Tumpey TM, et al. Early and sustained innate immune response defines pathology and death in nonhuman primates infected by highly pathogenic influenza virus. Proc Natl Acad Sci U S A 2009; 106: 3455-3460.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3455-3460
    • Baskin, C.R.1    Bielefeldt-Ohmann, H.2    Tumpey, T.M.3
  • 10
    • 50849097044 scopus 로고    scopus 로고
    • H5N1 and 1918 pandemic influenza virus infection results in early and excessive infiltration of macrophages and neutrophils in the lungs of mice
    • Perrone LA, Plowden JK, Garcia-Sastre A, et al. H5N1 and 1918 pandemic influenza virus infection results in early and excessive infiltration of macrophages and neutrophils in the lungs of mice. PLOS Pathog 2008; 4: e1000115-e1000115.
    • (2008) PLOS Pathog , vol.4 , pp. e1000115-e1000115
    • Perrone, L.A.1    Plowden, J.K.2    Garcia-Sastre, A.3
  • 11
    • 33846265834 scopus 로고    scopus 로고
    • Aberrant innate immune response in lethal infection of macaques with the 1918 influenza virus
    • Kobasa D, Jones SM, Shinya K, et al. Aberrant innate immune response in lethal infection of macaques with the 1918 influenza virus. Nature 2007; 445: 319-323.
    • (2007) Nature , vol.445 , pp. 319-323
    • Kobasa, D.1    Jones, S.M.2    Shinya, K.3
  • 12
    • 27744598497 scopus 로고    scopus 로고
    • Pathogenicity of influenza viruses with genes from the 1918 pandemic virus: Functional roles of alveolar macrophages and neutrophils in limiting virus replication and mortality in mice
    • Tumpey TM, Garcia-Sastre A, Taubenberger JK, et al. Pathogenicity of influenza viruses with genes from the 1918 pandemic virus: functional roles of alveolar macrophages and neutrophils in limiting virus replication and mortality in mice. J Virol 2005; 79: 14933-14944.
    • (2005) J Virol , vol.79 , pp. 14933-14944
    • Tumpey, T.M.1    Garcia-Sastre, A.2    Taubenberger, J.K.3
  • 13
    • 65249145291 scopus 로고    scopus 로고
    • TNF-A /iNOS-producing dendritic cells are the necessary evil of lethal influenza virus infection
    • Aldridge JR Jr., Moseley CE, Boltz DA, et al. TNF-A /iNOS-producing dendritic cells are the necessary evil of lethal influenza virus infection. Proc Natl Acad Sci U S A 2009; 106: 5306-5311.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5306-5311
    • Aldridge, J.R.1    Moseley, C.E.2    Boltz, D.A.3
  • 14
    • 3142765421 scopus 로고    scopus 로고
    • Cutting edge: Pulmonary immunopathology mediated by antigen-specific expression of TNF-A -alpha by antiviral CD8 + T cells
    • Xu L, Yoon H, Zhao MQ, et al. Cutting edge: pulmonary immunopathology mediated by antigen-specific expression of TNF-A -alpha by antiviral CD8 + T cells. J Immunol 2004; 173: 721-725.
    • (2004) J Immunol , vol.173 , pp. 721-725
    • Xu, L.1    Yoon, H.2    Zhao, M.Q.3
  • 15
    • 0034807183 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor reduces the severity of virus-specific lung immunopathology
    • Hussell T, Pennycook A, Openshaw PJ,. Inhibition of tumor necrosis factor reduces the severity of virus-specific lung immunopathology. Eur J Immunol 2001; 31: 2566-2573.
    • (2001) Eur J Immunol , vol.31 , pp. 2566-2573
    • Hussell, T.1    Pennycook, A.2    Openshaw, P.J.3
  • 16
    • 0032005791 scopus 로고    scopus 로고
    • Local and systemic cytokine response during experimental human influenza A virus infection
    • Hayden F, Fritz R, Lobo M, et al. Local and systemic cytokine response during experimental human influenza A virus infection. J Clin Invest 1998; 101: 643-649.
    • (1998) J Clin Invest , vol.101 , pp. 643-649
    • Hayden, F.1    Fritz, R.2    Lobo, M.3
  • 17
    • 77953296297 scopus 로고    scopus 로고
    • Role of surfactant protein A and D (SP-A and SP-D) in human antiviral host defense
    • Hartshorn KL,. Role of surfactant protein A and D (SP-A and SP-D) in human antiviral host defense. Front Biosci (Schol Ed) 2010; 2: 527-546.
    • (2010) Front Biosci (Schol Ed) , vol.2 , pp. 527-546
    • Hartshorn, K.L.1
  • 18
    • 78650412747 scopus 로고    scopus 로고
    • Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza A virus infection
    • Chang WC, White MR, Moyo P, et al. Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza A virus infection. BMC Immunol 2010; 11: 64-64.
    • (2010) BMC Immunol , vol.11 , pp. 64
    • Chang, W.C.1    White, M.R.2    Moyo, P.3
  • 19
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: Evidence from influenza virus infection of mice
    • Reading PC, Morey LS, Crouch EC, Anders EM,. Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice. J Virol 1997; 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
  • 20
    • 3543125873 scopus 로고    scopus 로고
    • Pulmonary collectins modulate strain-specific influenza a virus infection and host responses
    • Hawgood S, Brown C, Edmondson J, et al. Pulmonary collectins modulate strain-specific influenza a virus infection and host responses. J Virol 2004; 78: 8565-8572.
    • (2004) J Virol , vol.78 , pp. 8565-8572
    • Hawgood, S.1    Brown, C.2    Edmondson, J.3
  • 21
    • 0036008399 scopus 로고    scopus 로고
    • Surfactant protein-A-deficient mice display an exaggerated early inflammatory response to a beta-resistant strain of influenza A virus
    • Li G, Siddiqui J, Hendry M, et al. Surfactant protein-A-deficient mice display an exaggerated early inflammatory response to a beta-resistant strain of influenza A virus. Am J Respir Cell Mol Biol 2002; 26: 277-282.
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 277-282
    • Li, G.1    Siddiqui, J.2    Hendry, M.3
  • 22
    • 84927724692 scopus 로고    scopus 로고
    • Does a personal or family history of malignancy preclude the use of immunomodulators and biologics in IBD
    • Kalman RS, Hartshorn K, Farraye FA,. Does a personal or family history of malignancy preclude the use of immunomodulators and biologics in IBD. Inflamm Bowel Dis 2015; 21: 428-435.
    • (2015) Inflamm Bowel Dis , vol.21 , pp. 428-435
    • Kalman, R.S.1    Hartshorn, K.2    Farraye, F.A.3
  • 23
    • 0036081072 scopus 로고    scopus 로고
    • Absence of SP-A modulates innate and adaptive defense responses to pulmonary influenza infection
    • LeVine AM, Hartshorn K, Elliott J, et al. Absence of SP-A modulates innate and adaptive defense responses to pulmonary influenza infection. Am J Physiol Lung Cell Mol Physiol 2002; 282: L563-L572.
    • (2002) Am J Physiol Lung Cell Mol Physiol , vol.282 , pp. L563-L572
    • LeVine, A.M.1    Hartshorn, K.2    Elliott, J.3
  • 24
    • 0035889906 scopus 로고    scopus 로고
    • Surfactant protein D enhances clearance of influenza A virus from the lung in vivo
    • LeVine AM, Whitsett JA, Hartshorn KL, et al. Surfactant protein D enhances clearance of influenza A virus from the lung in vivo. J Immunol 2001; 167: 5868-5873.
    • (2001) J Immunol , vol.167 , pp. 5868-5873
    • LeVine, A.M.1    Whitsett, J.A.2    Hartshorn, K.L.3
  • 25
    • 33646701901 scopus 로고    scopus 로고
    • Surfactant protein D in human lung diseases
    • Hartl D, Griese M,. Surfactant protein D in human lung diseases. Eur J Clin Invest 2006; 36: 423-435.
    • (2006) Eur J Clin Invest , vol.36 , pp. 423-435
    • Hartl, D.1    Griese, M.2
  • 26
    • 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, Chen H, Wang F, et al. L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo. J Innate Immun 2012; 4: 312-324.
    • (2012) J Innate Immun , vol.4 , pp. 312-324
    • Pan, Q.1    Chen, H.2    Wang, F.3
  • 27
    • 84865404380 scopus 로고    scopus 로고
    • Human H-ficolin inhibits replication of seasonal and pandemic influenza A viruses
    • Verma A, White M, Vathipadiekal V, et al. Human H-ficolin inhibits replication of seasonal and pandemic influenza A viruses. J Immunol 2012; 189: 2478-2487.
    • (2012) J Immunol , vol.189 , pp. 2478-2487
    • Verma, A.1    White, M.2    Vathipadiekal, V.3
  • 28
    • 0028338939 scopus 로고
    • Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses
    • Hartshorn KL, Crouch EC, White MR, et al. Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses. J Clin Invest 1994; 94: 311-319.
    • (1994) J Clin Invest , vol.94 , pp. 311-319
    • Hartshorn, K.L.1    Crouch, E.C.2    White, M.R.3
  • 29
    • 67449161588 scopus 로고    scopus 로고
    • Immunodeficiency associated with FCN3 mutation and ficolin-3 deficiency
    • Munthe-Fog L, Hummelshoj T, Honore C, et al. Immunodeficiency associated with FCN3 mutation and ficolin-3 deficiency. N Engl J Med 2009; 360: 2637-2644.
    • (2009) N Engl J Med , vol.360 , pp. 2637-2644
    • Munthe-Fog, L.1    Hummelshoj, T.2    Honore, C.3
  • 30
  • 31
    • 84871300505 scopus 로고    scopus 로고
    • The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins
    • Tripathi S, Tecle T, Verma A, et al. The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins. J Gen Virol 2013; 94: 40-49.
    • (2013) J Gen Virol , vol.94 , pp. 40-49
    • Tripathi, S.1    Tecle, T.2    Verma, A.3
  • 32
    • 80054841451 scopus 로고    scopus 로고
    • Antiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37
    • Barlow PG, Svoboda P, Mackellar A, et al. Antiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37. PLOS ONE 2011; 6: e25333-e25333.
    • (2011) PLOS ONE , vol.6 , pp. e25333-e25333
    • Barlow, P.G.1    Svoboda, P.2    Mackellar, A.3
  • 33
    • 67649160595 scopus 로고    scopus 로고
    • Interactions of alpha-, beta-, and theta-defensins with influenza A virus and surfactant protein D
    • Doss M, White MR, Tecle T, et al. Interactions of alpha-, beta-, and theta-defensins with influenza A virus and surfactant protein D. J Immunol 2009; 182: 7878-7887.
    • (2009) J Immunol , vol.182 , pp. 7878-7887
    • Doss, M.1    White, M.R.2    Tecle, T.3
  • 34
    • 34548480179 scopus 로고    scopus 로고
    • Alpha-Defensin inhibits influenza virus replication by cell-mediated mechanism(s)
    • Salvatore M, Garcia-Sastre A, Ruchala P, et al. alpha-Defensin inhibits influenza virus replication by cell-mediated mechanism(s). J Infect Dis 2007; 196: 835-843.
    • (2007) J Infect Dis , vol.196 , pp. 835-843
    • Salvatore, M.1    Garcia-Sastre, A.2    Ruchala, P.3
  • 35
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: An observation study
    • Putsep K, Carlsson G, Boman HG, Andersson M,. Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 2002; 360: 1144-1149.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 36
    • 0029903353 scopus 로고    scopus 로고
    • Interactions of recombinant human pulmonary surfactant protein D and SP-D multimers with influenza A
    • Hartshorn K, Chang D, Rust K, et al. Interactions of recombinant human pulmonary surfactant protein D and SP-D multimers with influenza A. Am J Physiol 1996; 271: L753-L762.
    • (1996) Am J Physiol , vol.271 , pp. L753-L762
    • Hartshorn, K.1    Chang, D.2    Rust, K.3
  • 37
    • 71849086029 scopus 로고    scopus 로고
    • Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus
    • White M, Kingma P, Tecle T, et al. Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus. J Immunol 2008; 181: 7936-7943.
    • (2008) J Immunol , vol.181 , pp. 7936-7943
    • White, M.1    Kingma, P.2    Tecle, T.3
  • 38
    • 33747661710 scopus 로고    scopus 로고
    • Correction of pulmonary abnormalities in Sftpd-/- mice requires the collagenous domain of surfactant protein D
    • Kingma PS, Zhang L, Ikegami M, et al. Correction of pulmonary abnormalities in Sftpd-/- mice requires the collagenous domain of surfactant protein D. J Biol Chem 2006; 281: 24496-24505.
    • (2006) J Biol Chem , vol.281 , pp. 24496-24505
    • Kingma, P.S.1    Zhang, L.2    Ikegami, M.3
  • 39
    • 84858065747 scopus 로고    scopus 로고
    • Studies of the pattern recognition molecule H-ficolin: Specificity and purification
    • Zacho RM, Jensen L, Terp R, et al. Studies of the pattern recognition molecule H-ficolin: specificity and purification. J Biol Chem 2012; 287: 8071-8081.
    • (2012) J Biol Chem , vol.287 , pp. 8071-8081
    • Zacho, R.M.1    Jensen, L.2    Terp, R.3
  • 40
    • 77955283062 scopus 로고    scopus 로고
    • A novel L-ficolin/mannose-binding lectin chimeric molecule with enhanced activity against Ebola virus
    • Michelow IC, Dong M, Mungall BA, et al. A novel L-ficolin/mannose-binding lectin chimeric molecule with enhanced activity against Ebola virus. J Biol Chem 2010; 285: 24729-24739.
    • (2010) J Biol Chem , vol.285 , pp. 24729-24739
    • Michelow, I.C.1    Dong, M.2    Mungall, B.A.3
  • 41
    • 0023785810 scopus 로고
    • Effects of influenza A virus on human neutrophil calcium metabolism
    • Hartshorn KL, Collamer M, Auerbach M, et al. Effects of influenza A virus on human neutrophil calcium metabolism. J Immunol 1988; 141: 1295-1301.
    • (1988) J Immunol , vol.141 , pp. 1295-1301
    • Hartshorn, K.L.1    Collamer, M.2    Auerbach, M.3
  • 42
    • 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, Kash JC, Dugan VG, et al. The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding. Virology 2011; 412: 426-434.
    • (2011) Virology , vol.412 , pp. 426-434
    • Qi, L.1    Kash, J.C.2    Dugan, V.G.3
  • 43
    • 0031416787 scopus 로고    scopus 로고
    • Mechanisms of anti-influenza activity of surfactant proteins A and D: Comparison with serum collectins
    • Hartshorn KL, White MR, Shepherd V, Reid K, Jensenius JC, Crouch EC,. Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins. Am J Physiol 1997; 273: L1156-L1166.
    • (1997) Am J Physiol , vol.273 , pp. L1156-L1166
    • Hartshorn, K.L.1    White, M.R.2    Shepherd, V.3    Reid, K.4    Jensenius, J.C.5    Crouch, E.C.6
  • 44
    • 84901702029 scopus 로고    scopus 로고
    • Mutations flanking the carbohydrate binding site of surfactant protein D confer antiviral activity for pandemic influenza A viruses
    • Nikolaidis NM, White MR, Allen K, et al. Mutations flanking the carbohydrate binding site of surfactant protein D confer antiviral activity for pandemic influenza A viruses. Am J Physiol Lung Cell Mol Physiol 2014; 306: L1036-L1044.
    • (2014) Am J Physiol Lung Cell Mol Physiol , vol.306 , pp. L1036-L1044
    • Nikolaidis, N.M.1    White, M.R.2    Allen, K.3
  • 45
    • 81755181696 scopus 로고    scopus 로고
    • Mutagenesis of surfactant protein D informed by evolution and x-ray crystallography enhances defenses against influenza A virus in vivo
    • Crouch E, Nikolaidis N, McCormack FX, et al. Mutagenesis of surfactant protein D informed by evolution and x-ray crystallography enhances defenses against influenza A virus in vivo. J Biol Chem 2011; 286: 40681-40692.
    • (2011) J Biol Chem , vol.286 , pp. 40681-40692
    • Crouch, E.1    Nikolaidis, N.2    McCormack, F.X.3
  • 46
    • 65249118801 scopus 로고    scopus 로고
    • Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: Contributions of an extended site and residue 343
    • Crouch E, Hartshorn K, Horlacher T, et al. Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: contributions of an extended site and residue 343. Biochemistry 2009; 48: 3335-3345.
    • (2009) Biochemistry , vol.48 , pp. 3335-3345
    • Crouch, E.1    Hartshorn, K.2    Horlacher, T.3
  • 47
    • 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 WC, Hartshorn KL, White MR, et al. 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 2011; 81: 388-395.
    • (2011) Biochem Pharmacol , vol.81 , pp. 388-395
    • Chang, W.C.1    Hartshorn, K.L.2    White, M.R.3
  • 48
    • 84888197645 scopus 로고    scopus 로고
    • Efficacy of recombinant chimeric lectins, consisting of mannose binding lectin and L-ficolin, against influenza A viral infection in mouse model study
    • Takahashi K, Moyo P, Chigweshe L, et al. Efficacy of recombinant chimeric lectins, consisting of mannose binding lectin and L-ficolin, against influenza A viral infection in mouse model study. Virus Res 2013; 178: 495-501.
    • (2013) Virus Res , vol.178 , pp. 495-501
    • Takahashi, K.1    Moyo, P.2    Chigweshe, L.3
  • 49
    • 84908302078 scopus 로고    scopus 로고
    • LL-37 modulates human neutrophil responses to influenza A virus
    • Tripathi S, Verma A, Kim EJ, et al. LL-37 modulates human neutrophil responses to influenza A virus. J Leukoc Biol 2014; 96: 931-938.
    • (2014) J Leukoc Biol , vol.96 , pp. 931-938
    • Tripathi, S.1    Verma, A.2    Kim, E.J.3
  • 50
    • 84888628250 scopus 로고    scopus 로고
    • Molecular mechanisms of inhibition of influenza by surfactant protein d revealed by large-scale molecular dynamics simulation
    • Goh BC, Rynkiewicz MJ, Cafarella TR, et al. Molecular mechanisms of inhibition of influenza by surfactant protein d revealed by large-scale molecular dynamics simulation. Biochemistry 2013; 52: 8527-8538.
    • (2013) Biochemistry , vol.52 , pp. 8527-8538
    • Goh, B.C.1    Rynkiewicz, M.J.2    Cafarella, T.R.3
  • 51
    • 84861853797 scopus 로고    scopus 로고
    • Interleukin-6 is a potential biomarker for severe pandemic H1N1 influenza A infection
    • Paquette SG, Banner D, Zhao Z, et al. Interleukin-6 is a potential biomarker for severe pandemic H1N1 influenza A infection. PLOS ONE 2012; 7: e38214-e38214.
    • (2012) PLOS ONE , vol.7 , pp. e38214-e38214
    • Paquette, S.G.1    Banner, D.2    Zhao, Z.3
  • 52
    • 79955527970 scopus 로고    scopus 로고
    • Host defense peptide LL-37 selectively reduces proinflammatory macrophage responses
    • Brown KL, Poon GF, Birkenhead D, et al. Host defense peptide LL-37 selectively reduces proinflammatory macrophage responses. J Immunol 2011; 186: 5497-5505.
    • (2011) J Immunol , vol.186 , pp. 5497-5505
    • Brown, K.L.1    Poon, G.F.2    Birkenhead, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.