메뉴 건너뛰기




Volumn 6, Issue 3, 2014, Pages 1294-1316

Playing hide and seek: How glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection

Author keywords

Glycosylation; Immune evasion; Influenza virus; Lectin

Indexed keywords

EPITOPE; GLYCAN; HN PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ; LECTIN; MANNOSE BINDING LECTIN; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE; NEUTRALIZING ANTIBODY; OLIGOSACCHARIDE; SURFACTANT ASSOCIATED PROTEIN;

EID: 84897878395     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v6031294     Document Type: Review
Times cited : (230)

References (128)
  • 1
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R.; Kornfeld, S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 1985, 54, 631-664.
    • (1985) Annu. Rev. Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 2
    • 0022367414 scopus 로고
    • Oligosaccharide composition of an influenza virus hemagglutinin with host-determined binding properties
    • Deom, C.M.; Schulze, I.T. Oligosaccharide composition of an influenza virus hemagglutinin with host-determined binding properties. J. Biol. Chem. 1985, 260, 14771-14774.
    • (1985) J. Biol. Chem , vol.260 , pp. 14771-14774
    • Deom, C.M.1    Schulze, I.T.2
  • 3
    • 0018397745 scopus 로고
    • Host cell- and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza a viruses
    • Nakamura, K.; Compans, R.W. Host cell- and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza a viruses. Virology 1979, 95, 8-23.
    • (1979) Virology , vol.95 , pp. 8-23
    • Nakamura, K.1    Compans, R.W.2
  • 4
    • 0019350307 scopus 로고
    • Glycosylation sites of influenza viral glycoproteins: Characterization of tryptic glycopeptides from the a/ussr(h1n1) hemagglutinin glycoprotein
    • Basak, S.; Pritchard, D.G.; Bhown, A.S.; Compans, R.W. Glycosylation sites of influenza viral glycoproteins: Characterization of tryptic glycopeptides from the a/ussr(h1n1) hemagglutinin glycoprotein. J. Virol. 1981, 37, 549-558.
    • (1981) J. Virol , vol.37 , pp. 549-558
    • Basak, S.1    Pritchard, D.G.2    Bhown, A.S.3    Compans, R.W.4
  • 5
    • 0019864105 scopus 로고
    • Amino acid sequence and oligosaccharide distribution of the haemagglutinin from an early hong kong influenza virus variant a/aichi/2/68 (x-31)
    • Ward, C.W.; Dopheide, T.A. Amino acid sequence and oligosaccharide distribution of the haemagglutinin from an early hong kong influenza virus variant a/aichi/2/68 (x-31). Biochem. J. 1981, 193, 953-962.
    • (1981) Biochem. J , vol.193 , pp. 953-962
    • Ward, C.W.1    Dopheide, T.A.2
  • 6
    • 0016529818 scopus 로고
    • Incorporation of sulfate into influenza virus glycoproteins
    • Compans, R.W.; Pinter, A. Incorporation of sulfate into influenza virus glycoproteins. Virology 1975, 66, 151-160.
    • (1975) Virology , vol.66 , pp. 151-160
    • Compans, R.W.1    Pinter, A.2
  • 7
    • 0032007892 scopus 로고    scopus 로고
    • Sulphation of n-linked oligosaccharides of vesicular stomatitis and influenza virus envelope glycoproteins: Host cell specificity, subcellular localization and identification of substituted saccharides
    • Karaivanova, V.K.; Spiro, R.G. Sulphation of n-linked oligosaccharides of vesicular stomatitis and influenza virus envelope glycoproteins: Host cell specificity, subcellular localization and identification of substituted saccharides. Biochem. J. 1998, 329, 511-518.
    • (1998) Biochem. J , vol.329 , pp. 511-518
    • Karaivanova, V.K.1    Spiro, R.G.2
  • 8
    • 0032943114 scopus 로고    scopus 로고
    • Strain-specific differences in the effect of influenza a virus neuraminidase on vector-expressed hemagglutinin
    • Kaverin, N.V.; Klenk, H.D. Strain-specific differences in the effect of influenza a virus neuraminidase on vector-expressed hemagglutinin. Arch. Virol. 1999, 144, 781-786.
    • (1999) Arch. Virol , vol.144 , pp. 781-786
    • Kaverin, N.V.1    Klenk, H.D.2
  • 9
    • 0021932646 scopus 로고
    • Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase
    • Basak, S.; Tomana, M.; Compans, R.W. Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase. Virus Res. 1985, 2, 61-68.
    • (1985) Virus Res , vol.2 , pp. 61-68
    • Basak, S.1    Tomana, M.2    Compans, R.W.3
  • 10
    • 84874270957 scopus 로고    scopus 로고
    • Addition of glycosylation to influenza a virus hemagglutinin modulates antibody-mediated recognition of h1n1 2009 pandemic viruses
    • Job, E.R.; Deng, Y.M.; Barfod, K.K.; Tate, M.D.; Caldwell, N.; Reddiex, S.; Maurer-Stroh, S.; Brooks, A.G.; Reading, P.C. Addition of glycosylation to influenza a virus hemagglutinin modulates antibody-mediated recognition of h1n1 2009 pandemic viruses. J. Immunol. 2013, 190, 2169-2177.
    • (2013) J. Immunol , vol.190 , pp. 2169-2177
    • Job, E.R.1    Deng, Y.M.2    Barfod, K.K.3    Tate, M.D.4    Caldwell, N.5    Reddiex, S.6    Maurer-Stroh, S.7    Brooks, A.G.8    Reading, P.C.9
  • 11
    • 65249188741 scopus 로고    scopus 로고
    • Targeted n-linked glycosylation analysis of h5n1 influenza hemagglutinin by selective sample preparation and liquid chromatography/tandem mass spectrometry
    • Blake, T.A.; Williams, T.L.; Pirkle, J.L.; Barr, J.R. Targeted n-linked glycosylation analysis of h5n1 influenza hemagglutinin by selective sample preparation and liquid chromatography/tandem mass spectrometry. Anal. Chem. 2009, 81, 3109-3118.
    • (2009) Anal. Chem , vol.81 , pp. 3109-3118
    • Blake, T.A.1    Williams, T.L.2    Pirkle, J.L.3    Barr, J.R.4
  • 12
    • 0029041308 scopus 로고
    • The hydroxy amino acid in an asn-x-ser/thr sequon can influence n-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein
    • Kasturi, L.; Eshleman, J.R.; Wunner, W.H.; Shakin-Eshleman, S.H. The hydroxy amino acid in an asn-x-ser/thr sequon can influence n-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein. J. Biol. Chem. 1995, 270, 14756-14761.
    • (1995) J. Biol. Chem , vol.270 , pp. 14756-14761
    • Kasturi, L.1    Eshleman, J.R.2    Wunner, W.H.3    Shakin-Eshleman, S.H.4
  • 13
    • 0032510739 scopus 로고    scopus 로고
    • The amino acid following an asn-x-ser/thr sequon is an important determinant of n-linked core glycosylation efficiency
    • Mellquist, J.L.; Kasturi, L.; Spitalnik, S.L.; Shakin-Eshleman, S.H. The amino acid following an asn-x-ser/thr sequon is an important determinant of n-linked core glycosylation efficiency. Biochemistry 1998, 37, 6833-6837.
    • (1998) Biochemistry , vol.37 , pp. 6833-6837
    • Mellquist, J.L.1    Kasturi, L.2    Spitalnik, S.L.3    Shakin-Eshleman, S.H.4
  • 14
    • 79960872741 scopus 로고    scopus 로고
    • Glycosylation site alteration in the evolution of influenza a (h1n1) viruses
    • Sun, S.; Wang, Q.; Zhao, F.; Chen, W.; Li, Z. Glycosylation site alteration in the evolution of influenza a (h1n1) viruses. PLoS One 2011, 6, e22844.
    • (2011) PLoS One , vol.6
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 15
    • 4444376554 scopus 로고    scopus 로고
    • Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza a/h3n2 virus hemagglutinin
    • Abe, Y.; Takashita, E.; Sugawara, K.; Matsuzaki, Y.; Muraki, Y.; Hongo, S. Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza a/h3n2 virus hemagglutinin. J. Virol. 2004, 78, 9605-9611.
    • (2004) J. Virol , vol.78 , pp. 9605-9611
    • Abe, Y.1    Takashita, E.2    Sugawara, K.3    Matsuzaki, Y.4    Muraki, Y.5    Hongo, S.6
  • 16
    • 0030740376 scopus 로고    scopus 로고
    • Effects of glycosylation on the properties and functions of influenza virus hemagglutinin
    • Schulze, I.T. Effects of glycosylation on the properties and functions of influenza virus hemagglutinin. J. Infect. Dis. 1997, 176, S24-S28.
    • (1997) J. Infect. Dis , vol.176
    • Schulze, I.T.1
  • 17
    • 0033934134 scopus 로고    scopus 로고
    • Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: A study by reverse genetics
    • Wagner, R.; Wolff, T.; Herwig, A.; Pleschka, S.; Klenk, H.D. Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: A study by reverse genetics. J. Virol. 2000, 74, 6316-6323.
    • (2000) J. Virol , vol.74 , pp. 6316-6323
    • Wagner, R.1    Wolff, T.2    Herwig, A.3    Pleschka, S.4    Klenk, H.D.5
  • 18
    • 0027238117 scopus 로고
    • Role of conserved glycosylation sites in maturation and transport of influenza a virus hemagglutinin
    • Roberts, P.C.; Garten, W.; Klenk, H.D. Role of conserved glycosylation sites in maturation and transport of influenza a virus hemagglutinin. J. Virol. 1993, 67, 3048-3060.
    • (1993) J. Virol , vol.67 , pp. 3048-3060
    • Roberts, P.C.1    Garten, W.2    Klenk, H.D.3
  • 19
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels, R.; Kurowski, B.; Johnson, A.E.; Hebert, D.N. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell 2003, 11, 79-90.
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 20
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza a viruses
    • Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; Nakajima, K. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza a viruses. Virology 1991, 182, 475-485.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 21
    • 0030940057 scopus 로고    scopus 로고
    • Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity
    • Ohuchi, R.; Ohuchi, M.; Garten, W.; Klenk, H.D. Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity. J. Virol. 1997, 71, 3719-3725.
    • (1997) J. Virol , vol.71 , pp. 3719-3725
    • Ohuchi, R.1    Ohuchi, M.2    Garten, W.3    Klenk, H.D.4
  • 22
    • 0026489261 scopus 로고
    • Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus
    • Gallagher, P.J.; Henneberry, J.M.; Sambrook, J.F.; Gething, M.J. Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus. J. Virol. 1992, 66, 7136-7145.
    • (1992) J. Virol , vol.66 , pp. 7136-7145
    • Gallagher, P.J.1    Henneberry, J.M.2    Sambrook, J.F.3    Gething, M.J.4
  • 23
    • 44449115278 scopus 로고    scopus 로고
    • Changing selective pressure during antigenic changes in human influenza h3
    • Blackburne, B.P.; Hay, A.J.; Goldstein, R.A. Changing selective pressure during antigenic changes in human influenza h3. PLoS Pathog. 2008, 4, e1000058.
    • (2008) PLoS Pathog , vol.4
    • Blackburne, B.P.1    Hay, A.J.2    Goldstein, R.A.3
  • 24
    • 79251508720 scopus 로고    scopus 로고
    • Evolutionary dynamics of n-glycosylation sites of influenza virus hemagglutinin
    • RRN1001
    • Cherry, J.L.; Lipman, D.J.; Nikolskaya, A.; Wolf, Y.I. Evolutionary dynamics of n-glycosylation sites of influenza virus hemagglutinin. PLoS Curr. Influenza 2009, RRN1001.
    • (2009) PLoS Curr. Influenza
    • Cherry, J.L.1    Lipman, D.J.2    Nikolskaya, A.3    Wolf, Y.I.4
  • 25
    • 79251480393 scopus 로고    scopus 로고
    • Glycosylation focuses sequence variation in the influenza a virus h1 hemagglutinin globular domain
    • Das, S.R.; Puigbo, P.; Hensley, S.E.; Hurt, D.E.; Bennink, J.R.; Yewdell, J.W. Glycosylation focuses sequence variation in the influenza a virus h1 hemagglutinin globular domain. PLoS Pathog. 2010, 6, e1001211.
    • (2010) PLoS Pathog , vol.6
    • Das, S.R.1    Puigbo, P.2    Hensley, S.E.3    Hurt, D.E.4    Bennink, J.R.5    Yewdell, J.W.6
  • 26
    • 44649136618 scopus 로고    scopus 로고
    • Genetically destined potentials for n-linked glycosylation of influenza virus hemagglutinin
    • Igarashi, M.; Ito, K.; Kida, H.; Takada, A. Genetically destined potentials for n-linked glycosylation of influenza virus hemagglutinin. Virology 2008, 376, 323-329.
    • (2008) Virology , vol.376 , pp. 323-329
    • Igarashi, M.1    Ito, K.2    Kida, H.3    Takada, A.4
  • 27
    • 9744280420 scopus 로고    scopus 로고
    • Tracking global patterns of n-linked glycosylation site variation in highly variable viral glycoproteins: Hiv, siv, and hcv envelopes and influenza hemagglutinin
    • Zhang, M.; Gaschen, B.; Blay, W.; Foley, B.; Haigwood, N.; Kuiken, C.; Korber, B. Tracking global patterns of n-linked glycosylation site variation in highly variable viral glycoproteins: Hiv, siv, and hcv envelopes and influenza hemagglutinin. Glycobiology 2004, 14, 1229-1246.
    • (2004) Glycobiology , vol.14 , pp. 1229-1246
    • Zhang, M.1    Gaschen, B.2    Blay, W.3    Foley, B.4    Haigwood, N.5    Kuiken, C.6    Korber, B.7
  • 28
    • 80455168614 scopus 로고    scopus 로고
    • Why do influenza virus subtypes die out? A hypothesis
    • Palese, P.; Wang, T.T. Why do influenza virus subtypes die out? A hypothesis. MBio 2011, 2, e00150-e00151.
    • (2011) MBio , vol.2
    • Palese, P.1    Wang, T.T.2
  • 29
    • 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.; Deng, Y.M.; Tate, M.D.; Bottazzi, B.; Crouch, E.C.; Dean, M.M.; Mantovani, A.; Brooks, A.G.; Reading, P.C. Pandemic h1n1 influenza a viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies. J. Immunol. 2010, 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
  • 34
    • 0036255966 scopus 로고    scopus 로고
    • Effect of addition of new oligosaccharide chains to the globular head of influenza a/h2n2 virus haemagglutinin on the intracellular transport and biological activities of the molecule
    • Tsuchiya, E.; Sugawara, K.; Hongo, S.; Matsuzaki, Y.; Muraki, Y.; Li, Z.N.; Nakamura, K. Effect of addition of new oligosaccharide chains to the globular head of influenza a/h2n2 virus haemagglutinin on the intracellular transport and biological activities of the molecule. J. Gen. Virol. 2002, 83, 1137-1146.
    • (2002) J. Gen. Virol , vol.83 , pp. 1137-1146
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3    Matsuzaki, Y.4    Muraki, Y.5    Li, Z.N.6    Nakamura, K.7
  • 35
    • 84897876723 scopus 로고    scopus 로고
    • NetNGlyc. Available online, accessed on 14 November
    • NetNGlyc. Available online: http://www.cbs.dtu.dk/services/NetNGlyc/ (accessed on 14 November 2013).
    • (2013)
  • 36
    • 84897847506 scopus 로고    scopus 로고
    • Glyprot. Available online, accessed on 4 December
    • Glyprot. Available online: http://ww.glycosciences.de/modeling/glyprot/ (accessed on 4 December 2013).
    • (2013)
  • 37
    • 85164749093 scopus 로고    scopus 로고
    • Persistence of Vision Raytracer, version 3.7, Victoria, Australia, 2004. Available online, accessed on 4 December
    • Persistence of Vision Raytracer, version 3.7; Persistence of Vision Pty. Ltd: Williamstown, Victoria, Australia, 2004. Available online: http://www.povray.org/ (accessed on 4 December 2013).
    • (2013) Persistence of Vision Pty. Ltd: Williamstown
  • 38
    • 84868319844 scopus 로고    scopus 로고
    • The evolutionary pattern of glycosylation sites in influenza virus (h5n1) hemagglutinin and neuraminidase
    • Chen, W.; Zhong, Y.; Qin, Y.; Sun, S.; Li, Z. The evolutionary pattern of glycosylation sites in influenza virus (h5n1) hemagglutinin and neuraminidase. PLoS One 2012, 7, e49224.
    • (2012) PLoS One , vol.7
    • Chen, W.1    Zhong, Y.2    Qin, Y.3    Sun, S.4    Li, Z.5
  • 41
    • 0012464505 scopus 로고
    • Glycoproteins as influenza virus hemagglutinin inhibitors and as cellular receptors
    • Gottschalk, A., Ed.; Elsevier Science Publishing: New York, NY, USA
    • Gottschalk, A.; Belyavin, G.; Biddle, F. Glycoproteins as influenza virus hemagglutinin inhibitors and as cellular receptors. In Glycoproteins. Their Composition, Structure and Function; Gottschalk, A., Ed.; Elsevier Science Publishing: New York, NY, USA,1972; pp. 1082-1096.
    • (1972) In Glycoproteins. their Composition, Structure and Function , pp. 1082-1096
    • Gottschalk, A.1    Belyavin, G.2    Biddle, F.3
  • 42
    • 84862271837 scopus 로고    scopus 로고
    • Soluble host defense lectins in innate immunity to influenza virus
    • Ng, W.C.; Tate, M.D.; Brooks, A.G.; Reading, P.C. Soluble host defense lectins in innate immunity to influenza virus. J. Biomed. Biotechnol. 2012, 2012, 732191.
    • (2191) J. Biomed. Biotechnol , vol.2012 , Issue.73 , pp. 2012
    • Ng, W.C.1    Tate, M.D.2    Brooks, A.G.3    Reading, P.C.4
  • 43
    • 0025298243 scopus 로고
    • Bovine and mouse serum beta inhibitors of influenza a viruses are mannose-binding lectins
    • Anders, E.M.; Hartley, C.A.; Jackson, D.C. Bovine and mouse serum beta inhibitors of influenza a viruses are mannose-binding lectins. Proc. Natl. Acad. Sci. USA 1990, 87, 4485-4489.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4485-4489
    • Anders, E.M.1    Hartley, C.A.2    Jackson, D.C.3
  • 44
    • 0026653795 scopus 로고
    • Two distinct serum mannose-binding lectins function as beta inhibitors of influenza virus: Identification of bovine serum beta inhibitor as conglutinin
    • Hartley, C.A.; Jackson, D.C.; Anders, E.M. Two distinct serum mannose-binding lectins function as beta inhibitors of influenza virus: Identification of bovine serum beta inhibitor as conglutinin. J. Virol. 1992, 66, 4358-4363.
    • (1992) J. Virol , vol.66 , pp. 4358-4363
    • Hartley, C.A.1    Jackson, D.C.2    Anders, E.M.3
  • 45
    • 0032860314 scopus 로고    scopus 로고
    • C-type lectin-like domains
    • Drickamer, K. C-type lectin-like domains. Curr. Opin. Struct. Biol. 1999, 9, 585-590.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 585-590
    • Drickamer, K.1
  • 46
    • 0032135111 scopus 로고    scopus 로고
    • Collectins and pulmonary host defense
    • Crouch, E.C. Collectins and pulmonary host defense. Am. J. Respir. Cell Mol. Biol. 1998, 19, 177-201.
    • (1998) Am. J. Respir. Cell Mol. Biol , vol.19 , pp. 177-201
    • Crouch, E.C.1
  • 47
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: Evidence from influenza virus infection of mice
    • Reading, P.C.; Morey, L.S.; Crouch, E.C.; Anders, E.M. 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
  • 48
    • 79953248363 scopus 로고    scopus 로고
    • Responses of mouse airway epithelial cells and alveolar macrophages to virulent and avirulent strains of influenza a virus
    • Tate, M.D.; Schilter, H.C.; Brooks, A.G.; Reading, P.C. Responses of mouse airway epithelial cells and alveolar macrophages to virulent and avirulent strains of influenza a virus. Viral. Immunol. 2011, 24, 77-88.
    • (2011) Viral. Immunol , vol.24 , pp. 77-88
    • Tate, M.D.1    Schilter, H.C.2    Brooks, A.G.3    Reading, P.C.4
  • 49
    • 79952814603 scopus 로고    scopus 로고
    • Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection
    • Tate, M.D.; Brooks, A.G.; Reading, P.C. Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection. Immunol. Cell Biol. 2011, 89, 482-491.
    • (2011) Immunol. Cell Biol , vol.89 , pp. 482-491
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 53
    • 0035889906 scopus 로고    scopus 로고
    • Surfactant protein d enhances clearance of influenza a virus from the lung in vivo
    • LeVine, A.M.; Whitsett, J.A.; Hartshorn, K.L.; Crouch, E.C.; Korfhagen, T.R. 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    Crouch, E.C.4    Korfhagen, T.R.5
  • 54
  • 56
    • 0037151086 scopus 로고    scopus 로고
    • Complementation of pulmonary abnormalities in sp-d(-/-) mice with an sp-d/conglutinin fusion protein
    • Zhang, L.; Hartshorn, K.L.; Crouch, E.C.; Ikegami, M.; Whitsett, J.A. Complementation of pulmonary abnormalities in sp-d(-/-) mice with an sp-d/conglutinin fusion protein. J. Biol. Chem. 2002, 277, 22453-22459.
    • (2002) J. Biol. Chem , vol.277 , pp. 22453-22459
    • Zhang, L.1    Hartshorn, K.L.2    Crouch, E.C.3    Ikegami, M.4    Whitsett, J.A.5
  • 57
    • 78650412747 scopus 로고    scopus 로고
    • Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza a virus infection
    • Chang, W.C.; White, M.R.; Moyo, P.; McClear, S.; Thiel, S.; Hartshorn, K.L.; Takahashi, K. Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza a virus infection. BMC Immunol. 2010, 11, 64.
    • (2010) BMC Immunol , vol.11 , pp. 64
    • Chang, W.C.1    White, M.R.2    Moyo, P.3    McClear, S.4    Thiel, S.5    Hartshorn, K.L.6    Takahashi, K.7
  • 60
    • 77953331970 scopus 로고    scopus 로고
    • Increasing antiviral activity of surfactant protein d trimers by introducing residues from bovine serum collectins: Dissociation of mannan-binding and antiviral activity
    • Hartshorn, K.L.; White, M.R.; Smith, K.; Sorensen, G.; Kuroki, Y.; Holmskov, U.; Head, J.; Crouch, E.C. Increasing antiviral activity of surfactant protein d trimers by introducing residues from bovine serum collectins: Dissociation of mannan-binding and antiviral activity. Scand. J. Immunol. 2010, 72, 22-30.
    • (2010) Scand. J. Immunol , vol.72 , pp. 22-30
    • Hartshorn, K.L.1    White, M.R.2    Smith, K.3    Sorensen, G.4    Kuroki, Y.5    Holmskov, U.6    Head, J.7    Crouch, E.C.8
  • 62
    • 80051921486 scopus 로고    scopus 로고
    • Reading, P.C. 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, M.D.; Brooks, A.G.; Reading, P.C. 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. 2011, 187, 1884-1894.
    • (2011) J. Immunol , vol.187 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2
  • 63
    • 79953117247 scopus 로고    scopus 로고
    • Glycosylation of the hemagglutinin modulates the sensitivity of h3n2 influenza viruses to innate proteins in airway secretions and virulence in mice
    • Tate, M.D.; Job, E.R.; Brooks, A.G.; Reading, P.C. Glycosylation of the hemagglutinin modulates the sensitivity of h3n2 influenza viruses to innate proteins in airway secretions and virulence in mice. Virology 2011, 413, 84-92.
    • (2011) Virology , vol.413 , pp. 84-92
    • Tate, M.D.1    Job, E.R.2    Brooks, A.G.3    Reading, P.C.4
  • 64
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus a/pr/8/34 hemagglutinin (h1 subtype)
    • Caton, A.J.; Brownlee, G.G.; Yewdell, J.W.; Gerhard, W. The antigenic structure of the influenza virus a/pr/8/34 hemagglutinin (h1 subtype). Cell 1982, 31, 417-427.
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 65
    • 84880260784 scopus 로고    scopus 로고
    • N-linked glycosylation of the hemagglutinin protein influences virulence and antigenicity of the 1918 pandemic and seasonal h1n1 influenza a viruses
    • Sun, X.; Jayaraman, A.; Maniprasad, P.; Raman, R.; Houser, K.V.; Pappas, C.; Zeng, H.; Sasisekharan, R.; Katz, J.M.; Tumpey, T.M. N-linked glycosylation of the hemagglutinin protein influences virulence and antigenicity of the 1918 pandemic and seasonal h1n1 influenza a viruses. J. Virol. 2013, 87, 8756-8766.
    • (2013) J. Virol , vol.87 , pp. 8756-8766
    • Sun, X.1    Jayaraman, A.2    Maniprasad, P.3    Raman, R.4    Houser, K.V.5    Pappas, C.6    Zeng, H.7    Sasisekharan, R.8    Katz, J.M.9    Tumpey, T.M.10
  • 67
    • 79551602706 scopus 로고    scopus 로고
    • The pandemic (h1n1) 2009 influenza virus is resistant to mannose-binding lectin
    • Tokunaga, H.; Ushirogawa, H.; Ohuchi, M. The pandemic (h1n1) 2009 influenza virus is resistant to mannose-binding lectin. Virol. J. 2011, 8, 50.
    • (2011) Virol. J , vol.8 , pp. 50
    • Tokunaga, H.1    Ushirogawa, H.2    Ohuchi, M.3
  • 68
    • 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, J.C.; Dugan, V.G.; Jagger, B.W.; Lau, Y.F.; Sheng, Z.M.; Crouch, E.C.; Hartshorn, K.L.; Taubenberger, J.K. 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    Jagger, B.W.4    Lau, Y.F.5    Sheng, Z.M.6    Crouch, E.C.7    Hartshorn, K.L.8    Taubenberger, J.K.9
  • 70
  • 71
    • 80655146211 scopus 로고    scopus 로고
    • Major histocompatibility complex class ii expression and hemagglutinin subtype influence the infectivity of type a influenza virus for respiratory dendritic cells
    • Hargadon, K.M.; Zhou, H.; Albrecht, R.A.; Dodd, H.A.; Garcia-Sastre, A.; Braciale, T.J. Major histocompatibility complex class ii expression and hemagglutinin subtype influence the infectivity of type a influenza virus for respiratory dendritic cells. J. Virol. 2011, 85, 11955-11963.
    • (2011) J. Virol , vol.85 , pp. 11955-11963
    • Hargadon, K.M.1    Zhou, H.2    Albrecht, R.A.3    Dodd, H.A.4    Garcia-Sastre, A.5    Braciale, T.J.6
  • 72
    • 43249125302 scopus 로고    scopus 로고
    • Differential response of respiratory dendritic cell subsets to influenza virus infection
    • Hao, X.; Kim, T.S.; Braciale, T.J. Differential response of respiratory dendritic cell subsets to influenza virus infection. J. Virol. 2008, 82, 4908-4919.
    • (2008) J. Virol , vol.82 , pp. 4908-4919
    • Hao, X.1    Kim, T.S.2    Braciale, T.J.3
  • 73
    • 0019505004 scopus 로고
    • Interaction of influenza virus with mouse macrophages
    • Rodgers, B.; Mims, C.A. Interaction of influenza virus with mouse macrophages. Infect. Immun. 1981, 31, 751-757.
    • (1981) Infect. Immun , vol.31 , pp. 751-757
    • Rodgers, B.1    Mims, C.A.2
  • 74
    • 0018257734 scopus 로고
    • Host defense mechanisms against influenza virus: Interaction of influenza virus with murine macrophages in vitro
    • Wells, M.A.; Albrecht, P.; Daniel, S.; Ennis, F.A. Host defense mechanisms against influenza virus: Interaction of influenza virus with murine macrophages in vitro. Infect. Immun. 1978, 22, 758-762.
    • (1978) Infect. Immun , vol.22 , pp. 758-762
    • Wells, M.A.1    Albrecht, P.2    Daniel, S.3    Ennis, F.A.4
  • 75
    • 84873036417 scopus 로고    scopus 로고
    • The hemagglutinin protein of highly pathogenic h5n1 influenza viruses overcomes an early block in the replication cycle to promote productive replication in macrophages
    • Cline, T.D.; Karlsson, E.A.; Seufzer, B.J.; Schultz-Cherry, S. The hemagglutinin protein of highly pathogenic h5n1 influenza viruses overcomes an early block in the replication cycle to promote productive replication in macrophages. J. Virol. 2013, 87, 1411-1419.
    • (2013) J. Virol , vol.87 , pp. 1411-1419
    • Cline, T.D.1    Karlsson, E.A.2    Seufzer, B.J.3    Schultz-Cherry, S.4
  • 76
    • 77954492854 scopus 로고    scopus 로고
    • Critical role of airway macrophages in modulating disease severity during influenza virus infection of mice
    • Tate, M.D.; Pickett, D.L.; van Rooijen, N.; Brooks, A.G.; Reading, P.C. Critical role of airway macrophages in modulating disease severity during influenza virus infection of mice. J. Virol. 2010, 84, 7569-7580.
    • (2010) J. Virol , vol.84 , pp. 7569-7580
    • Tate, M.D.1    Pickett, D.L.2    van Rooijen, N.3    Brooks, A.G.4    Reading, P.C.5
  • 78
    • 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, T.M.; Garcia-Sastre, A.; Taubenberger, J.K.; Palese, P.; Swayne, D.E.; Pantin-Jackwood, M.J.; Schultz-Cherry, S.; Solorzano, A.; Van Rooijen, N.; Katz J.M.; 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    Palese, P.4    Swayne, D.E.5    Pantin-Jackwood, M.J.6    Schultz-Cherry, S.7    Solorzano, A.8    van Rooijen, N.9    Katz, J.M.10
  • 79
    • 46949088340 scopus 로고    scopus 로고
    • Protective influenza-specific cd8 t cell responses require interactions with dendritic cells in the lungs
    • McGill, J.; van Rooijen, N.; Legge, K.L. Protective influenza-specific cd8 t cell responses require interactions with dendritic cells in the lungs. J. Exp. Med. 2008, 205, 1635-1646.
    • (2008) J. Exp. Med , vol.205 , pp. 1635-1646
    • McGill, J.1    van Rooijen, N.2    Legge, K.L.3
  • 80
    • 84865416254 scopus 로고    scopus 로고
    • Rapid differentiation of monocytes into type i ifn-producing myeloid dendritic cells as an antiviral strategy against influenza virus infection
    • Cao, W.; Taylor, A.K.; Biber, R.E.; Davis, W.G.; Kim, J.H.; Reber, A.J.; Chirkova, T.; de La Cruz, J.A.; Pandey, A.; Ranjan P.; et al. Rapid differentiation of monocytes into type i ifn-producing myeloid dendritic cells as an antiviral strategy against influenza virus infection. J. Immunol. 2012, 189, 2257-2265.
    • (2012) J. Immunol , vol.189 , pp. 2257-2265
    • Cao, W.1    Taylor, A.K.2    Biber, R.E.3    Davis, W.G.4    Kim, J.H.5    Reber, A.J.6    Chirkova, T.7    de La Cruz, J.A.8    Pandey, A.9    Ranjan, P.10
  • 81
    • 84863464103 scopus 로고    scopus 로고
    • Cell-surface receptors on macrophages and dendritic cells for attachment and entry of influenza virus
    • Londrigan, S.L.; Tate, M.D.; Brooks, A.G.; Reading, P.C. Cell-surface receptors on macrophages and dendritic cells for attachment and entry of influenza virus. J. Leukoc. Biol. 2012, 92, 97-106.
    • (2012) J. Leukoc. Biol , vol.92 , pp. 97-106
    • Londrigan, S.L.1    Tate, M.D.2    Brooks, A.G.3    Reading, P.C.4
  • 82
    • 0034063448 scopus 로고    scopus 로고
    • Involvement of the mannose receptor in infection of macrophages by influenza virus
    • Reading, P.C.; Miller, J.L.; Anders, E.M. Involvement of the mannose receptor in infection of macrophages by influenza virus. J. Virol. 2000, 74, 5190-5197.
    • (2000) J. Virol , vol.74 , pp. 5190-5197
    • Reading, P.C.1    Miller, J.L.2    Anders, E.M.3
  • 83
    • 77950479967 scopus 로고    scopus 로고
    • Macrophage receptors for influenza a virus: Role of the macrophage galactose-type lectin and mannose receptor in viral entry
    • Upham, J.P.; Pickett, D.; Irimura, T.; Anders, E.M.; Reading, P.C. Macrophage receptors for influenza a virus: Role of the macrophage galactose-type lectin and mannose receptor in viral entry. J. Virol. 2010, 84, 3730-3737.
    • (2010) J. Virol , vol.84 , pp. 3730-3737
    • Upham, J.P.1    Pickett, D.2    Irimura, T.3    Anders, E.M.4    Reading, P.C.5
  • 84
    • 84892468991 scopus 로고    scopus 로고
    • The macrophage galactose-type lectin can function as an attachment and entry receptor for influenza virus
    • Ng, W.C.; Liong, S.; Tate, M.D.; Irimura, T.; Denda-Nagai, K.; Brooks, A.G.; Londrigan, S.L.; Reading, P.C. The macrophage galactose-type lectin can function as an attachment and entry receptor for influenza virus. J. Virol. 2013, 88, 1659-1672.
    • (2013) J. Virol , vol.88 , pp. 1659-1672
    • Ng, W.C.1    Liong, S.2    Tate, M.D.3    Irimura, T.4    Denda-Nagai, K.5    Brooks, A.G.6    Londrigan, S.L.7    Reading, P.C.8
  • 86
    • 79952410920 scopus 로고    scopus 로고
    • N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza a viruses into cells expressing dc-sign or l-sign
    • Londrigan, S.L.; Turville, S.G.; Tate, M.D.; Deng, Y.M.; Brooks, A.G.; Reading, P.C. N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza a viruses into cells expressing dc-sign or l-sign. J. Virol. 2011, 85, 2990-3000.
    • (2011) J. Virol , vol.85 , pp. 2990-3000
    • Londrigan, S.L.1    Turville, S.G.2    Tate, M.D.3    Deng, Y.M.4    Brooks, A.G.5    Reading, P.C.6
  • 88
    • 84881102897 scopus 로고    scopus 로고
    • Glycans from avian influenza virus are recognized by chicken dendritic cells and are targets for the humoral immune response in chicken
    • de Geus, E.D.; Tefsen, B.; van Haarlem, D.A.; van Eden, W.; van Die, I.; Vervelde, L. Glycans from avian influenza virus are recognized by chicken dendritic cells and are targets for the humoral immune response in chicken. Mol. Immunol. 2013, 56, 452-462.
    • (2013) Mol. Immunol , vol.56 , pp. 452-462
    • de Geus, E.D.1    Tefsen, B.2    van Haarlem, D.A.3    van Eden, W.4    van Die, I.5    Vervelde, L.6
  • 89
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of hong kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley, D.C.; Wilson, I.A.; Skehel, J.J. Structural identification of the antibody-binding sites of hong kong influenza haemagglutinin and their involvement in antigenic variation. Nature 1981, 289, 373-378.
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 90
    • 0021112689 scopus 로고
    • Antigenicity and evolution amongst recent influenza viruses of h1n1 subtype
    • Raymond, F.L.; Caton, A.J.; Cox, N.J.; Kendal, A.P.; Brownlee, G.G. Antigenicity and evolution amongst recent influenza viruses of h1n1 subtype. Nucleic Acids Res. 1983, 11, 7191-7203.
    • (1983) Nucleic Acids Res , vol.11 , pp. 7191-7203
    • Raymond, F.L.1    Caton, A.J.2    Cox, N.J.3    Kendal, A.P.4    Brownlee, G.G.5
  • 92
    • 84876530780 scopus 로고    scopus 로고
    • Glycosylation on hemagglutinin affects the virulence and pathogenicity of pandemic h1n1/2009 influenza a virus in mice
    • Zhang, Y.; Zhu, J.; Li, Y.; Bradley, K.C.; Cao, J.; Chen, H.; Jin, M.; Zhou, H. Glycosylation on hemagglutinin affects the virulence and pathogenicity of pandemic h1n1/2009 influenza a virus in mice. PLoS One 2013, 8, e61397.
    • (2013) PLoS One , vol.8
    • Zhang, Y.1    Zhu, J.2    Li, Y.3    Bradley, K.C.4    Cao, J.5    Chen, H.6    Jin, M.7    Zhou, H.8
  • 94
    • 79251583146 scopus 로고    scopus 로고
    • Structural basis of influenza virus neutralization
    • Han, T.; Marasco, W.A. Structural basis of influenza virus neutralization. Ann. N. Y. Acad. Sci. 2011, 1217, 178-190.
    • (2011) Ann. N. Y. Acad. Sci , vol.1217 , pp. 178-190
    • Han, T.1    Marasco, W.A.2
  • 99
    • 77949824961 scopus 로고    scopus 로고
    • Incidence of 2009 pandemic influenza a h1n1 infection in england: A cross-sectional serological study
    • Miller, E.; Hoschler, K.; Hardelid, P.; Stanford, E.; Andrews, N.; Zambon, M. Incidence of 2009 pandemic influenza a h1n1 infection in england: A cross-sectional serological study. Lancet 2010, 375, 1100-1108.
    • (2010) Lancet , vol.375 , pp. 1100-1108
    • Miller, E.1    Hoschler, K.2    Hardelid, P.3    Stanford, E.4    Andrews, N.5    Zambon, M.6
  • 100
    • 84865100648 scopus 로고    scopus 로고
    • Effect of priming with h1n1 influenza viruses of variable antigenic distances on challenge with 2009 pandemic h1n1 virus
    • O'Donnell, C.D.; Wright, A.; Vogel, L.N.; Wei, C.J.; Nabel, G.J.; Subbarao, K. Effect of priming with h1n1 influenza viruses of variable antigenic distances on challenge with 2009 pandemic h1n1 virus. J. Virol. 2012, 86, 8625-8633.
    • (2012) J. Virol , vol.86 , pp. 8625-8633
    • O'Donnell, C.D.1    Wright, A.2    Vogel, L.N.3    Wei, C.J.4    Nabel, G.J.5    Subbarao, K.6
  • 101
    • 84880362193 scopus 로고    scopus 로고
    • Genetic requirement for hemagglutinin glycosylation and its implications for influenza a h1n1 virus evolution
    • Kim, J.I.; Lee, I.; Park, S.; Hwang, M.W.; Bae, J.Y.; Lee, S.; Heo, J.; Park, M.S.; Garcia-Sastre, A. Genetic requirement for hemagglutinin glycosylation and its implications for influenza a h1n1 virus evolution. J. Virol. 2013, 87, 7539-7549.
    • (2013) J. Virol , vol.87 , pp. 7539-7549
    • Kim, J.I.1    Lee, I.2    Park, S.3    Hwang, M.W.4    Bae, J.Y.5    Lee, S.6    Heo, J.7    Park, M.S.8    Garcia-Sastre, A.9
  • 102
    • 79952713119 scopus 로고    scopus 로고
    • Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice
    • Wanzeck, K.; Boyd, K.L.; McCullers, J.A. Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice. Am. J. Respir. Crit. Care Med. 2011, 183, 767-773.
    • (2011) Am. J. Respir. Crit. Care Med , vol.183 , pp. 767-773
    • Wanzeck, K.1    Boyd, K.L.2    McCullers, J.A.3
  • 103
    • 84890874733 scopus 로고    scopus 로고
    • Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyper-glycosylation of the globular head domain
    • doi:10.1128/JVI.02608-13
    • Eggink, D.; Goff, P.H.; Palese, P. Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyper-glycosylation of the globular head domain. J. Virol. 2013, doi:10.1128/JVI.02608-13.
    • (2013) J. Virol
    • Eggink, D.1    Goff, P.H.2    Palese, P.3
  • 108
    • 0027417244 scopus 로고
    • Conservation of determinants for class ii-restricted t cells within site e of influenza virus hemagglutinin and factors influencing their expression
    • Brown, L.E.; White, D.O.; Jackson, D.C. Conservation of determinants for class ii-restricted t cells within site e of influenza virus hemagglutinin and factors influencing their expression. J. Virol. 1993, 67, 2887-2893.
    • (1993) J. Virol , vol.67 , pp. 2887-2893
    • Brown, L.E.1    White, D.O.2    Jackson, D.C.3
  • 110
    • 0025232782 scopus 로고
    • The role of the endoplasmic reticulum in antigen processing. N-glycosylation of influenza hemagglutinin abrogates cd4+ cytotoxic t cell recognition of endogenously processed antigen
    • Thomas, D.B.; Hodgson, J.; Riska, P.F.; Graham, C.M. The role of the endoplasmic reticulum in antigen processing. N-glycosylation of influenza hemagglutinin abrogates cd4+ cytotoxic t cell recognition of endogenously processed antigen. J. Immunol. 1990, 144, 2789-2794.
    • (1990) J. Immunol , vol.144 , pp. 2789-2794
    • Thomas, D.B.1    Hodgson, J.2    Riska, P.F.3    Graham, C.M.4
  • 111
    • 0027180032 scopus 로고
    • Modulation of cd4+ t-cell recognition of influenza hemagglutinin by carbohydrate side chains located outside a t-cell determinant
    • Drummer, H.E.; Jackson, D.C.; Brown, L.E. Modulation of cd4+ t-cell recognition of influenza hemagglutinin by carbohydrate side chains located outside a t-cell determinant. Virology 1993, 192, 282-289.
    • (1993) Virology , vol.192 , pp. 282-289
    • Drummer, H.E.1    Jackson, D.C.2    Brown, L.E.3
  • 112
    • 0028243697 scopus 로고
    • Glycosylation of a synthetic peptide representing a t-cell determinant of influenza virus hemagglutinin results in loss of recognition by cd4+ t-cell clones
    • Jackson, D.C.; Drummer, H.E.; Urge, L.; Otvos, L., Jr.; Brown, L.E. Glycosylation of a synthetic peptide representing a t-cell determinant of influenza virus hemagglutinin results in loss of recognition by cd4+ t-cell clones. Virology 1994, 199, 422-430.
    • (1994) Virology , vol.199 , pp. 422-430
    • Jackson, D.C.1    Drummer, H.E.2    Urge, L.3    Otvos Jr., L.4    Brown, L.E.5
  • 113
    • 0032145579 scopus 로고    scopus 로고
    • Effects of host-dependent glycosylation of hemagglutinin on receptor-binding properties on h1n1 human influenza a virus grown in mdck cells and in embryonated eggs
    • Gambaryan, A.S.; Marinina, V.P.; Tuzikov, A.B.; Bovin, N.V.; Rudneva, I.A.; Sinitsyn, B.V.; Shilov, A.A.; Matrosovich, M.N. Effects of host-dependent glycosylation of hemagglutinin on receptor-binding properties on h1n1 human influenza a virus grown in mdck cells and in embryonated eggs. Virology 1998, 247, 170-177.
    • (1998) Virology , vol.247 , pp. 170-177
    • Gambaryan, A.S.1    Marinina, V.P.2    Tuzikov, A.B.3    Bovin, N.V.4    Rudneva, I.A.5    Sinitsyn, B.V.6    Shilov, A.A.7    Matrosovich, M.N.8
  • 115
    • 0036893179 scopus 로고    scopus 로고
    • Tight binding of influenza virus hemagglutinin to its receptor interferes with fusion pore dilation
    • Ohuchi, M.; Ohuchi, R.; Sakai, T.; Matsumoto, A. Tight binding of influenza virus hemagglutinin to its receptor interferes with fusion pore dilation. J. Virol. 2002, 76, 12405-12413.
    • (2002) J. Virol , vol.76 , pp. 12405-12413
    • Ohuchi, M.1    Ohuchi, R.2    Sakai, T.3    Matsumoto, A.4
  • 116
    • 0024242218 scopus 로고
    • Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport, and activity of the molecule
    • Gallagher, P.; Henneberry, J.; Wilson, I.; Sambrook, J.; Gething, M.J. Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport, and activity of the molecule. J. Cell Biol. 1988, 107, 2059-2073.
    • (1988) J. Cell Biol , vol.107 , pp. 2059-2073
    • Gallagher, P.1    Henneberry, J.2    Wilson, I.3    Sambrook, J.4    Gething, M.J.5
  • 117
    • 0032927194 scopus 로고    scopus 로고
    • The surface glycoproteins of h5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties
    • Matrosovich, M.; Zhou, N.; Kawaoka, Y.; Webster, R. The surface glycoproteins of h5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J. Virol. 1999, 73, 1146-1155.
    • (1999) J. Virol , vol.73 , pp. 1146-1155
    • Matrosovich, M.1    Zhou, N.2    Kawaoka, Y.3    Webster, R.4
  • 118
    • 77953297916 scopus 로고    scopus 로고
    • Glycosylation at 158n of the hemagglutinin protein and receptor binding specificity synergistically affect the antigenicity and immunogenicity of a live attenuated h5n1 a/vietnam/1203/2004 vaccine virus in ferrets
    • Wang, W.; Lu, B.; Zhou, H.; Suguitan, A.L., Jr.; Cheng, X.; Subbarao, K.; Kemble, G.; Jin, H. Glycosylation at 158n of the hemagglutinin protein and receptor binding specificity synergistically affect the antigenicity and immunogenicity of a live attenuated h5n1 a/vietnam/1203/2004 vaccine virus in ferrets. J. Virol. 2010, 84, 6570-6577.
    • (2010) J. Virol , vol.84 , pp. 6570-6577
    • Wang, W.1    Lu, B.2    Zhou, H.3    Suguitan Jr., A.L.4    Cheng, X.5    Subbarao, K.6    Kemble, G.7    Jin, H.8
  • 119
    • 0030863130 scopus 로고    scopus 로고
    • Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety
    • Ohuchi, M.; Ohuchi, R.; Feldmann, A.; Klenk, H.D. Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety. J. Virol. 1997, 71, 8377-8384.
    • (1997) J. Virol , vol.71 , pp. 8377-8384
    • Ohuchi, M.1    Ohuchi, R.2    Feldmann, A.3    Klenk, H.D.4
  • 121
    • 84871173025 scopus 로고    scopus 로고
    • A single residue within the v5 region of hiv-1 envelope facilitates viral escape from the broadly neutralizing monoclonal antibody vrc01
    • Guo, D.; Shi, X.; Arledge, K.C.; Song, D.; Jiang, L.; Fu, L.; Gong, X.; Zhang, S.; Wang, X.; Zhang, L. A single residue within the v5 region of hiv-1 envelope facilitates viral escape from the broadly neutralizing monoclonal antibody vrc01. J. Biol. Chem. 2012, 287, 43170-43179.
    • (2012) J. Biol. Chem , vol.287 , pp. 43170-43179
    • Guo, D.1    Shi, X.2    Arledge, K.C.3    Song, D.4    Jiang, L.5    Fu, L.6    Gong, X.7    Zhang, S.8    Wang, X.9    Zhang, L.A.10
  • 122
    • 79961179950 scopus 로고    scopus 로고
    • Evolution of human immunodeficiency virus type 1 in a patient with cross-reactive neutralizing activity in serum
    • van Gils, M.J.; Edo-Matas, D.; Bowles, E.J.; Burger, J.A.; Stewart-Jones, G.B.; Schuitemaker, H. Evolution of human immunodeficiency virus type 1 in a patient with cross-reactive neutralizing activity in serum. J. Virol. 2011, 85, 8443-8448.
    • (2011) J. Virol , vol.85 , pp. 8443-8448
    • van Gils, M.J.1    Edo-Matas, D.2    Bowles, E.J.3    Burger, J.A.4    Stewart-Jones, G.B.5    Schuitemaker, H.6
  • 123
    • 84857072874 scopus 로고    scopus 로고
    • Prediction of biological functions on glycosylation site migrations in human influenza h1n1 viruses
    • Sun, S.; Wang, Q.; Zhao, F.; Chen, W.; Li, Z. Prediction of biological functions on glycosylation site migrations in human influenza h1n1 viruses. PLoS One 2012, 7, e32119.
    • (2012) PLoS One , vol.7
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 124
    • 0031014661 scopus 로고    scopus 로고
    • Changes in the hemagglutinin molecule of influenza type a (h3n2) virus associated with increased virulence for mice
    • Hartley, C.A.; Reading, P.C.; Ward, A.C.; Anders, E.M. Changes in the hemagglutinin molecule of influenza type a (h3n2) virus associated with increased virulence for mice. Arch. Virol. 1997, 142, 75-88.
    • (1997) Arch. Virol , vol.142 , pp. 75-88
    • Hartley, C.A.1    Reading, P.C.2    Ward, A.C.3    Anders, E.M.4
  • 125
    • 73949084221 scopus 로고    scopus 로고
    • Loss of a single n-linked glycan from the hemagglutinin of influenza virus is associated with resistance to collectins and increased virulence in mice
    • Reading, P.C.; Pickett, D.L.; Tate, M.D.; Whitney, P.G.; Job, E.R.; Brooks, A.G. Loss of a single n-linked glycan from the hemagglutinin of influenza virus is associated with resistance to collectins and increased virulence in mice. Respir. Res. 2009, 10, 117.
    • (2009) Respir. Res , vol.10 , pp. 117
    • Reading, P.C.1    Pickett, D.L.2    Tate, M.D.3    Whitney, P.G.4    Job, E.R.5    Brooks, A.G.6
  • 126
    • 0036748176 scopus 로고    scopus 로고
    • Lung surfactant protein d (sp-d) and the molecular diverted descendants: Conglutinin, cl-43 and cl-46
    • Hansen, S.; Holmskov, U. Lung surfactant protein d (sp-d) and the molecular diverted descendants: Conglutinin, cl-43 and cl-46. Immunobiology 2002, 205, 498-517.
    • (2002) Immunobiology , vol.205 , pp. 498-517
    • Hansen, S.1    Holmskov, U.2
  • 128
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in casp8
    • Krieger, E.; Joo, K.; Lee, J.; Raman, S.; Thompson, J.; Tyka, M.; Baker, D.; Karplus, K. Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in casp8. Proteins 2009, 77, 114-122.
    • (2009) Proteins , vol.77 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Raman, S.4    Thompson, J.5    Tyka, M.6    Baker, D.7    Karplus, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.