메뉴 건너뛰기




Volumn 87, Issue 15, 2013, Pages 8756-8766

N-linked glycosylation of the hemagglutinin protein influences virulence and antigenicity of the 1918 pandemic and seasonal H1N1 influenza A viruses

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ;

EID: 84880260784     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00593-13     Document Type: Article
Times cited : (85)

References (44)
  • 1
    • 0034051550 scopus 로고    scopus 로고
    • Global epidemiology of influenza: past and present
    • Cox NJ, Subbarao K. 2000. Global epidemiology of influenza: past and present. Annu. Rev. Med.. 51:407-421.
    • (2000) Annu. Rev. Med. , vol.51 , pp. 407-421
    • Cox, N.J.1    Subbarao, K.2
  • 2
    • 0036514779 scopus 로고    scopus 로고
    • Updating the accounts: global mortality of the 1918-1920 "Spanish" influenza pandemic
    • Johnson NP, Mueller J. 2002. Updating the accounts: global mortality of the 1918-1920 "Spanish" influenza pandemic. Bull. Hist. Med.. 76:105-115.
    • (2002) Bull. Hist. Med. , vol.76 , pp. 105-115
    • Johnson, N.P.1    Mueller, J.2
  • 3
    • 67650896045 scopus 로고    scopus 로고
    • Historical perspective-emergence of influenza A (H1N1) viruses
    • Zimmer SM, Burke DS. 2009. Historical perspective-emergence of influenza A (H1N1) viruses. N. Engl. J. Med. 361:279-285.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 279-285
    • Zimmer, S.M.1    Burke, D.S.2
  • 4
    • 0021921441 scopus 로고
    • Why was the 1918 influenza pandemic so lethal? The possible role of a neurovirulent neuraminidase
    • Maurizi CP. 1985. Why was the 1918 influenza pandemic so lethal? The possible role of a neurovirulent neuraminidase. Med. Hypotheses 16:1-5.
    • (1985) Med. Hypotheses , vol.16 , pp. 1-5
    • Maurizi, C.P.1
  • 6
    • 79953770830 scopus 로고    scopus 로고
    • The first influenza pandemic of the new millennium
    • Neumann G, Kawaoka Y. 2011. The first influenza pandemic of the new millennium. Influenza Other Respi. Viruses. 5:157-166.
    • (2011) Influenza Other Respi. Viruses. , vol.5 , pp. 157-166
    • Neumann, G.1    Kawaoka, Y.2
  • 7
    • 77950958001 scopus 로고    scopus 로고
    • Update: influenza activity-United States, August 30, 2009-March 27, 2010, and composition of the 2010-11 influenza vaccine
    • Centers for Disease Control and Prevention
    • Centers for Disease Control and Prevention. 2010. Update: influenza activity-United States, August 30, 2009-March 27, 2010, and composition of the 2010-11 influenza vaccine. MMWR. Morbid. Mortal. Wkly. Rep.. 59:423-430.
    • (2010) MMWR. Morbid. Mortal. Wkly. Rep.. , vol.59 , pp. 423-430
  • 10
    • 0033602713 scopus 로고    scopus 로고
    • Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    • Steinhauer DA. 1999. Role of hemagglutinin cleavage for the pathogenicity of influenza virus. Virology. 258:1-20.
    • (1999) Virology , vol.258 , pp. 1-20
    • Steinhauer, D.A.1
  • 11
    • 0023736676 scopus 로고
    • Sequence requirements for cleavage activation of influenza virus hemagglutinin expressed in mammalian cells
    • U. S. A.
    • Kawaoka Y, Webster RG. 1988. Sequence requirements for cleavage activation of influenza virus hemagglutinin expressed in mammalian cells. Proc. Natl. Acad. Sci. U. S. A.. 85:324-328.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 324-328
    • Kawaoka, Y.1    Webster, R.G.2
  • 12
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson IA, Skehel JJ, Wiley DC. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature. 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 13
    • 0019121690 scopus 로고
    • Glycosylation sites of influenza viral glycoproteins
    • Tryptic glycopeptides from the A/WSN (H0N1) hemagglutinin glycoprotein
    • Nakamura K, Bhown AS, Compans RW. 1980. Glycosylation sites of influenza viral glycoproteins. Tryptic glycopeptides from the A/WSN (H0N1) hemagglutinin glycoprotein. Virology. 107:208-221.
    • (1980) Virology , vol.107 , pp. 208-221
    • Nakamura, K.1    Bhown, A.S.2    Compans, R.W.3
  • 14
    • 0021327568 scopus 로고
    • Carbohydrates of influenza virus
    • V. Oligosaccharides attached to individual glycosylation sites of the hemagglutinin of fowl plague virus.
    • Keil W, Niemann H, Schwarz RT, Klenk HD. 1984. Carbohydrates of influenza virus. V. Oligosaccharides attached to individual glycosylation sites of the hemagglutinin of fowl plague virus. Virology. 133:77-91.
    • (1984) Virology , vol.133 , pp. 77-91
    • Keil, W.1    Niemann, H.2    Schwarz, R.T.3    Klenk, H.D.4
  • 15
    • 67649625767 scopus 로고    scopus 로고
    • Glycan analysis in cell culture-based influenza vaccine production: influence of host cell line and virus strain on the glycosylation pattern of viral hemagglutinin
    • Schwarzer J, Rapp E, Hennig R, Genzel Y, Jordan I, Sandig V, Reichl U. 2009. Glycan analysis in cell culture-based influenza vaccine production: influence of host cell line and virus strain on the glycosylation pattern of viral hemagglutinin. Vaccine. 27:4325-4336.
    • (2009) Vaccine , vol.27 , pp. 4325-4336
    • Schwarzer, J.1    Rapp, E.2    Hennig, R.3    Genzel, Y.4    Jordan, I.5    Sandig, V.6    Reichl, U.7
  • 16
    • 0027238117 scopus 로고
    • Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin
    • Roberts PC, Garten W, Klenk HD. 1993. Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin. J. Virol.. 67:3048-3060.
    • (1993) J. Virol. , vol.67 , pp. 3048-3060
    • Roberts, P.C.1    Garten, W.2    Klenk, H.D.3
  • 17
    • 0026489261 scopus 로고
    • Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus
    • Gallagher PJ, Henneberry JM, Sambrook JF, Gething MJ. 1992. Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus. J. Virol.. 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
  • 18
    • 0037196586 scopus 로고    scopus 로고
    • Importance of hemagglutinin glycosylation for the biological functions of influenza virus
    • Klenk HD, Wagner R, Heuer D, Wolff T. 2002. Importance of hemagglutinin glycosylation for the biological functions of influenza virus. Virus Res.. 82:73-75.
    • (2002) Virus Res. , vol.82 , pp. 73-75
    • Klenk, H.D.1    Wagner, R.2    Heuer, D.3    Wolff, T.4
  • 19
    • 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. 2004. Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin. J. Virol. 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
  • 20
    • 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 HD. 1997. Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety. J. Virol.. 71:8377-8384.
    • (1997) J. Virol. , vol.71 , pp. 8377-8384
    • Ohuchi, M.1    Ohuchi, R.2    Feldmann, A.3    Klenk, H.D.4
  • 21
    • 67649840704 scopus 로고    scopus 로고
    • Signalling through C-type lectin receptors: shaping immune responses
    • Geijtenbeek TB, Gringhuis SI. 2009. Signalling through C-type lectin receptors: shaping immune responses. Nat. Rev. Immunol.. 9:465-479.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 465-479
    • Geijtenbeek, T.B.1    Gringhuis, S.I.2
  • 22
    • 34247530859 scopus 로고    scopus 로고
    • Virus glycosylation: role in virulence and immune interactions
    • Vigerust DJ, Shepherd VL. 2007. Virus glycosylation: role in virulence and immune interactions. Trends Microbiol.. 15:211-218.
    • (2007) Trends Microbiol. , vol.15 , pp. 211-218
    • Vigerust, D.J.1    Shepherd, V.L.2
  • 23
    • 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. 2011. Glycosylation site alteration in the evolution of influenza A (H1N1) viruses. PLoS One 6:e22844. doi:10.1371/journal.pone.0022844.
    • (2011) PLoS One. , vol.6
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 24
    • 77649176948 scopus 로고    scopus 로고
    • Predicting the antigenic structure of the pandemic (H1N1) 2009 influenza virus hemagglutinin
    • Igarashi M, Ito K, Yoshida R, Tomabechi D, Kida H, Takada A. 2010. Predicting the antigenic structure of the pandemic (H1N1) 2009 influenza virus hemagglutinin. PLoS One 5:e8553. doi:10.1371/journal.pone.0008553.
    • (2010) PLoS One. , vol.5
    • Igarashi, M.1    Ito, K.2    Yoshida, R.3    Tomabechi, D.4    Kida, H.5    Takada, A.6
  • 25
    • 36048957993 scopus 로고    scopus 로고
    • Highly pathogenic avian influenza H5N1 viruses elicit an attenuated type I interferon response in polarized human bronchial epithelial cells
    • Zeng H, Goldsmith C, Thawatsupha P, Chittaganpitch M, Waicharoen S, Zaki S, Tumpey TM, Katz JM. 2007. Highly pathogenic avian influenza H5N1 viruses elicit an attenuated type I interferon response in polarized human bronchial epithelial cells. J. Virol.. 81:12439-12449.
    • (2007) J. Virol. , vol.81 , pp. 12439-12449
    • Zeng, H.1    Goldsmith, C.2    Thawatsupha, P.3    Chittaganpitch, M.4    Waicharoen, S.5    Zaki, S.6    Tumpey, T.M.7    Katz, J.M.8
  • 26
    • 78650653968 scopus 로고    scopus 로고
    • The 2009 pandemic H1N1 and triple-reassortant swine H1N1 influenza viruses replicate efficiently but elicit an attenuated inflammatory response in polarized human bronchial epithelial cells
    • Zeng H, Pappas C, Katz JM, Tumpey TM. 2011. The 2009 pandemic H1N1 and triple-reassortant swine H1N1 influenza viruses replicate efficiently but elicit an attenuated inflammatory response in polarized human bronchial epithelial cells. J. Virol.. 85:686-696.
    • (2011) J. Virol. , vol.85 , pp. 686-696
    • Zeng, H.1    Pappas, C.2    Katz, J.M.3    Tumpey, T.M.4
  • 27
    • 0037135677 scopus 로고    scopus 로고
    • Eightplasmid system for rapid generation of influenza virus vaccines
    • Hoffmann E, Krauss S, Perez D, Webby R, Webster RG. 2002. Eightplasmid system for rapid generation of influenza virus vaccines. Vaccine. 20:3165-3170.
    • (2002) Vaccine , vol.20 , pp. 3165-3170
    • Hoffmann, E.1    Krauss, S.2    Perez, D.3    Webby, R.4    Webster, R.G.5
  • 28
    • 77956634502 scopus 로고    scopus 로고
    • Modifications to the hemagglutinin cleavage site control the virulence of a neurotropic H1N1 influenza virus
    • Sun X, Tse LV, Ferguson AD, Whittaker GR. 2010. Modifications to the hemagglutinin cleavage site control the virulence of a neurotropic H1N1 influenza virus. J. Virol.. 84:8683-8690.
    • (2010) J. Virol. , vol.84 , pp. 8683-8690
    • Sun, X.1    Tse, L.V.2    Ferguson, A.D.3    Whittaker, G.R.4
  • 29
    • 0038024223 scopus 로고    scopus 로고
    • Sialic acid receptor specificity on erythrocytes affects detection of antibody to avian influenza haemagglutinin
    • Stephenson I, Wood JM, Nicholson KG, Zambon MC. 2003. Sialic acid receptor specificity on erythrocytes affects detection of antibody to avian influenza haemagglutinin. J. Med. Virol.. 70:391-398.
    • (2003) J. Med. Virol. , vol.70 , pp. 391-398
    • Stephenson, I.1    Wood, J.M.2    Nicholson, K.G.3    Zambon, M.C.4
  • 31
    • 80053062205 scopus 로고    scopus 로고
    • Effect of D222G mutation in the hemagglutinin protein on receptor binding, pathogenesis and transmissibility of the 2009 pandemic H1N1 influenza virus
    • Belser JA, Jayaraman A, Raman R, Pappas C, Zeng H, Cox NJ, Katz JM, Sasisekharan R, Tumpey TM. 2011. Effect of D222G mutation in the hemagglutinin protein on receptor binding, pathogenesis and transmissibility of the 2009 pandemic H1N1 influenza virus. PLoS One 6:e25091. doi:10.1371/journal.pone.0025091.
    • (2011) PLoS One. , vol.6
    • Belser, J.A.1    Jayaraman, A.2    Raman, R.3    Pappas, C.4    Zeng, H.5    Cox, N.J.6    Katz, J.M.7    Sasisekharan, R.8    Tumpey, T.M.9
  • 33
    • 55949101550 scopus 로고    scopus 로고
    • Biophys. J.
    • Kasson PM, Pande VS. 2008. Structural basis for influence of viral glycans on ligand binding by influenza hemagglutinin. Biophys. J. 95:L48-L50.
    • (2008) , vol.95
    • Kasson, P.M.1    Pande, V.S.2
  • 34
    • 48749093648 scopus 로고    scopus 로고
    • Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity
    • Stevens J, Blixt O, Chen LM, Donis RO, Paulson JC, Wilson IA. 2008. Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity. J. Mol. Biol.. 381:1382-1394.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1382-1394
    • Stevens, J.1    Blixt, O.2    Chen, L.M.3    Donis, R.O.4    Paulson, J.C.5    Wilson, I.A.6
  • 36
    • 77951466468 scopus 로고    scopus 로고
    • Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity, and immunogenicity in ferrets
    • Xu Q, Wang W, Cheng X, Zengel J, Jin H. 2010. Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity, and immunogenicity in ferrets. J. Virol.. 84:4936-4945.
    • (2010) J. Virol. , vol.84 , pp. 4936-4945
    • Xu, Q.1    Wang, W.2    Cheng, X.3    Zengel, J.4    Jin, H.5
  • 37
    • 79251508720 scopus 로고    scopus 로고
    • Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin
    • RRN1001
    • Cherry JL, Lipman DJ, Nikolskaya A, Wolf YI. 2009. Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin. PLoS Curr. 18:RRN1001. doi:10.1371/currents.RRN1001.
    • (2009) PLoS Curr. , vol.18
    • Cherry, J.L.1    Lipman, D.J.2    Nikolskaya, A.3    Wolf, Y.I.4
  • 38
    • 84934437867 scopus 로고    scopus 로고
    • Glycosylation as a target for recognition of influenza viruses by the innate immune system
    • Reading PC, Tate MD, Pickett DL, Brooks AG. 2007. Glycosylation as a target for recognition of influenza viruses by the innate immune system. Adv. Exp. Med. Biol.. 598:279-292.
    • (2007) Adv. Exp. Med. Biol. , vol.598 , pp. 279-292
    • Reading, P.C.1    Tate, M.D.2    Pickett, D.L.3    Brooks, A.G.4
  • 39
    • 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. 2011. 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.. 187:1884-1894.
    • (2011) J. Immunol. , vol.187 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 40
    • 84863425227 scopus 로고    scopus 로고
    • Antibody pressure by a human monoclonal antibody targeting the 2009 pandemic H1N1 virus hemagglutinin drives the emergence of a virus with increased virulence in mice
    • O'Donnell CD, Vogel L, Wright A, Das SR, Wrammert J, Li GM, McCausland M, Zheng NY, Yewdell JW, Ahmed R, Wilson PC, Subbarao K. 2012. Antibody pressure by a human monoclonal antibody targeting the 2009 pandemic H1N1 virus hemagglutinin drives the emergence of a virus with increased virulence in mice. mBio 3(3):e00120 -12. doi:10.1128/mBio.00120-12.
    • (2012) mBio , vol.3 , Issue.3
    • O'Donnell, C.D.1    Vogel, L.2    Wright, A.3    Das, S.R.4    Wrammert, J.5    Li, G.M.6    McCausland, M.7    Zheng, N.Y.8    Yewdell, J.W.9    Ahmed, R.10    Wilson, P.C.11    Subbarao, K.12
  • 43
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel JJ, Wiley DC. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem.. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 44
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed LJ, Muench H. 1938. A simple method of estimating fifty percent endpoints. J. Hygiene. 27:493-497.
    • (1938) J. Hygiene. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.