메뉴 건너뛰기




Volumn 175, Issue 2-4, 2015, Pages 244-256

Hemagglutinin glycosylation modulates the pathogenicity and antigenicity of the H5N1 avian influenza virus

Author keywords

Antigenicity; Avian influenza virus; Glycosylation; Hemagglutinin; Pathogenicity

Indexed keywords

AVIAN INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; NEUTRALIZING ANTIBODY;

EID: 84922742404     PISSN: 03781135     EISSN: 18732542     Source Type: Journal    
DOI: 10.1016/j.vetmic.2014.12.011     Document Type: Article
Times cited : (47)

References (55)
  • 1
    • 0035813039 scopus 로고    scopus 로고
    • Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture
    • Baigent S.J., McCauley J.W. Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture. Virus Res. 2001, 79:177-185.
    • (2001) Virus Res. , vol.79 , pp. 177-185
    • Baigent, S.J.1    McCauley, J.W.2
  • 2
    • 80054995402 scopus 로고    scopus 로고
    • Reversion of PB2-627E to -627K during replication of an H5N1 Clade 2.2 virus in mammalian hosts depends on the origin of the nucleoprotein
    • Bogs J., Kalthoff D., Veits J., Pavlova S., Schwemmle M., Manz B., Mettenleiter T.C., Stech J. Reversion of PB2-627E to -627K during replication of an H5N1 Clade 2.2 virus in mammalian hosts depends on the origin of the nucleoprotein. J. Virol. 2011, 85:10691-10698.
    • (2011) J. Virol. , vol.85 , pp. 10691-10698
    • Bogs, J.1    Kalthoff, D.2    Veits, J.3    Pavlova, S.4    Schwemmle, M.5    Manz, B.6    Mettenleiter, T.C.7    Stech, J.8
  • 3
    • 0344406204 scopus 로고    scopus 로고
    • Impact of glycosylation on the immunogenicity of a DNA-based influenza H5 HA vaccine
    • Bright R.A., Ross T.M., Subbarao K., Robinson H.L., Katz J.M. Impact of glycosylation on the immunogenicity of a DNA-based influenza H5 HA vaccine. Virology 2003, 308:270-278.
    • (2003) Virology , vol.308 , pp. 270-278
    • Bright, R.A.1    Ross, T.M.2    Subbarao, K.3    Robinson, H.L.4    Katz, J.M.5
  • 5
    • 84862260858 scopus 로고    scopus 로고
    • Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis
    • Chen W., Sun S., Li Z. Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis. PLoS ONE 2012, 7:e38794.
    • (2012) PLoS ONE , vol.7
    • Chen, W.1    Sun, S.2    Li, Z.3
  • 6
    • 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
  • 7
    • 0037038866 scopus 로고    scopus 로고
    • Induction of proinflammatory cytokines in human macrophages by influenza A (H5N1) viruses: a mechanism for the unusual severity of human disease?
    • Cheung C., Poon L., Lau A., Luk W., Lau Y., Shortridge K., Gordon S., Guan Y., Peiris J. Induction of proinflammatory cytokines in human macrophages by influenza A (H5N1) viruses: a mechanism for the unusual severity of human disease?. Lancet 2002, 360:1831-1837.
    • (2002) Lancet , vol.360 , pp. 1831-1837
    • Cheung, C.1    Poon, L.2    Lau, A.3    Luk, W.4    Lau, Y.5    Shortridge, K.6    Gordon, S.7    Guan, Y.8    Peiris, J.9
  • 8
    • 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
  • 9
    • 1842345479 scopus 로고
    • Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence
    • Deshpande K.L., Fried V.A., Ando M., Webster R.G. Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:36-40.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 36-40
    • Deshpande, K.L.1    Fried, V.A.2    Ando, M.3    Webster, R.G.4
  • 10
    • 74549123629 scopus 로고    scopus 로고
    • Identification of amino acids in HA and PB2 critical for the transmission of H5N1 avian influenza viruses in a mammalian host
    • Gao Y., Zhang Y., Shinya K., Deng G., Jiang Y., Li Z., Guan Y., Tian G., Li Y., Shi J. Identification of amino acids in HA and PB2 critical for the transmission of H5N1 avian influenza viruses in a mammalian host. PLoS Pathog. 2009, 5:e1000709.
    • (2009) PLoS Pathog. , vol.5
    • Gao, Y.1    Zhang, Y.2    Shinya, K.3    Deng, G.4    Jiang, Y.5    Li, Z.6    Guan, Y.7    Tian, G.8    Li, Y.9    Shi, J.10
  • 13
    • 0025851040 scopus 로고
    • Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2,3 linkages
    • Hoyer L.L., Roggentin P., Schauer R., Vimr E.R. Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2,3 linkages. J. Biochem. 1991, 110:462-467.
    • (1991) J. Biochem. , vol.110 , pp. 462-467
    • Hoyer, L.L.1    Roggentin, P.2    Schauer, R.3    Vimr, E.R.4
  • 14
    • 84874708826 scopus 로고    scopus 로고
    • The PA-gene-mediated lethal dissemination and excessive innate immune response contribute to the high virulence of H5N1 avian influenza virus in mice
    • Hu J., Hu Z., Song Q., Gu M., Liu X., Wang X., Hu S., Chen C., Liu H., Liu W., Chen S., Peng D. The PA-gene-mediated lethal dissemination and excessive innate immune response contribute to the high virulence of H5N1 avian influenza virus in mice. J. Virol. 2013, 87:2660-2672.
    • (2013) J. Virol. , vol.87 , pp. 2660-2672
    • Hu, J.1    Hu, Z.2    Song, Q.3    Gu, M.4    Liu, X.5    Wang, X.6    Hu, S.7    Chen, C.8    Liu, H.9    Liu, W.10    Chen, S.11    Peng, D.12
  • 15
    • 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
  • 16
    • 84864585610 scopus 로고    scopus 로고
    • N-linked glycosylation in the hemagglutinin of influenza A viruses
    • Kim J.I., Park M.S. N-linked glycosylation in the hemagglutinin of influenza A viruses. Yonsei Med. J. 2012, 53:886-893.
    • (2012) Yonsei Med. J. , vol.53 , pp. 886-893
    • Kim, J.I.1    Park, M.S.2
  • 17
    • 84861302846 scopus 로고    scopus 로고
    • Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin
    • Kobayashi Y., Suzuki Y. Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin. J. Virol. 2012, 86:3446-3451.
    • (2012) J. Virol. , vol.86 , pp. 3446-3451
    • Kobayashi, Y.1    Suzuki, Y.2
  • 19
    • 36049022594 scopus 로고    scopus 로고
    • Influenza virus transmission is dependent on relative humidity and temperature
    • Lowen A.C., Mubareka S., Steel J., Palese P. Influenza virus transmission is dependent on relative humidity and temperature. PLoS Pathog. 2007, 3:1470-1476.
    • (2007) PLoS Pathog. , vol.3 , pp. 1470-1476
    • Lowen, A.C.1    Mubareka, S.2    Steel, J.3    Palese, P.4
  • 20
    • 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
  • 21
    • 66149122168 scopus 로고    scopus 로고
    • Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice
    • Matsuoka Y., Swayne D.E., Thomas C., Rameix-Welti M.A., Naffakh N., Warnes C., Altholtz M., Donis R., Subbarao K. Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice. J. Virol. 2009, 83:4704-4708.
    • (2009) J. Virol. , vol.83 , pp. 4704-4708
    • Matsuoka, Y.1    Swayne, D.E.2    Thomas, C.3    Rameix-Welti, M.A.4    Naffakh, N.5    Warnes, C.6    Altholtz, M.7    Donis, R.8    Subbarao, K.9
  • 22
    • 77956022248 scopus 로고    scopus 로고
    • Thermostability of subpopulations of H2N3 influenza virus isolates from mallard ducks
    • Negovetich N.J., Webster R.G. Thermostability of subpopulations of H2N3 influenza virus isolates from mallard ducks. J. Virol. 2010, 84:9369-9376.
    • (2010) J. Virol. , vol.84 , pp. 9369-9376
    • Negovetich, N.J.1    Webster, R.G.2
  • 23
    • 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
  • 24
    • 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
  • 27
    • 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
  • 28
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed L.J., Muench H. A simple method of estimating fifty percent endpoints. Am. J. Epidemiol. 1938, 27:493-497.
    • (1938) Am. J. Epidemiol. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 29
  • 31
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman J.S., Lamb R.A. Influenza virus assembly and budding. Virology 2011, 411:229-236.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 32
    • 33645278326 scopus 로고    scopus 로고
    • Avian flu: influenza virus receptors in the human airway
    • Shinya K., Ebina M., Yamada S., Ono M., Kasai N., Kawaoka Y. Avian flu: influenza virus receptors in the human airway. Nature 2006, 440:435-436.
    • (2006) Nature , vol.440 , pp. 435-436
    • Shinya, K.1    Ebina, M.2    Yamada, S.3    Ono, M.4    Kasai, N.5    Kawaoka, Y.6
  • 33
    • 0003746861 scopus 로고
    • A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody
    • Skehel J., Stevens D., Daniels R., Douglas A., Knossow M., Wilson I., Wiley D. A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proc. Natl. Acad. Sci. U. S. A. 1984, 81:1779-1783.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 1779-1783
    • Skehel, J.1    Stevens, D.2    Daniels, R.3    Douglas, A.4    Knossow, M.5    Wilson, I.6    Wiley, D.7
  • 35
    • 59249096926 scopus 로고    scopus 로고
    • Transmission of influenza virus in a mammalian host is increased by PB2 amino acids 627K or 627E/701N
    • Steel J., Lowen A.C., Mubareka S., Palese P. Transmission of influenza virus in a mammalian host is increased by PB2 amino acids 627K or 627E/701N. PLoS Pathog. 2009, 5:e1000252.
    • (2009) PLoS Pathog. , vol.5
    • Steel, J.1    Lowen, A.C.2    Mubareka, S.3    Palese, P.4
  • 36
  • 37
    • 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 , pp. e22844
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 38
    • 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
  • 41
    • 58149333269 scopus 로고    scopus 로고
    • Role of amino acid residues at positions 322 and 329 of hemagglutinin in virulence of H5N1 avian influenza virus
    • Tang Y., Wu P., Sun Q., Peng D., Zhang W., Li Y., Wang W., Long J., Zhang P., Liu X. Role of amino acid residues at positions 322 and 329 of hemagglutinin in virulence of H5N1 avian influenza virus. Chin. J. Virol. 2008, 24:340-344.
    • (2008) Chin. J. Virol. , vol.24 , pp. 340-344
    • Tang, Y.1    Wu, P.2    Sun, Q.3    Peng, D.4    Zhang, W.5    Li, Y.6    Wang, W.7    Long, J.8    Zhang, P.9    Liu, X.10
  • 42
    • 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
  • 43
    • 0036936397 scopus 로고    scopus 로고
    • Role of overlapping glycosylation sequons in antigenic properties, intracellular transport and biological activities of influenza A/H2N2 virus haemagglutinin
    • Tsuchiya E., Sugawara K., Hongo S., Matsuzaki Y., Muraki Y., Nakamura K. Role of overlapping glycosylation sequons in antigenic properties, intracellular transport and biological activities of influenza A/H2N2 virus haemagglutinin. J. Gen. Virol. 2002, 83:3067-3074.
    • (2002) J. Gen. Virol. , vol.83 , pp. 3067-3074
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3    Matsuzaki, Y.4    Muraki, Y.5    Nakamura, K.6
  • 46
    • 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
  • 48
    • 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., 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, A.L.4    Cheng, X.5    Subbarao, K.6    Kemble, G.7    Jin, H.8
  • 49
    • 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.
    • (2011) Am. J. Respir. Crit. Care Med. , vol.183 , pp. 767
    • Wanzeck, K.1    Boyd, K.L.2    McCullers, J.A.3
  • 51
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley D., Wilson I., Skehel 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.1    Wilson, I.2    Skehel, J.3
  • 53
    • 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
  • 54
    • 80053620304 scopus 로고    scopus 로고
    • Increase in viral yield in eggs and MDCK cells of reassortant H5N1 vaccine candidate viruses caused by insertion of 38 amino acids into the NA stalk
    • Zhang W., Xue T., Wu X., Zhang P., Zhao G., Peng D., Hu S., Wang X., Liu X., Liu W. Increase in viral yield in eggs and MDCK cells of reassortant H5N1 vaccine candidate viruses caused by insertion of 38 amino acids into the NA stalk. Vaccine 2011, 29:8032-8041.
    • (2011) Vaccine , vol.29 , pp. 8032-8041
    • Zhang, W.1    Xue, T.2    Wu, X.3    Zhang, P.4    Zhao, G.5    Peng, D.6    Hu, S.7    Wang, X.8    Liu, X.9    Liu, W.10
  • 55
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.