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Volumn 413, Issue 1, 2011, Pages 128-138

Receptor specificity of the influenza virus hemagglutinin modulates sensitivity to soluble collectins of the innate immune system and virulence in mice

Author keywords

Hemagglutinin; Influenza; Mouse; Sialic acid; Virulence

Indexed keywords

COLLECTIN; INFLUENZA VIRUS HEMAGGLUTININ; SIALIC ACID; VIRUS RECEPTOR;

EID: 79953107367     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.01.035     Document Type: Article
Times cited : (9)

References (91)
  • 1
    • 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
  • 2
    • 0028344851 scopus 로고
    • Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin
    • Anders E.M., Hartley C.A., Reading P.C., Ezekowitz R.A. Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin. J. Gen. Virol. 1994, 75(Pt 3):615-622.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PT 3 , pp. 615-622
    • Anders, E.M.1    Hartley, C.A.2    Reading, P.C.3    Ezekowitz, R.A.4
  • 3
    • 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
  • 4
    • 0011734245 scopus 로고
    • Adaptation of influenza virus to mice. III. Development of resistance to beta-inhibitor
    • Briody B.A., Cassel W.A., Medill M.A. Adaptation of influenza virus to mice. III. Development of resistance to beta-inhibitor. J. Immunol. 1955, 74:41-45.
    • (1955) J. Immunol. , vol.74 , pp. 41-45
    • Briody, B.A.1    Cassel, W.A.2    Medill, M.A.3
  • 5
    • 0035811003 scopus 로고    scopus 로고
    • Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: identification of functional themes
    • Brown E.G., Liu H., Kit L.C., Baird S., Nesrallah M. Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: identification of functional themes. Proc. Natl Acad. Sci. USA 2001, 98:6883-6888.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6883-6888
    • Brown, E.G.1    Liu, H.2    Kit, L.C.3    Baird, S.4    Nesrallah, M.5
  • 6
    • 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.Y., Poon L.L., Lau A.S., Luk W., Lau Y.L., Shortridge K.F., Gordon S., Guan Y., Peiris J.S. 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.Y.1    Poon, L.L.2    Lau, A.S.3    Luk, W.4    Lau, Y.L.5    Shortridge, K.F.6    Gordon, S.7    Guan, Y.8    Peiris, J.S.9
  • 7
    • 8044253238 scopus 로고
    • The action of normal mouse serum on influenza virus
    • Chu C.M. The action of normal mouse serum on influenza virus. J. Gen. Microbiol. 1951, 5:739-757.
    • (1951) J. Gen. Microbiol. , vol.5 , pp. 739-757
    • Chu, C.M.1
  • 8
    • 36049034216 scopus 로고    scopus 로고
    • A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence
    • Conenello G.M., Zamarin D., Perrone L.A., Tumpey T., Palese P. A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence. PLoS Pathog. 2007, 3:1414-1421.
    • (2007) PLoS Pathog. , vol.3 , pp. 1414-1421
    • Conenello, G.M.1    Zamarin, D.2    Perrone, L.A.3    Tumpey, T.4    Palese, P.5
  • 9
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor R.J., Kawaoka Y., Webster R.G., Paulson J.C. Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 1994, 205:17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 10
    • 0035048532 scopus 로고    scopus 로고
    • Surfactant proteins a and d and pulmonary host defense
    • Crouch E., Wright J.R. Surfactant proteins a and d and pulmonary host defense. Annu. Rev. Physiol. 2001, 63:521-554.
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 521-554
    • Crouch, E.1    Wright, J.R.2
  • 12
    • 0022656816 scopus 로고
    • Variant influenza virus hemagglutinin that induces fusion at elevated pH
    • Doms R.W., Gething M.J., Henneberry J., White J., Helenius A. Variant influenza virus hemagglutinin that induces fusion at elevated pH. J. Virol. 1986, 57:603-613.
    • (1986) J. Virol. , vol.57 , pp. 603-613
    • Doms, R.W.1    Gething, M.J.2    Henneberry, J.3    White, J.4    Helenius, A.5
  • 13
    • 0030917883 scopus 로고    scopus 로고
    • Binding of the influenza A virus to cell-surface receptors: structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography
    • Eisen M.B., Sabesan S., Skehel J.J., Wiley D.C. Binding of the influenza A virus to cell-surface receptors: structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography. Virology 1997, 232:19-31.
    • (1997) Virology , vol.232 , pp. 19-31
    • Eisen, M.B.1    Sabesan, S.2    Skehel, J.J.3    Wiley, D.C.4
  • 14
    • 0000704066 scopus 로고
    • The contribution of sialic acid to the surface charge of the erythrocyte
    • Eylar E.H., Madoff M.A., Brody O.V., Oncley J.L. The contribution of sialic acid to the surface charge of the erythrocyte. J. Biol. Chem. 1962, 237:1992-2000.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1992-2000
    • Eylar, E.H.1    Madoff, M.A.2    Brody, O.V.3    Oncley, J.L.4
  • 16
    • 29444438899 scopus 로고    scopus 로고
    • The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host
    • Gabriel G., Dauber B., Wolff T., Planz O., Klenk H.D., Stech J. The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host. Proc. Natl Acad. Sci. USA 2005, 102:18590-18595.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18590-18595
    • Gabriel, G.1    Dauber, B.2    Wolff, T.3    Planz, O.4    Klenk, H.D.5    Stech, J.6
  • 17
    • 0030737610 scopus 로고    scopus 로고
    • Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers: non-egg-adapted human H1 and H3 influenza A and influenza B viruses share a common high binding affinity for 6'-sialyl(N-acetyllactosamine)
    • Gambaryan A.S., Tuzikov A.B., Piskarev V.E., Yamnikova S.S., Lvov D.K., Robertson J.S., Bovin N.V., Matrosovich M.N. Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers: non-egg-adapted human H1 and H3 influenza A and influenza B viruses share a common high binding affinity for 6'-sialyl(N-acetyllactosamine). Virology 1997, 232:345-350.
    • (1997) Virology , vol.232 , pp. 345-350
    • Gambaryan, A.S.1    Tuzikov, A.B.2    Piskarev, V.E.3    Yamnikova, S.S.4    Lvov, D.K.5    Robertson, J.S.6    Bovin, N.V.7    Matrosovich, M.N.8
  • 18
    • 0033526523 scopus 로고    scopus 로고
    • Effects of egg-adaptation on the receptor-binding properties of human influenza A and B viruses
    • Gambaryan A.S., Robertson J.S., Matrosovich M.N. Effects of egg-adaptation on the receptor-binding properties of human influenza A and B viruses. Virology 1999, 258:232-239.
    • (1999) Virology , vol.258 , pp. 232-239
    • Gambaryan, A.S.1    Robertson, J.S.2    Matrosovich, M.N.3
  • 19
    • 0033014710 scopus 로고    scopus 로고
    • Biological heterogeneity, including systemic replication in mice, of H5N1 influenza A virus isolates from humans in Hong Kong
    • Gao P., Watanabe S., Ito T., Goto H., Wells K., McGregor M., Cooley A.J., Kawaoka Y. Biological heterogeneity, including systemic replication in mice, of H5N1 influenza A virus isolates from humans in Hong Kong. J. Virol. 1999, 73:3184-3189.
    • (1999) J. Virol. , vol.73 , pp. 3184-3189
    • Gao, P.1    Watanabe, S.2    Ito, T.3    Goto, H.4    Wells, K.5    McGregor, M.6    Cooley, A.J.7    Kawaoka, Y.8
  • 20
    • 0029979088 scopus 로고    scopus 로고
    • Two evolutionary strategies of influenza viruses to escape host non-specific inhibitors: alteration of hemagglutinin or neuraminidase specificity
    • Gimsa U., Grotzinger I., Gimsa J. Two evolutionary strategies of influenza viruses to escape host non-specific inhibitors: alteration of hemagglutinin or neuraminidase specificity. Virus Res. 1996, 42:127-135.
    • (1996) Virus Res. , vol.42 , pp. 127-135
    • Gimsa, U.1    Grotzinger, I.2    Gimsa, J.3
  • 21
    • 34248214025 scopus 로고    scopus 로고
    • Effective replication of human influenza viruses in mice lacking a major alpha2, 6 sialyltransferase
    • Glaser L., Conenello G., Paulson J., Palese P. Effective replication of human influenza viruses in mice lacking a major alpha2, 6 sialyltransferase. Virus Res. 2007, 126:9-18.
    • (2007) Virus Res. , vol.126 , pp. 9-18
    • Glaser, L.1    Conenello, G.2    Paulson, J.3    Palese, P.4
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta M., Gao P., Halfmann P., Kawaoka Y. Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 2001, 293:1840-1842.
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 26
    • 33847683732 scopus 로고    scopus 로고
    • Pathogeneses of respiratory infections with virulent and attenuated vaccinia viruses
    • Hayasaka D., Ennis F.A., Terajima M. Pathogeneses of respiratory infections with virulent and attenuated vaccinia viruses. Virol. J. 2007, 4:22.
    • (2007) Virol. J. , vol.4 , pp. 22
    • Hayasaka, D.1    Ennis, F.A.2    Terajima, M.3
  • 30
    • 0037135677 scopus 로고    scopus 로고
    • Eight-plasmid system for rapid generation of influenza virus vaccines
    • Hoffmann E., Krauss S., Perez D., Webby R., Webster R.G. Eight-plasmid system for rapid generation of influenza virus vaccines. Vaccine 2002, 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
  • 31
    • 0030986645 scopus 로고    scopus 로고
    • Susceptibility of mononuclear phagocytes to influenza A virus infection and possible role in the antiviral response
    • Hofmann P., Sprenger H., Kaufmann A., Bender A., Hasse C., Nain M., Gemsa D. Susceptibility of mononuclear phagocytes to influenza A virus infection and possible role in the antiviral response. J. Leukoc. Biol. 1997, 61:408-414.
    • (1997) J. Leukoc. Biol. , vol.61 , pp. 408-414
    • Hofmann, P.1    Sprenger, H.2    Kaufmann, A.3    Bender, A.4    Hasse, C.5    Nain, M.6    Gemsa, D.7
  • 32
    • 0035559445 scopus 로고    scopus 로고
    • Universal primer set for the full-length amplification of all influenza A viruses
    • Hoffmann E., Stech J., Guan Y., Webster R.G., Perez D.R. Universal primer set for the full-length amplification of all influenza A viruses. Arch. Virol. 2001, 146:2275-2289.
    • (2001) Arch. Virol. , vol.146 , pp. 2275-2289
    • Hoffmann, E.1    Stech, J.2    Guan, Y.3    Webster, R.G.4    Perez, D.R.5
  • 34
    • 0031579234 scopus 로고    scopus 로고
    • Receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species
    • Ito T., Suzuki Y., Mitnaul L., Vines A., Kida H., Kawaoka Y. Receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species. Virology 1997, 227:493-499.
    • (1997) Virology , vol.227 , pp. 493-499
    • Ito, T.1    Suzuki, Y.2    Mitnaul, L.3    Vines, A.4    Kida, H.5    Kawaoka, Y.6
  • 35
    • 0030981954 scopus 로고    scopus 로고
    • Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection
    • Ito T., Suzuki Y., Takada A., Kawamoto A., Otsuki K., Masuda H., Yamada M., Suzuki T., Kida H., Kawaoka Y. Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection. J. Virol. 1997, 71:3357-3362.
    • (1997) J. Virol. , vol.71 , pp. 3357-3362
    • Ito, T.1    Suzuki, Y.2    Takada, A.3    Kawamoto, A.4    Otsuki, K.5    Masuda, H.6    Yamada, M.7    Suzuki, T.8    Kida, H.9    Kawaoka, Y.10
  • 36
    • 56449102489 scopus 로고    scopus 로고
    • Experimental evolution of human influenza virus H3 hemagglutinin in the mouse lung identifies adaptive regions in HA1 and HA2
    • Keleta L., Ibricevic A., Bovin N.V., Brody S.L., Brown E.G. Experimental evolution of human influenza virus H3 hemagglutinin in the mouse lung identifies adaptive regions in HA1 and HA2. J. Virol. 2008, 82:11599-11608.
    • (2008) J. Virol. , vol.82 , pp. 11599-11608
    • Keleta, L.1    Ibricevic, A.2    Bovin, N.V.3    Brody, S.L.4    Brown, E.G.5
  • 37
    • 18044386993 scopus 로고    scopus 로고
    • Improvement of influenza A/Fujian/411/02 (H3N2) virus growth in embryonated chicken eggs by balancing the hemagglutinin and neuraminidase activities, using reverse genetics
    • Lu B., Zhou H., Ye D., Kemble G., Jin H. Improvement of influenza A/Fujian/411/02 (H3N2) virus growth in embryonated chicken eggs by balancing the hemagglutinin and neuraminidase activities, using reverse genetics. J. Virol. 2005, 79:6763-6771.
    • (2005) J. Virol. , vol.79 , pp. 6763-6771
    • Lu, B.1    Zhou, H.2    Ye, D.3    Kemble, G.4    Jin, H.5
  • 38
    • 34347261987 scopus 로고    scopus 로고
    • Acute lung injury/acute respiratory distress syndrome (ALI/ARDS): the mechanism, present strategies and future perspectives of therapies
    • Luh S.P., Chiang C.H. Acute lung injury/acute respiratory distress syndrome (ALI/ARDS): the mechanism, present strategies and future perspectives of therapies. J. Zhejiang Univ. Sci. B 2007, 8:60-69.
    • (2007) J. Zhejiang Univ. Sci. B , vol.8 , pp. 60-69
    • Luh, S.P.1    Chiang, C.H.2
  • 39
    • 0032493798 scopus 로고    scopus 로고
    • Screening of N-acylneuraminic acids in serum and tissue specimens of mouse C57BI with Lewis' lung cancer by high-performance liquid chromatography
    • Makatsori E., Fermani K., Aletras A., Karamanos N.K., Tsegenidis T. Screening of N-acylneuraminic acids in serum and tissue specimens of mouse C57BI with Lewis' lung cancer by high-performance liquid chromatography. J. Chromatogr. B Biomed. Sci. Appl. 1998, 712:23-29.
    • (1998) J. Chromatogr. B Biomed. Sci. Appl. , vol.712 , pp. 23-29
    • Makatsori, E.1    Fermani, K.2    Aletras, A.3    Karamanos, N.K.4    Tsegenidis, T.5
  • 40
    • 0344289526 scopus 로고    scopus 로고
    • Ganglioside expression in tissues of mice lacking the tumor necrosis factor receptor 1
    • Markotic A., Lumen R., Marusic A., Jonjic S., Muthing J. Ganglioside expression in tissues of mice lacking the tumor necrosis factor receptor 1. Carbohydr. Res. 1999, 321:75-87.
    • (1999) Carbohydr. Res. , vol.321 , pp. 75-87
    • Markotic, A.1    Lumen, R.2    Marusic, A.3    Jonjic, S.4    Muthing, J.5
  • 41
    • 0030748536 scopus 로고    scopus 로고
    • Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site
    • Matrosovich M.N., Gambaryan A.S., Teneberg S., Piskarev V.E., Yamnikova S.S., Lvov D.K., Robertson J.S., Karlsson K.A. Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 1997, 233:224-234.
    • (1997) Virology , vol.233 , pp. 224-234
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Teneberg, S.3    Piskarev, V.E.4    Yamnikova, S.S.5    Lvov, D.K.6    Robertson, J.S.7    Karlsson, K.A.8
  • 42
    • 0031902989 scopus 로고    scopus 로고
    • Molecular mechanisms of serum resistance of human influenza H3N2 virus and their involvement in virus adaptation in a new host
    • Matrosovich M., Gao P., Kawaoka Y. Molecular mechanisms of serum resistance of human influenza H3N2 virus and their involvement in virus adaptation in a new host. J. Virol. 1998, 72:6373-6380.
    • (1998) J. Virol. , vol.72 , pp. 6373-6380
    • Matrosovich, M.1    Gao, P.2    Kawaoka, Y.3
  • 43
    • 1842585032 scopus 로고    scopus 로고
    • Human and avian influenza viruses target different cell types in cultures of human airway epithelium
    • Matrosovich M.N., Matrosovich T.Y., Gray T., Roberts N.A., Klenk H.D. Human and avian influenza viruses target different cell types in cultures of human airway epithelium. Proc. Natl Acad. Sci. USA 2004, 101:4620-4624.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4620-4624
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 44
    • 18844448981 scopus 로고    scopus 로고
    • A single amino acid change in the C-terminal domain of the matrix protein M1 of influenza B virus confers mouse adaptation and virulence
    • McCullers J.A., Hoffmann E., Huber V.C., Nickerson A.D. A single amino acid change in the C-terminal domain of the matrix protein M1 of influenza B virus confers mouse adaptation and virulence. Virology 2005, 336:318-326.
    • (2005) Virology , vol.336 , pp. 318-326
    • McCullers, J.A.1    Hoffmann, E.2    Huber, V.C.3    Nickerson, A.D.4
  • 45
    • 0035840797 scopus 로고    scopus 로고
    • Hemagglutinin residues of recent human A(H3N2) influenza viruses that contribute to the inability to agglutinate chicken erythrocytes
    • Medeiros R., Escriou N., Naffakh N., Manuguerra J.C., van der Werf S. Hemagglutinin residues of recent human A(H3N2) influenza viruses that contribute to the inability to agglutinate chicken erythrocytes. Virology 2001, 289:74-85.
    • (2001) Virology , vol.289 , pp. 74-85
    • Medeiros, R.1    Escriou, N.2    Naffakh, N.3    Manuguerra, J.C.4    van der Werf, S.5
  • 46
    • 4043177653 scopus 로고    scopus 로고
    • Binding of the hemagglutinin from human or equine influenza H3 viruses to the receptor is altered by substitutions at residue 193
    • Medeiros R., Naffakh N., Manuguerra J.C., van der Werf S. Binding of the hemagglutinin from human or equine influenza H3 viruses to the receptor is altered by substitutions at residue 193. Arch. Virol. 2004, 149:1663-1671.
    • (2004) Arch. Virol. , vol.149 , pp. 1663-1671
    • Medeiros, R.1    Naffakh, N.2    Manuguerra, J.C.3    van der Werf, S.4
  • 47
    • 70949102147 scopus 로고    scopus 로고
    • Detection of expression of influenza virus receptors in tissues of BALB/c mice by histochemistry
    • Ning Z.Y., Luo M.Y., Qi W.B., Yu B., Jiao P.R., Liao M. Detection of expression of influenza virus receptors in tissues of BALB/c mice by histochemistry. Vet. Res. Commun. 2009, 33:895-903.
    • (2009) Vet. Res. Commun. , vol.33 , pp. 895-903
    • Ning, Z.Y.1    Luo, M.Y.2    Qi, W.B.3    Yu, B.4    Jiao, P.R.5    Liao, M.6
  • 48
    • 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
  • 49
    • 0034532059 scopus 로고    scopus 로고
    • Change in receptor-binding specificity of recent human influenza A viruses (H3N2): a single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides
    • Nobusawa E., Ishihara H., Morishita T., Sato K., Nakajima K. Change in receptor-binding specificity of recent human influenza A viruses (H3N2): a single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides. Virology 2000, 278:587-596.
    • (2000) Virology , vol.278 , pp. 587-596
    • Nobusawa, E.1    Ishihara, H.2    Morishita, T.3    Sato, K.4    Nakajima, K.5
  • 50
    • 0025899105 scopus 로고
    • Thymic atrophy in type 2 reovirus infected mice: immunosuppression and effects of thymic hormone. Thymic atrophy caused by reo-2
    • Onodera T., Taniguchi T., Tsuda T., Yoshihara K., Shimizu S., Sato M., Awaya A., Hayashi T. Thymic atrophy in type 2 reovirus infected mice: immunosuppression and effects of thymic hormone. Thymic atrophy caused by reo-2. Thymus 1991, 18:95-109.
    • (1991) Thymus , vol.18 , pp. 95-109
    • Onodera, T.1    Taniguchi, T.2    Tsuda, T.3    Yoshihara, K.4    Shimizu, S.5    Sato, M.6    Awaya, A.7    Hayashi, T.8
  • 52
    • 61649123517 scopus 로고    scopus 로고
    • Sialic acid recognition is a key determinant of influenza A virus tropism in murine trachea epithelial cell cultures
    • Pekosz A., Newby C., Bose P.S., Lutz A. Sialic acid recognition is a key determinant of influenza A virus tropism in murine trachea epithelial cell cultures. Virology 2009, 386:61-67.
    • (2009) Virology , vol.386 , pp. 61-67
    • Pekosz, A.1    Newby, C.2    Bose, P.S.3    Lutz, A.4
  • 53
    • 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 L.A., Plowden J.K., Garcia-Sastre A., Katz J.M., Tumpey T.M. 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.
    • (2008) PLoS Pathog. , vol.4
    • Perrone, L.A.1    Plowden, J.K.2    Garcia-Sastre, A.3    Katz, J.M.4    Tumpey, T.M.5
  • 54
    • 77049100507 scopus 로고    scopus 로고
    • Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys
    • Pillai S.P., Lee C.W. Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys. Virol. J. 2010, 7:5.
    • (2010) Virol. J. , vol.7 , pp. 5
    • Pillai, S.P.1    Lee, C.W.2
  • 55
    • 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
  • 56
    • 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
  • 57
    • 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
  • 58
    • 77955656446 scopus 로고    scopus 로고
    • Influenza viruses differ in ability to infect macrophages and to induce a local inflammatory response following intraperitoneal injection of mice
    • Reading P.C., Whitney P.G., Pickett D.L., Tate M.D., Brooks A.G. Influenza viruses differ in ability to infect macrophages and to induce a local inflammatory response following intraperitoneal injection of mice. Immunol. Cell Biol. 2010, 88:641-650.
    • (2010) Immunol. Cell Biol. , vol.88 , pp. 641-650
    • Reading, P.C.1    Whitney, P.G.2    Pickett, D.L.3    Tate, M.D.4    Brooks, A.G.5
  • 59
    • 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
  • 60
    • 0020520729 scopus 로고
    • Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin
    • Rogers G.N., Paulson J.C. Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 1983, 127:361-373.
    • (1983) Virology , vol.127 , pp. 361-373
    • Rogers, G.N.1    Paulson, J.C.2
  • 63
    • 0025958279 scopus 로고
    • Distinct glycoprotein inhibitors of influenza A virus in different animal sera
    • Ryan-Poirier K.A., Kawaoka Y. Distinct glycoprotein inhibitors of influenza A virus in different animal sera. J. Virol. 1991, 65:389-395.
    • (1991) J. Virol. , vol.65 , pp. 389-395
    • Ryan-Poirier, K.A.1    Kawaoka, Y.2
  • 64
    • 0027175267 scopus 로고
    • Alpha 2-macroglobulin is the major neutralizing inhibitor of influenza A virus in pig serum
    • Ryan-Poirier K.A., Kawaoka Y. Alpha 2-macroglobulin is the major neutralizing inhibitor of influenza A virus in pig serum. Virology 1993, 193:974-976.
    • (1993) Virology , vol.193 , pp. 974-976
    • Ryan-Poirier, K.A.1    Kawaoka, Y.2
  • 65
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • Sauter N.K., Hanson J.E., Glick G.D., Brown J.H., Crowther R.L., Park S.J., Skehel J.J., Wiley D.C. Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 1992, 31:9609-9621.
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1    Hanson, J.E.2    Glick, G.D.3    Brown, J.H.4    Crowther, R.L.5    Park, S.J.6    Skehel, J.J.7    Wiley, D.C.8
  • 66
    • 0028478322 scopus 로고
    • Changes in its hemagglutinin during the adaptation of the influenza virus to mice and their role in the acquisition of virulent properties and resistance to serum inhibitors
    • Shilov A.A., Sinitsyn B.V. Changes in its hemagglutinin during the adaptation of the influenza virus to mice and their role in the acquisition of virulent properties and resistance to serum inhibitors. Vopr. Virusol. 1994, 39:153-157.
    • (1994) Vopr. Virusol. , vol.39 , pp. 153-157
    • Shilov, A.A.1    Sinitsyn, B.V.2
  • 67
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 2000, 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 68
    • 0030271198 scopus 로고    scopus 로고
    • Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis
    • Smeenk C.A., Wright K.E., Burns B.F., Thaker A.J., Brown E.G. Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis. Virus Res. 1996, 44:79-95.
    • (1996) Virus Res. , vol.44 , pp. 79-95
    • Smeenk, C.A.1    Wright, K.E.2    Burns, B.F.3    Thaker, A.J.4    Brown, E.G.5
  • 70
    • 0033563211 scopus 로고    scopus 로고
    • Long term prevention of allergic lung inflammation in a mouse model of asthma by CpG oligodeoxynucleotides
    • Sur S., Wild J.S., Choudhury B.K., Sur N., Alam R., Klinman D.M. Long term prevention of allergic lung inflammation in a mouse model of asthma by CpG oligodeoxynucleotides. J. Immunol. 1999, 162:6284-6293.
    • (1999) J. Immunol. , vol.162 , pp. 6284-6293
    • Sur, S.1    Wild, J.S.2    Choudhury, B.K.3    Sur, N.4    Alam, R.5    Klinman, D.M.6
  • 71
    • 0021894206 scopus 로고
    • N-Acetylneuraminyllactosylceramide, GM3-NeuAc, a new influenza A virus receptor which mediates the adsorption-fusion process of viral infection. Binding specificity of influenza virus A/Aichi/2/68 (H3N2) to membrane-associated GM3 with different molecular species of sialic acid
    • Suzuki Y., Matsunaga M., Matsumoto M. N-Acetylneuraminyllactosylceramide, GM3-NeuAc, a new influenza A virus receptor which mediates the adsorption-fusion process of viral infection. Binding specificity of influenza virus A/Aichi/2/68 (H3N2) to membrane-associated GM3 with different molecular species of sialic acid. J. Biol. Chem. 1985, 260:1362-1365.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1362-1365
    • Suzuki, Y.1    Matsunaga, M.2    Matsumoto, M.3
  • 72
    • 0022970310 scopus 로고
    • Human influenza A virus hemagglutinin distinguishes sialyloligosaccharides in membrane-associated gangliosides as its receptor which mediates the adsorption and fusion processes of virus infection. Specificity for oligosaccharides and sialic acids and the sequence to which sialic acid is attached
    • Suzuki Y., Nagao Y., Kato H., Matsumoto M., Nerome K., Nakajima K., Nobusawa E. Human influenza A virus hemagglutinin distinguishes sialyloligosaccharides in membrane-associated gangliosides as its receptor which mediates the adsorption and fusion processes of virus infection. Specificity for oligosaccharides and sialic acids and the sequence to which sialic acid is attached. J. Biol. Chem. 1986, 261:17057-17061.
    • (1986) J. Biol. Chem. , vol.261 , pp. 17057-17061
    • Suzuki, Y.1    Nagao, Y.2    Kato, H.3    Matsumoto, M.4    Nerome, K.5    Nakajima, K.6    Nobusawa, E.7
  • 74
    • 0019297043 scopus 로고
    • Pathogenicity of influenza virus
    • Sweet C., Smith H. Pathogenicity of influenza virus. Microbiol. Rev. 1980, 44:303-330.
    • (1980) Microbiol. Rev. , vol.44 , pp. 303-330
    • Sweet, C.1    Smith, H.2
  • 75
    • 52649136695 scopus 로고    scopus 로고
    • The role of neutrophils in the upper and lower respiratory tract during influenza virus infection of mice
    • Tate M.D., Brooks A.G., Reading P.C. The role of neutrophils in the upper and lower respiratory tract during influenza virus infection of mice. Respir. Res. 2008, 9:57.
    • (2008) Respir. Res. , vol.9 , pp. 57
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 76
    • 73349124131 scopus 로고    scopus 로고
    • Neutrophils ameliorate lung injury and the development of severe disease during influenza infection
    • Tate M.D., Deng Y.M., Jones J.E., Anderson G.P., Brooks A.G., Reading P.C. Neutrophils ameliorate lung injury and the development of severe disease during influenza infection. J. Immunol. 2009, 183:7441-7450.
    • (2009) J. Immunol. , vol.183 , pp. 7441-7450
    • Tate, M.D.1    Deng, Y.M.2    Jones, J.E.3    Anderson, G.P.4    Brooks, A.G.5    Reading, P.C.6
  • 77
    • 79953126078 scopus 로고    scopus 로고
    • Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection. Immunol Cell Bio. In press.
    • Tate, M.D., Brooks, A.G., Reading, P.C., 2010a. Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection. Immunol Cell Bio. In press.
    • (2010)
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 78
    • 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
  • 79
    • 78651505939 scopus 로고    scopus 로고
    • Correlation between sialic acid expression and infection of murine macrophages by different strains of influenza virus
    • Tate M.D., Brooks A.G., Reading P.C. Correlation between sialic acid expression and infection of murine macrophages by different strains of influenza virus. Microb. Infect. 2011, 13:202-207.
    • (2011) Microb. Infect. , vol.13 , pp. 202-207
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 81
    • 0034051290 scopus 로고    scopus 로고
    • Depletion of lymphocytes and diminished cytokine production in mice infected with a highly virulent influenza A (H5N1) virus isolated from humans
    • Tumpey T.M., Lu X., Morken T., Zaki S.R., Katz J.M. Depletion of lymphocytes and diminished cytokine production in mice infected with a highly virulent influenza A (H5N1) virus isolated from humans. J. Virol. 2000, 74:6105-6116.
    • (2000) J. Virol. , vol.74 , pp. 6105-6116
    • Tumpey, T.M.1    Lu, X.2    Morken, T.3    Zaki, S.R.4    Katz, J.M.5
  • 83
    • 0031820967 scopus 로고    scopus 로고
    • The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction
    • Vines A., Wells K., Matrosovich M., Castrucci M.R., Ito T., Kawaoka Y. The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction. J. Virol. 1998, 72:7626-7631.
    • (1998) J. Virol. , vol.72 , pp. 7626-7631
    • Vines, A.1    Wells, K.2    Matrosovich, M.3    Castrucci, M.R.4    Ito, T.5    Kawaoka, Y.6
  • 84
    • 0036090557 scopus 로고    scopus 로고
    • Functional balance between haemagglutinin and neuraminidase in influenza virus infections
    • Wagner R., Matrosovich M., Klenk H.D. Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev. Med. Virol. 2002, 12:159-166.
    • (2002) Rev. Med. Virol. , vol.12 , pp. 159-166
    • Wagner, R.1    Matrosovich, M.2    Klenk, H.D.3
  • 85
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W., Brown J.H., Cusack S., Paulson J.C., Skehel J.J., Wiley D.C. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 1988, 333:426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 86
    • 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
  • 88
    • 33745040229 scopus 로고    scopus 로고
    • Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs
    • Widjaja L., Ilyushina N., Webster R.G., Webby R.J. Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs. Virology 2006, 350:137-145.
    • (2006) Virology , vol.350 , pp. 137-145
    • Widjaja, L.1    Ilyushina, N.2    Webster, R.G.3    Webby, R.J.4
  • 89
    • 0017356912 scopus 로고
    • Effects of low- and high-passage influenza virus infection in normal and nude mice
    • Wyde P.R., Couch R.B., Mackler B.F., Cate T.R., Levy B.M. Effects of low- and high-passage influenza virus infection in normal and nude mice. Infect. Immun. 1977, 15:221-229.
    • (1977) Infect. Immun. , vol.15 , pp. 221-229
    • Wyde, P.R.1    Couch, R.B.2    Mackler, B.F.3    Cate, T.R.4    Levy, B.M.5
  • 90
    • 0027815143 scopus 로고
    • Polymorphonuclear leukocytes as a significant source of tumor necrosis factor-alpha in endotoxin-challenged lung tissue
    • Xing Z., Kirpalani H., Torry D., Jordana M., Gauldie J. Polymorphonuclear leukocytes as a significant source of tumor necrosis factor-alpha in endotoxin-challenged lung tissue. Am. J. Pathol. 1993, 143:1009-1015.
    • (1993) Am. J. Pathol. , vol.143 , pp. 1009-1015
    • Xing, Z.1    Kirpalani, H.2    Torry, D.3    Jordana, M.4    Gauldie, J.5


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