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Volumn 7, Issue 5, 2012, Pages

A novel pathogenic mechanism of highly pathogenic avian influenza H5N1 viruses involves hemagglutinin mediated resistance to serum innate inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; HEMAGGLUTININ; INNATE SERUM INHIBITOR; SIALIDASE; UNCLASSIFIED DRUG; HEMAGGLUTININ, AVIAN INFLUENZA A VIRUS; INFLUENZA VIRUS HEMAGGLUTININ; RECOMBINANT PROTEIN; VIRUS ANTIGEN;

EID: 84860475769     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036318     Document Type: Article
Times cited : (8)

References (41)
  • 1
    • 38349068756 scopus 로고    scopus 로고
    • Update on avian influenza A (H5N1) virus infection in humans
    • Writing Committee of the Second World Health Organization Consultation on Clinical Aspects of Human Infection with Avian Influenza A (H5N1) Virus
    • Abdel-Ghafar AN, Chotpitayasunondh T, Gao Z, Hayden FG, Nguyen DH, et al. Writing Committee of the Second World Health Organization Consultation on Clinical Aspects of Human Infection with Avian Influenza A (H5N1) Virus (2008) Update on avian influenza A (H5N1) virus infection in humans. N Engl J Med 358: 261-273.
    • (2008) N Engl J Med , vol.358 , pp. 261-273
    • Abdel-Ghafar, A.N.1    Chotpitayasunondh, T.2    Gao, Z.3    Hayden, F.G.4    Nguyen, D.H.5
  • 2
    • 34248170234 scopus 로고    scopus 로고
    • Avian influenza virus (H5N1): a threat to human health
    • Peiris JS, de Jong MD, Guan Y, (2007) Avian influenza virus (H5N1): a threat to human health. Clin Microbiol Rev 20: 243-267.
    • (2007) Clin Microbiol Rev , vol.20 , pp. 243-267
    • Peiris, J.S.1    de Jong, M.D.2    Guan, Y.3
  • 4
    • 13744258437 scopus 로고    scopus 로고
    • Fatal avian influenza A (H5N1) in a child presenting with diarrhea followed by coma
    • de Jong MD, Bach VC, Phan TQ, Vo MH, Tran TT, et al. (2005) Fatal avian influenza A (H5N1) in a child presenting with diarrhea followed by coma. N Engl J Med 352: 686-691.
    • (2005) N Engl J Med , vol.352 , pp. 686-691
    • de Jong, M.D.1    Bach, V.C.2    Phan, T.Q.3    Vo, M.H.4    Tran, T.T.5
  • 5
    • 34648840650 scopus 로고    scopus 로고
    • H5N1 infection of the respiratory tract and beyond: a molecular pathology study
    • Gu J, Xie Z, Gao Z, Liu J, Korteweg C, et al. (2007) H5N1 infection of the respiratory tract and beyond: a molecular pathology study. Lancet 370: 1137-1145.
    • (2007) Lancet , vol.370 , pp. 1137-1145
    • Gu, J.1    Xie, Z.2    Gao, Z.3    Liu, J.4    Korteweg, C.5
  • 7
    • 80053206038 scopus 로고    scopus 로고
    • Clinical and virological factors associated with viremia in pandemic influenza A/H1N1/2009 virus infection
    • Tse H, To KK, Wen X, Chen H, Chan KH, et al. (2011) Clinical and virological factors associated with viremia in pandemic influenza A/H1N1/2009 virus infection. PLoS One 6: e22534.
    • (2011) PLoS One , vol.6
    • Tse, H.1    To, K.K.2    Wen, X.3    Chen, H.4    Chan, K.H.5
  • 8
    • 0001584990 scopus 로고
    • Human influenza infection with proved viremia-Report of a case
    • Naficy K, (1963) Human influenza infection with proved viremia-Report of a case. N Engl J Med 269: 964-966.
    • (1963) N Engl J Med , vol.269 , pp. 964-966
    • Naficy, K.1
  • 9
    • 0014691144 scopus 로고
    • Proved viraemia in Asian influenza (Hong Kong variant) during incubation period
    • Khakpour M, Saidi A, Naficy K, (1969) Proved viraemia in Asian influenza (Hong Kong variant) during incubation period. Br Med J 4: 208-209.
    • (1969) Br Med J , vol.4 , pp. 208-209
    • Khakpour, M.1    Saidi, A.2    Naficy, K.3
  • 10
    • 0031242322 scopus 로고    scopus 로고
    • Viremia in influenza: detection by polymerase chain reaction
    • Tsuruoka H, Xu H, Kuroda K, Hosaka Y, (1997) Viremia in influenza: detection by polymerase chain reaction. Nihon Rinsho 55: 2714-2718.
    • (1997) Nihon Rinsho , vol.55 , pp. 2714-2718
    • Tsuruoka, H.1    Xu, H.2    Kuroda, K.3    Hosaka, Y.4
  • 11
    • 0031416787 scopus 로고    scopus 로고
    • Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins
    • Hartshorn KL, White MR, Shepherd V, Reid K, Jensenius JC, et al. (1997) Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins. Am J Physiol 273 (6 Pt 1): L1156-L1166.
    • (1997) Am J Physiol , vol.273 , Issue.6 Pt
    • Hartshorn, K.L.1    White, M.R.2    Shepherd, V.3    Reid, K.4    Jensenius, J.C.5
  • 12
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice
    • Reading PC, Morey LS, Crouch EC, Anders EM, (1997) Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice. J Virol 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
  • 13
    • 0037675777 scopus 로고    scopus 로고
    • Surfactant protein D (SP-D) serum levels in patients with community-acquired pneumonia
    • Leth-Larsen R, Nordenbaek C, Tornoe I, Moeller V, Schlosser A, et al. (2003) Surfactant protein D (SP-D) serum levels in patients with community-acquired pneumonia. Clin Immunol 108: 29-37.
    • (2003) Clin Immunol , vol.108 , pp. 29-37
    • Leth-Larsen, R.1    Nordenbaek, C.2    Tornoe, I.3    Moeller, V.4    Schlosser, A.5
  • 14
    • 46149126526 scopus 로고    scopus 로고
    • Antiviral activity of the long chain pentraxin PTX3 against influenza viruses
    • Reading PC, Bozza S, Gilbertson B, Tate M, Moretti S, et al. (2008) Antiviral activity of the long chain pentraxin PTX3 against influenza viruses. J Immunol 180: 3391-3398.
    • (2008) J Immunol , vol.180 , pp. 3391-3398
    • Reading, P.C.1    Bozza, S.2    Gilbertson, B.3    Tate, M.4    Moretti, S.5
  • 15
    • 0034862518 scopus 로고    scopus 로고
    • Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies
    • Horváth A, Andersen I, Junker K, Lyck Fogh-Schultz B, Holm Nielsen E, et al. (2001) Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies. Antiviral Res 52: 43-53.
    • (2001) Antiviral Res , vol.52 , pp. 43-53
    • Horváth, A.1    Andersen, I.2    Junker, K.3    Lyck Fogh-Schultz, B.4    Holm Nielsen, E.5
  • 16
    • 0032973147 scopus 로고    scopus 로고
    • Human mannan-binding lectin inhibits the infection of influenza A virus without complement
    • Kase T, Suzuki Y, Kawai T, Sakamoto T, Ohtani K, et al. (1999) Human mannan-binding lectin inhibits the infection of influenza A virus without complement. Immunology 97: 385-392.
    • (1999) Immunology , vol.97 , pp. 385-392
    • Kase, T.1    Suzuki, Y.2    Kawai, T.3    Sakamoto, T.4    Ohtani, K.5
  • 17
    • 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 ER, Deng YM, Tate MD, Bottazzi B, Crouch EC, et al. (2010) Pandemic H1N1 influenza A viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies. J Immunol 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
  • 18
    • 1342279570 scopus 로고    scopus 로고
    • The relevance of complement to virus biology
    • Blue CE, Spiller OB, Blackbourn DJ, (2004) The relevance of complement to virus biology. Virology 319: 176-184.
    • (2004) Virology , vol.319 , pp. 176-184
    • Blue, C.E.1    Spiller, O.B.2    Blackbourn, D.J.3
  • 19
    • 0029561157 scopus 로고
    • A serum mannose binding lectin mediates complement dependent lysis of influenza virus-infected cells
    • Reading PC, Hartley CA, Ezekowitz RA, Anders EM, (1995) A serum mannose binding lectin mediates complement dependent lysis of influenza virus-infected cells. Biochem Biophys Res Commun 26: 1128-1136.
    • (1995) Biochem Biophys Res Commun , vol.26 , pp. 1128-1136
    • Reading, P.C.1    Hartley, C.A.2    Ezekowitz, R.A.3    Anders, E.M.4
  • 20
    • 0028344851 scopus 로고
    • Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin
    • Anders EM, Hartley CA, Reading PC, Ezekowitz RA, (1994) Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin. J Gen Virol 75: 615-622.
    • (1994) J Gen Virol , vol.75 , pp. 615-622
    • Anders, E.M.1    Hartley, C.A.2    Reading, P.C.3    Ezekowitz, R.A.4
  • 21
    • 33947434002 scopus 로고    scopus 로고
    • Natural antibody and complement mediate neutralization of influenza virus in the absence of prior immunity
    • Jayasekera JP, Moseman EA, Carroll MC, (2007) Natural antibody and complement mediate neutralization of influenza virus in the absence of prior immunity. J Virol 81: 3487-3494.
    • (2007) J Virol , vol.81 , pp. 3487-3494
    • Jayasekera, J.P.1    Moseman, E.A.2    Carroll, M.C.3
  • 22
    • 50549175163 scopus 로고
    • The influenza virus hemagglutination inhibitors of normal rabbit serum: I. Separation of the inhibitory components
    • Cohen A, Belyavin G, (1961) The influenza virus hemagglutination inhibitors of normal rabbit serum: I. Separation of the inhibitory components. Virology 13: 58-67.
    • (1961) Virology , vol.13 , pp. 58-67
    • Cohen, A.1    Belyavin, G.2
  • 24
    • 0025298243 scopus 로고
    • Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins
    • Anders E, Hartley C, Jackson D, (1990) Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins. Proc Natl Acad Sci U S A 87: 4485-4489.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4485-4489
    • Anders, E.1    Hartley, C.2    Jackson, D.3
  • 25
    • 0024360659 scopus 로고
    • Basis for the potent inhibition of influenza virus infection by equine and guinea pig α2-macroglobulin
    • Pritchett TJ, Paulson JC, (1989) Basis for the potent inhibition of influenza virus infection by equine and guinea pig α2-macroglobulin. J Biol Chem 15: 9850-9858.
    • (1989) J Biol Chem , vol.15 , pp. 9850-9858
    • Pritchett, T.J.1    Paulson, J.C.2
  • 26
    • 84857039318 scopus 로고    scopus 로고
    • Contribution of murine innate serum inhibitors toward interference within influenza virus immune assays
    • Cwach KT, Sandbulte HR, Klonoski JM, Huber VC, (2012) Contribution of murine innate serum inhibitors toward interference within influenza virus immune assays. Influenza Other Respi Viruses 6: 127-135.
    • (2012) Influenza Other Respi Viruses , vol.6 , pp. 127-135
    • Cwach, K.T.1    Sandbulte, H.R.2    Klonoski, J.M.3    Huber, V.C.4
  • 27
    • 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
  • 28
    • 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 MD, Job ER, Brooks AG, Reading PC, (2011) Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice. Virology 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
  • 29
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA, (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41: 95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 30
    • 79952140653 scopus 로고    scopus 로고
    • Influenza virus vaccine based on the conserved hemagglutinin stalk domain
    • Steel J, Lowen AC, Wang TT, Yondola M, Gao Q, et al. (2010) Influenza virus vaccine based on the conserved hemagglutinin stalk domain. MBio 1: e00018-10.
    • (2010) MBio , vol.1
    • Steel, J.1    Lowen, A.C.2    Wang, T.T.3    Yondola, M.4    Gao, Q.5
  • 32
    • 34547776772 scopus 로고    scopus 로고
    • N-linked glycosylation attenuates H3N2 influenza viruses
    • Vigerust DJ, Ulett KB, Boyd KL, Madsen J, Hawgood S, et al. (2007) N-linked glycosylation attenuates H3N2 influenza viruses. J Virol 81: 8593-8600.
    • (2007) J Virol , vol.81 , pp. 8593-8600
    • Vigerust, D.J.1    Ulett, K.B.2    Boyd, K.L.3    Madsen, J.4    Hawgood, S.5
  • 33
    • 79251508720 scopus 로고    scopus 로고
    • Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin
    • Cherry JL, Lipman DJ, Nikolskaya A, Wolf YI, (2009) Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin. PLoS Curr 1: RRN1001.
    • (2009) PLoS Curr , vol.1
    • Cherry, J.L.1    Lipman, D.J.2    Nikolskaya, A.3    Wolf, Y.I.4
  • 34
    • 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
  • 35
    • 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
  • 36
  • 37
    • 33645069136 scopus 로고    scopus 로고
    • Virology. Clues to the virulence of H5N1 viruses in humans
    • Krug RM, (2006) Virology. Clues to the virulence of H5N1 viruses in humans. Science 311: 1562-1563.
    • (2006) Science , vol.311 , pp. 1562-1563
    • Krug, R.M.1
  • 39
    • 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 RG, Perez DR, (2001) Universal primer set for the full-length amplification of all influenza A viruses. Arch Virol 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
  • 40
    • 3342983070 scopus 로고    scopus 로고
    • WHO manual on animal influenza diagnosis and surveillance
    • World Health Organization, Available:. Accessed 13 October 2011
    • World Health Organization (2002) WHO manual on animal influenza diagnosis and surveillance. Available: http://www.who.int/csr/resources/publications/influenza/en/whocdscsrncs20025rev.pdf. Accessed 13 October 2011.
    • (2002)
  • 41
    • 0002958859 scopus 로고
    • General principle underlying laboratory diagnosis of viral infection
    • In: Lennette EH, Schmidt NJ, editors, Washington DC, American Health Association Inc
    • Hawkes RA, (1979) General principle underlying laboratory diagnosis of viral infection. In: Lennette EH, Schmidt NJ, editors. Diagnostic procedures for viral, rickettsial and chlamydial infection, 5th ed Washington DC American Health Association Inc pp. 32-41.
    • (1979) Diagnostic Procedures for Viral, Rickettsial and Chlamydial Infection, 5th Ed , pp. 32-41
    • Hawkes, R.A.1


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