메뉴 건너뛰기




Volumn 90, Issue 11, 2009, Pages 2751-2758

Influenza A virus M1 blocks the classical complement pathway through interacting with C1qA

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1QA; IMMUNOGLOBULIN G; MATRIX PROTEIN; UNCLASSIFIED DRUG; COMPLEMENT COMPONENT C1; M1 PROTEIN, INFLUENZA A VIRUS;

EID: 70350459876     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.014316-0     Document Type: Article
Times cited : (41)

References (44)
  • 1
    • 0141737104 scopus 로고    scopus 로고
    • Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)
    • Akarsu, H., Burmeister, W. P., Petosa, C., Petit, I., Muller, C. W., Ruigrok, R. W. & Baudin, F. (2003). Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J 22, 4646-4655.
    • (2003) EMBO J , vol.22 , pp. 4646-4655
    • Akarsu, H.1    Burmeister, W.P.2    Petosa, C.3    Petit, I.4    Muller, C.W.5    Ruigrok, R.W.6    Baudin, F.7
  • 2
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali, A., Avalos, R. T., Ponimaskin, E. & Nayak, D. P. (2000). Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein. J Virol 74, 8709-8719.
    • (2000) J Virol , vol.74 , pp. 8709-8719
    • Ali, A.1    Avalos, R.T.2    Ponimaskin, E.3    Nayak, D.P.4
  • 3
    • 0035864293 scopus 로고    scopus 로고
    • Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer
    • Arzt, S., Baudin, F., Barge, A., Timmins, P., Burmeister, W. P. & Ruigrok, R. W. (2001). Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer. Virology 279, 439-446.
    • (2001) Virology , vol.279 , pp. 439-446
    • Arzt, S.1    Baudin, F.2    Barge, A.3    Timmins, P.4    Burmeister, W.P.5    Ruigrok, R.W.6
  • 4
    • 0030966390 scopus 로고    scopus 로고
    • Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells
    • Avalos, R. T., Yu, Z. & Nayak, D. P. (1997). Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells. J Virol 71, 2947-2958.
    • (1997) J Virol , vol.71 , pp. 2947-2958
    • Avalos, R.T.1    Yu, Z.2    Nayak, D.P.3
  • 5
    • 0034939645 scopus 로고    scopus 로고
    • Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses
    • Barman, S., Ali, A., Hui, E. K., Adhikary, L. & Nayak, D. P. (2001). Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses. Virus Res 77, 61-69.
    • (2001) Virus Res , vol.77 , pp. 61-69
    • Barman, S.1    Ali, A.2    Hui, E.K.3    Adhikary, L.4    Nayak, D.P.5
  • 6
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin, F., Petit, I., Weissenhorn, W. & Ruigrok, R. W. (2001). In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 281, 102-108.
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 7
    • 0020680927 scopus 로고
    • Neutralization of influenza virus by normal human sera: Mechanisms involving antibody and complement
    • Beebe, D. P., Schreiber, R. D. & Cooper, N. R. (1983). Neutralization of influenza virus by normal human sera: mechanisms involving antibody and complement. J Immunol 130, 1317-1322.
    • (1983) J Immunol , vol.130 , pp. 1317-1322
    • Beebe, D.P.1    Schreiber, R.D.2    Cooper, N.R.3
  • 8
    • 37849026708 scopus 로고    scopus 로고
    • Human astrovirus coat protein inhibits serum complement activation via C1, the first component of the classical pathway
    • Bonapàrte, R. S., Hair, P. S., Banthia, D., Marshall, D. M., Cunnion, K. M. & Krishna, N. K. (2008). Human astrovirus coat protein inhibits serum complement activation via C1, the first component of the classical pathway. J Virol 82, 817-827.
    • (2008) J Virol , vol.82 , pp. 817-827
    • Bonapàrte, R.S.1    Hair, P.S.2    Banthia, D.3    Marshall, D.M.4    Cunnion, K.M.5    Krishna, N.K.6
  • 9
    • 19944393903 scopus 로고    scopus 로고
    • The morphology and composition of influenza A virus particles are not affected by low levels of M1 and M2 proteins in infected cells
    • Bourmakina, S. V. & García-Sastre, A. (2005). The morphology and composition of influenza A virus particles are not affected by low levels of M1 and M2 proteins in infected cells. J Virol 79, 7926-7932.
    • (2005) J Virol , vol.79 , pp. 7926-7932
    • Bourmakina, S.V.1    García-Sastre, A.2
  • 10
    • 0017730206 scopus 로고
    • Immunologic recognition of influenza virus-infected cells. II. Expression of influenza A matrix protein on the infected cell surface and its role in recognition by cross-reactive cytotoxic T cells
    • Braciale, T. J. (1977). Immunologic recognition of influenza virus-infected cells. II. Expression of influenza A matrix protein on the infected cell surface and its role in recognition by cross-reactive cytotoxic T cells. J Exp Med 146, 673-689.
    • (1977) J Exp Med , vol.146 , pp. 673-689
    • Braciale, T.J.1
  • 11
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui, M., Whittaker, G. & Helenius, A. (1996). Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J Virol 70, 8391-8401.
    • (1996) J Virol , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 12
    • 11144244386 scopus 로고    scopus 로고
    • Influenza A viruses with mutations in the M1 helix six domain display a wide variety of morphological phenotypes
    • Burleigh, L. M., Calder, L. J., Skehel, J. J. & Steinhauer, D. A. (2005). Influenza A viruses with mutations in the M1 helix six domain display a wide variety of morphological phenotypes. J Virol 79, 1262-1270.
    • (2005) J Virol , vol.79 , pp. 1262-1270
    • Burleigh, L.M.1    Calder, L.J.2    Skehel, J.J.3    Steinhauer, D.A.4
  • 13
    • 0030749976 scopus 로고    scopus 로고
    • Influenza virus M1 protein binds to RNA through its nuclear localization signal
    • Elster, C., Larsen, K., Gagnon, J., Ruigrok, R. W. & Baudin, F. (1997). Influenza virus M1 protein binds to RNA through its nuclear localization signal. J Gen Virol 78, 1589-1596.
    • (1997) J Gen Virol , vol.78 , pp. 1589-1596
    • Elster, C.1    Larsen, K.2    Gagnon, J.3    Ruigrok, R.W.4    Baudin, F.5
  • 15
    • 0024452262 scopus 로고
    • A novel function of the herpes simplex virus type 1 Fc receptor: Participation in bipolar bridging of antiviral immunoglobulin G
    • Frank, I. & Friedman, H. M. (1989). A novel function of the herpes simplex virus type 1 Fc receptor: participation in bipolar bridging of antiviral immunoglobulin G. J Virol 63, 4479-4488.
    • (1989) J Virol , vol.63 , pp. 4479-4488
    • Frank, I.1    Friedman, H.M.2
  • 16
    • 0021246307 scopus 로고
    • Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells
    • Friedman, H. M., Cohen, G. H., Eisenberg, R. J., Seidel, C. A. & Cines, D. B. (1984). Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells. Nature 309, 633-635.
    • (1984) Nature , vol.309 , pp. 633-635
    • Friedman, H.M.1    Cohen, G.H.2    Eisenberg, R.J.3    Seidel, C.A.4    Cines, D.B.5
  • 18
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1
    • Harris, A., Forouhar, F., Qiu, S., Sha, B. & Luo, M. (2001). The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 289, 34-44.
    • (2001) Virology , vol.289 , pp. 34-44
    • Harris, A.1    Forouhar, F.2    Qiu, S.3    Sha, B.4    Luo, M.5
  • 19
    • 0031777155 scopus 로고    scopus 로고
    • Molecular mimicry of the inflammation modulatory proteins (IMPs) of poxviruses: Evasion of the inflammatory response to preserve viral habitat
    • Howard, J., Justus, D. E., Totmenin, A. V., Shchelkunov, S. & Kotwal, G. J. (1998). Molecular mimicry of the inflammation modulatory proteins (IMPs) of poxviruses: evasion of the inflammatory response to preserve viral habitat. J Leukoc Biol 64, 68-71.
    • (1998) J Leukoc Biol , vol.64 , pp. 68-71
    • Howard, J.1    Justus, D.E.2    Totmenin, A.V.3    Shchelkunov, S.4    Kotwal, G.J.5
  • 20
    • 0035450255 scopus 로고    scopus 로고
    • Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export
    • Huang, X., Liu, T., Muller, J., Levandowski, R. A. & Ye, Z. (2001). Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology 287, 405-416.
    • (2001) Virology , vol.287 , pp. 405-416
    • Huang, X.1    Liu, T.2    Muller, J.3    Levandowski, R.A.4    Ye, Z.5
  • 21
    • 0026752584 scopus 로고
    • Structural basis of C3b binding by glycoprotein C of herpes simplex virus
    • Hung, S. L., Srinivasan, S., Friedman, H. M., Eisenberg, R. J. & Cohen, G. H. (1992). Structural basis of C3b binding by glycoprotein C of herpes simplex virus. J Virol 66, 4013-4027.
    • (1992) J Virol , vol.66 , pp. 4013-4027
    • Hung, S.L.1    Srinivasan, S.2    Friedman, H.M.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 22
    • 0028100351 scopus 로고
    • The interaction of glycoprotein C of herpes simplex virus types 1 and 2 with the alternative complement pathway
    • Hung, S. L., Peng, C., Kostavasili, I., Friedman, H. M., Lambris, J. D., Eisenberg, R. J. & Cohen, G. H. (1994). The interaction of glycoprotein C of herpes simplex virus types 1 and 2 with the alternative complement pathway. Virology 203, 299-312.
    • (1994) Virology , vol.203 , pp. 299-312
    • Hung, S.L.1    Peng, C.2    Kostavasili, I.3    Friedman, H.M.4    Lambris, J.D.5    Eisenberg, R.J.6    Cohen, G.H.7
  • 23
    • 33947434002 scopus 로고    scopus 로고
    • Natural antibody and complement mediate neutralization of influenza virus in the absence of prior immunity
    • Jayasekera, J. P., Moseman, E. A. & Carroll, M. C. (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
  • 24
    • 0028787383 scopus 로고
    • Collagen-like complement component C1q is a membrane protein of human monocyte-derived macrophages that mediates endocytosis
    • Kaul, M. & Loos, M. (1995). Collagen-like complement component C1q is a membrane protein of human monocyte-derived macrophages that mediates endocytosis. J Immunol 155, 5795-5802.
    • (1995) J Immunol , vol.155 , pp. 5795-5802
    • Kaul, M.1    Loos, M.2
  • 25
    • 0033947551 scopus 로고    scopus 로고
    • C1q: Structure, function, and receptors
    • Kishore, U. & Reid, K. B. (2000). C1q: structure, function, and receptors. Immunopharmacology 49, 159-170.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.2
  • 26
    • 0021176012 scopus 로고
    • Identification and characterization of a monoclonal antibody to an antigen expressed on activated macrophages
    • Koestler, T. P., Rieman, D., Muirhead, K., Greig, R. G. & Poste, G. (1984). Identification and characterization of a monoclonal antibody to an antigen expressed on activated macrophages. Proc Natl Acad Sci U S A 81, 4505-4509.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 4505-4509
    • Koestler, T.P.1    Rieman, D.2    Muirhead, K.3    Greig, R.G.4    Poste, G.5
  • 27
    • 0031702845 scopus 로고    scopus 로고
    • The inflammation modulatory protein (IMP) of cowpox virus drastically diminishes the tissue damage by down-regulating cellular infiltration resulting from complement activation
    • Kotwal, G. J., Miller, C. G. & Justus, D. E. (1998). The inflammation modulatory protein (IMP) of cowpox virus drastically diminishes the tissue damage by down-regulating cellular infiltration resulting from complement activation. Mol Cell Biochem 185, 39-46.
    • (1998) Mol Cell Biochem , vol.185 , pp. 39-46
    • Kotwal, G.J.1    Miller, C.G.2    Justus, D.E.3
  • 28
    • 64049094864 scopus 로고    scopus 로고
    • Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication
    • Liu, X., Sun, L., Yu, M., Wang, Z., Xu, C., Xue, Q., Zhang, K., Ye, X., Kitamura, Y. & Liu, W. (2009). Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication. Cell Microbiol 11, 730-741.
    • (2009) Cell Microbiol , vol.11 , pp. 730-741
    • Liu, X.1    Sun, L.2    Yu, M.3    Wang, Z.4    Xu, C.5    Xue, Q.6    Zhang, K.7    Ye, X.8    Kitamura, Y.9    Liu, W.10
  • 29
    • 33747036652 scopus 로고    scopus 로고
    • Enhancement of neutralizing activity of influenza virus-specific antibodies by serum components
    • Mozdzanowska, K., Feng, J., Eid, M., Zharikova, D. & Gerhard, W. (2006). Enhancement of neutralizing activity of influenza virus-specific antibodies by serum components. Virology 352, 418-426.
    • (2006) Virology , vol.352 , pp. 418-426
    • Mozdzanowska, K.1    Feng, J.2    Eid, M.3    Zharikova, D.4    Gerhard, W.5
  • 30
    • 47649116956 scopus 로고    scopus 로고
    • Host factors for replication and transcription of the influenza virus genome
    • Nagata, K., Kawaguchi, A. & Naito, T. (2008). Host factors for replication and transcription of the influenza virus genome. Rev Med Virol 18, 247-260.
    • (2008) Rev Med Virol , vol.18 , pp. 247-260
    • Nagata, K.1    Kawaguchi, A.2    Naito, T.3
  • 31
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • Nayak, D. P., Hui, E. K. & Barman, S. (2004). Assembly and budding of influenza virus. Virus Res 106, 147-165.
    • (2004) Virus Res , vol.106 , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.2    Barman, S.3
  • 34
    • 0035090589 scopus 로고    scopus 로고
    • Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade
    • Pleschka, S., Wolff, T., Ehrhardt, C., Hobom, G., Planz, O., Rapp, U. R. & Ludwig, S. (2001). Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade. Nat Cell Biol 3, 301-305.
    • (2001) Nat Cell Biol , vol.3 , pp. 301-305
    • Pleschka, S.1    Wolff, T.2    Ehrhardt, C.3    Hobom, G.4    Planz, O.5    Rapp, U.R.6    Ludwig, S.7
  • 35
    • 0034702018 scopus 로고    scopus 로고
    • The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C
    • Reinhardt, J. & Wolff, T. (2000). The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. Vet Microbiol 74, 87-100.
    • (2000) Vet Microbiol , vol.74 , pp. 87-100
    • Reinhardt, J.1    Wolff, T.2
  • 36
    • 0018952322 scopus 로고
    • Influenza type A virus M protein expression on infected cells is responsible for cross-reactive recognition by cytotoxic thymus-derived lymphocytes
    • Reiss, C. S. & Schulman, J. L. (1980). Influenza type A virus M protein expression on infected cells is responsible for cross-reactive recognition by cytotoxic thymus-derived lymphocytes. Infect Immun 29, 719-723.
    • (1980) Infect Immun , vol.29 , pp. 719-723
    • Reiss, C.S.1    Schulman, J.L.2
  • 38
    • 0028009775 scopus 로고
    • Inhibition of complement-mediated cytolysis by the terminal complement inhibitor of herpesvirus saimiri
    • Rother, R. P., Rollins, S. A., Fodor, W. L., Albrecht, J. C., Setter, E., Fleckenstein, B. & Squinto, S. P. (1994). Inhibition of complement-mediated cytolysis by the terminal complement inhibitor of herpesvirus saimiri. J Virol 68, 730-737.
    • (1994) J Virol , vol.68 , pp. 730-737
    • Rother, R.P.1    Rollins, S.A.2    Fodor, W.L.3    Albrecht, J.C.4    Setter, E.5    Fleckenstein, B.6    Squinto, S.P.7
  • 39
    • 0031039724 scopus 로고    scopus 로고
    • Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1
    • Sha, B. & Luo, M. (1997). Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1. Nat Struct Biol 4, 239-244.
    • (1997) Nat Struct Biol , vol.4 , pp. 239-244
    • Sha, B.1    Luo, M.2
  • 40
    • 0024454843 scopus 로고
    • RNA-binding properties of influenza A virus matrix protein M1
    • Wakefield, L. & Brownlee, G. G. (1989). RNA-binding properties of influenza A virus matrix protein M1. Nucleic Acids Res 17, 8569-8580.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8569-8580
    • Wakefield, L.1    Brownlee, G.G.2
  • 41
    • 0029656043 scopus 로고    scopus 로고
    • Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein
    • Watanabe, K., Handa, H., Mizumoto, K. & Nagata, K. (1996). Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein. J Virol 70, 241-247.
    • (1996) J Virol , vol.70 , pp. 241-247
    • Watanabe, K.1    Handa, H.2    Mizumoto, K.3    Nagata, K.4
  • 42
    • 33749338927 scopus 로고    scopus 로고
    • Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle
    • Watanabe, K., Fuse, T., Asano, I., Tsukahara, F., Maru, Y., Nagata, K., Kitazato, K. & Kobayashi, N. (2006). Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle. FEBS Lett 580, 5785-5790.
    • (2006) FEBS Lett , vol.580 , pp. 5785-5790
    • Watanabe, K.1    Fuse, T.2    Asano, I.3    Tsukahara, F.4    Maru, Y.5    Nagata, K.6    Kitazato, K.7    Kobayashi, N.8
  • 43
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye, Z., Liu, T., Offringa, D. P., McInnis, J. & Levandowski, R. A. (1999). Association of influenza virus matrix protein with ribonucleoproteins. J Virol 73, 7467-7473.
    • (1999) J Virol , vol.73 , pp. 7467-7473
    • Ye, Z.1    Liu, T.2    Offringa, D.P.3    McInnis, J.4    Levandowski, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.