메뉴 건너뛰기




Volumn 53, Issue 7, 1997, Pages 995-1003

Inhibition of influenza virus fusion by polyanionic proteins

Author keywords

antiviral agents; hemagglutinin; influenza virus; membrane fusion; polyanions; serum albumin

Indexed keywords

ANTIVIRUS AGENT; POLYANION; SERUM ALBUMIN;

EID: 0031009016     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(96)00876-3     Document Type: Article
Times cited : (30)

References (46)
  • 1
    • 0025914865 scopus 로고
    • Potent in vitro anti-human immunodeficiency virus-1 activity of modified human serum albumins
    • Jansen RW, Molema G, Pauwels R, Schols D, De Clercq E and Meijer DKF, Potent in vitro anti-human immunodeficiency virus-1 activity of modified human serum albumins. Mol Pharmacol 39: 818-823, 1991.
    • (1991) Mol Pharmacol , vol.39 , pp. 818-823
    • Jansen, R.W.1    Molema, G.2    Pauwels, R.3    Schols, D.4    De Clercq, E.5    Meijer, D.K.F.6
  • 2
    • 0027361964 scopus 로고
    • Novel, negatively charged, human serum albumins display potent and selective in vitro anti-human immunodeficiency virus type 1 activity
    • Jansen RW, Schols D, Pauwels R, De Clercq E and Meijer DKF, Novel, negatively charged, human serum albumins display potent and selective in vitro anti-human immunodeficiency virus type 1 activity. Mol Pharmacol 44: 1003-1007, 1993.
    • (1993) Mol Pharmacol , vol.44 , pp. 1003-1007
    • Jansen, R.W.1    Schols, D.2    Pauwels, R.3    De Clercq, E.4    Meijer, D.K.F.5
  • 3
    • 0028236956 scopus 로고
    • Negatively-charged albumins: A novel class of polyanionic proteins with a potent anti-HIV activity
    • Swart PJ and Meijer DKF, Negatively-charged albumins: A novel class of polyanionic proteins with a potent anti-HIV activity. Int Antivir News 2: 69-71, 1994.
    • (1994) Int Antivir News , vol.2 , pp. 69-71
    • Swart, P.J.1    Meijer, D.K.F.2
  • 4
    • 0029080953 scopus 로고
    • Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro
    • Harmsen MC, Swart PJ, de Béthune MP, Pauwels R, De Clercq E, The TH and Meijer DKF, Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J Infect Dis 172: 380-388, 1995.
    • (1995) J Infect Dis , vol.172 , pp. 380-388
    • Harmsen, M.C.1    Swart, P.J.2    De Béthune, M.P.3    Pauwels, R.4    De Clercq, E.5    The, T.H.6    Meijer, D.K.F.7
  • 6
    • 0029892820 scopus 로고    scopus 로고
    • Antiviral effects of milk proteins: Acylation results in polyanionic compounds with potent activity against human immunodeficiency virus type 1 and 2 in vitro
    • Swart PJ, Kuipers ME, Smit C, Pauwels R, de Béthune MP, De Clercq E, Meijer DKF and Huisman JG, Antiviral effects of milk proteins: Acylation results in polyanionic compounds with potent activity against human immunodeficiency virus type 1 and 2 in vitro. AIDS Res Hum Retroviruses 12: 769-775, 1996.
    • (1996) AIDS Res Hum Retroviruses , vol.12 , pp. 769-775
    • Swart, P.J.1    Kuipers, M.E.2    Smit, C.3    Pauwels, R.4    De Béthune, M.P.5    De Clercq, E.6    Meijer, D.K.F.7    Huisman, J.G.8
  • 7
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC and Skehel JJ, The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu Rev Biochem 56: 365-394, 1987.
    • (1987) Annu Rev Biochem , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 8
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White JM, Viral and cellular membrane fusion proteins. Annu Rev Physiol 52: 675-697, 1990.
    • (1990) Annu Rev Physiol , vol.52 , pp. 675-697
    • White, J.M.1
  • 10
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson IA, Skehel JJ and Wiley DC, Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289: 366-373, 1981.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 11
    • 0002466516 scopus 로고
    • The influenza virus hemagglutinin: Membrane fusion activity in intact virions and reconstituted virosomes
    • Ed. Bentz J. CRC Press, Boca Raton
    • Wilschut J and Bron R, The influenza virus hemagglutinin: Membrane fusion activity in intact virions and reconstituted virosomes. In: Viral Fusion Mechanisms (Ed. Bentz J), pp. 133-160. CRC Press, Boca Raton, 1993.
    • (1993) Viral Fusion Mechanisms , pp. 133-160
    • Wilschut, J.1    Bron, R.2
  • 12
    • 0028448430 scopus 로고
    • Membrane fusion: Anchors aweigh
    • Stegmann T, Membrane fusion: Anchors aweigh. Curr Biol 4: 551-554, 1994.
    • (1994) Curr Biol , vol.4 , pp. 551-554
    • Stegmann, T.1
  • 13
    • 0029257245 scopus 로고
    • Structural characterization of viral fusion proteins
    • Hughson FM, Structural characterization of viral fusion proteins. Curr Biol 5: 265-274, 1995.
    • (1995) Curr Biol , vol.5 , pp. 265-274
    • Hughson, F.M.1
  • 14
    • 0027434098 scopus 로고
    • Evaluation of viral membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay
    • Stegmann T, Schoen P, Bron R, Wey J, Bartoldus I, Ortiz A, Nieva JL and Wilschut J, Evaluation of viral membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay. Biochemistry 32: 11330-11337, 1993.
    • (1993) Biochemistry , vol.32 , pp. 11330-11337
    • Stegmann, T.1    Schoen, P.2    Bron, R.3    Wey, J.4    Bartoldus, I.5    Ortiz, A.6    Nieva, J.L.7    Wilschut, J.8
  • 15
    • 0021832341 scopus 로고
    • Kinetics of pH-dependent fusion between influenza virus and liposomes
    • Stegmann T, Hoekstra D, Scherphof G and Wilschut J, Kinetics of pH-dependent fusion between influenza virus and liposomes. Biochemistry 24: 3107-3113, 1985.
    • (1985) Biochemistry , vol.24 , pp. 3107-3113
    • Stegmann, T.1    Hoekstra, D.2    Scherphof, G.3    Wilschut, J.4
  • 16
    • 0027509351 scopus 로고
    • Membrane fusion of Semliki Forest virus in a model system: Correlation between fusion kinetics and structural changes in the envelope glycoprotein
    • Bron R, Wahlberg JM, Garoff H and Wilschut J, Membrane fusion of Semliki Forest virus in a model system: Correlation between fusion kinetics and structural changes in the envelope glycoprotein. EMBO J 12: 693-701, 1993.
    • (1993) EMBO J , vol.12 , pp. 693-701
    • Bron, R.1    Wahlberg, J.M.2    Garoff, H.3    Wilschut, J.4
  • 17
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames BN, Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol 8: 115-118, 1966.
    • (1966) Methods Enzymol , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 18
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG and Dyer WJ, A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-917, 1959.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 19
    • 50549164858 scopus 로고
    • A rapid and sensitive sub-micro phosphorus determination
    • Böttcher CJF, van Gent CM and Pries C, A rapid and sensitive sub-micro phosphorus determination. Anal Chim Acta 24: 203-204, 1961.
    • (1961) Anal Chim Acta , vol.24 , pp. 203-204
    • Böttcher, C.J.F.1    Van Gent, C.M.2    Pries, C.3
  • 21
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
    • Habeeb AFSA, Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal Biochem 14: 328-336, 1966.
    • (1966) Anal Biochem , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 22
    • 0025935290 scopus 로고
    • Formaldehyde treated albumin contains monomeric and polymeric forms that are differently cleared by endothelial and Kupffer cells of the liver: Evidence for scavenger receptor heterogeneity
    • Jansen RW, Molema G, Harms G, Kruijt JK, van Berkel TJC, Hardonk MJ and Meijer DKF, Formaldehyde treated albumin contains monomeric and polymeric forms that are differently cleared by endothelial and Kupffer cells of the liver: Evidence for scavenger receptor heterogeneity. Biochem Biophys Res Comm 180: 23-32, 1991.
    • (1991) Biochem Biophys Res Comm , vol.180 , pp. 23-32
    • Jansen, R.W.1    Molema, G.2    Harms, G.3    Kruijt, J.K.4    Van Berkel, T.J.C.5    Hardonk, M.J.6    Meijer, D.K.F.7
  • 23
    • 0025881866 scopus 로고
    • Hepatic endocytosis of various types of mannose-treated albumins. What is important, sugar recognition, net charge, or the combination of these features
    • Jansen RW, Molema G, Ching TL, Oosting R, Harms G, Moolenaar F, Hardonk MJ and Meijer DKF, Hepatic endocytosis of various types of mannose-treated albumins. What is important, sugar recognition, net charge, or the combination of these features. J Biol Chem 266: 3343-3348, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 3343-3348
    • Jansen, R.W.1    Molema, G.2    Ching, T.L.3    Oosting, R.4    Harms, G.5    Moolenaar, F.6    Hardonk, M.J.7    Meijer, D.K.F.8
  • 25
    • 0027317501 scopus 로고
    • Preparation, properties and applications of reconstituted influenza virus envelopes
    • Bron R, Ortiz A, Dijkstra J, Stegmann T and Wilschut J, Preparation, properties and applications of reconstituted influenza virus envelopes (virosomes). Methods Enzymol 220: 313-331, 1993.
    • (1993) Methods Enzymol , vol.220 , pp. 313-331
    • Bron, R.1    Ortiz, A.2    Dijkstra, J.3    Stegmann, T.4    Wilschut, J.5
  • 26
    • 0016360444 scopus 로고
    • Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes
    • Steck TL and Kant JA, Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes. Methods Enzymol 31: 172-180, 1974.
    • (1974) Methods Enzymol , vol.31 , pp. 172-180
    • Steck, T.L.1    Kant, J.A.2
  • 27
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope MJ, Bally MB, Webb G and Cullis PR, Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim Biophys Acta 812: 55-65, 1985.
    • (1985) Biochim Biophys Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 28
    • 0027163749 scopus 로고
    • Fluorescence dequenching kinetics of single cell-cell fusion complexes
    • Chen Y, Rubin RJ and Szabo A, Fluorescence dequenching kinetics of single cell-cell fusion complexes. Biophys J 65: 325-333, 1993.
    • (1993) Biophys J , vol.65 , pp. 325-333
    • Chen, Y.1    Rubin, R.J.2    Szabo, A.3
  • 29
    • 0022977607 scopus 로고
    • Fusion activity of influenza virus. A comparison between biological and artificial target membrane vesicles
    • Stegmann T, Hoekstra D, Scherphof G and Wilschut J, Fusion activity of influenza virus. A comparison between biological and artificial target membrane vesicles. J Biol Chem 261: 10966-10969, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 10966-10969
    • Stegmann, T.1    Hoekstra, D.2    Scherphof, G.3    Wilschut, J.4
  • 30
    • 0029201982 scopus 로고
    • Fusion of Semliki Forest virus with cholesterol-containing liposomes at low pH: A specific requirement for spingolipids
    • Wilschut J, Corver J, Nieva JL, Bron R, Moesby L, Reddy CK and Bittman R, Fusion of Semliki Forest virus with cholesterol-containing liposomes at low pH: A specific requirement for spingolipids. Mol Membr Biol 12: 143-149, 1995.
    • (1995) Mol Membr Biol , vol.12 , pp. 143-149
    • Wilschut, J.1    Corver, J.2    Nieva, J.L.3    Bron, R.4    Moesby, L.5    Reddy, C.K.6    Bittman, R.7
  • 31
    • 0025647464 scopus 로고
    • Intermediates in influenza induced membrane fusion
    • Stegmann T, White JM and Helenius A, Intermediates in influenza induced membrane fusion. EMBO J 9: 4231-4241, 1990.
    • (1990) EMBO J , vol.9 , pp. 4231-4241
    • Stegmann, T.1    White, J.M.2    Helenius, A.3
  • 32
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • Stegmann T, Delfino JM, Richards FM and Helenius A, The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J Biol Chem 266: 18404-18410, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 33
    • 0025363004 scopus 로고
    • Dextran sulfate inhibits the fusion of influenza virus with model membranes, and suppresses influenza virus replication in vivo
    • Lüscher-Mattli M and Glück R, Dextran sulfate inhibits the fusion of influenza virus with model membranes, and suppresses influenza virus replication in vivo. Antiviral Res 14: 39-50, 1990.
    • (1990) Antiviral Res , vol.14 , pp. 39-50
    • Lüscher-Mattli, M.1    Glück, R.2
  • 34
    • 0026784334 scopus 로고
    • Dextran sulfate inhibits fusion of influenza virus and cells expressing influenza hemagglutinin with red blood cells
    • Krumbiegel M, Dimitrov DS, Puri A and Blumenthal R, Dextran sulfate inhibits fusion of influenza virus and cells expressing influenza hemagglutinin with red blood cells. Biochim Biophys Acta 1110: 158-164, 1992.
    • (1992) Biochim Biophys Acta , vol.1110 , pp. 158-164
    • Krumbiegel, M.1    Dimitrov, D.S.2    Puri, A.3    Blumenthal, R.4
  • 35
    • 0026699012 scopus 로고
    • The influence of dextran sulfate on influenza A virus fusion with erythrocyte membranes
    • Herrmann A, Korte T, Arnold K and Hillebrecht B, The influence of dextran sulfate on influenza A virus fusion with erythrocyte membranes. Antiviral Res 19: 295-311, 1992.
    • (1992) Antiviral Res , vol.19 , pp. 295-311
    • Herrmann, A.1    Korte, T.2    Arnold, K.3    Hillebrecht, B.4
  • 36
    • 0027352217 scopus 로고
    • A comparative study of the effect of dextran sulfate on the fusion and the in vitro replication of influenza A and B, Semliki Forest, vesicular stomatitis, rabies, Sendai, and mumps virus
    • Lüscher-Mattli M, Glück R, Kempf C and Zanoni-Grassi M, A comparative study of the effect of dextran sulfate on the fusion and the in vitro replication of influenza A and B, Semliki Forest, vesicular stomatitis, rabies, Sendai, and mumps virus. Arch Virol 130: 317-326, 1993.
    • (1993) Arch Virol , vol.130 , pp. 317-326
    • Lüscher-Mattli, M.1    Glück, R.2    Kempf, C.3    Zanoni-Grassi, M.4
  • 37
    • 0000941268 scopus 로고
    • Entry of animal viruses into cells
    • Marsh M and Pelchen-Matthews A, Entry of animal viruses into cells. Rev Med Virol 3: 173-185, 1993.
    • (1993) Rev Med Virol , vol.3 , pp. 173-185
    • Marsh, M.1    Pelchen-Matthews, A.2
  • 38
    • 0029556891 scopus 로고
    • Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin
    • Pass D and Kim PS, Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr Biol 5: 1377-1383, 1995.
    • (1995) Curr Biol , vol.5 , pp. 1377-1383
    • Pass, D.1    Kim, P.S.2
  • 39
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • Rabenstein M and Shin YK, A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation. Biochemistry 34: 13390-13397, 1995.
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.K.2
  • 41
    • 0026492542 scopus 로고
    • Membrane fusion
    • White JM, Membrane fusion. Science 258: 917-924, 1992.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 42
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection
    • Freed EO and Martin MA, The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection. J Bio! Chem 270: 23883-23886, 1995.
    • (1995) J Bio! Chem , vol.270 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 43
    • 0019300295 scopus 로고
    • Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins
    • Garoff H, Frischauf AM, Simons K, Lehrach H and Delius H, Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins. Nature 288: 236-241, 1980.
    • (1980) Nature , vol.288 , pp. 236-241
    • Garoff, H.1    Frischauf, A.M.2    Simons, K.3    Lehrach, H.4    Delius, H.5
  • 44
    • 0029108852 scopus 로고
    • Membrane fusion and the alphavirus life cycle
    • Kielian M, Membrane fusion and the alphavirus life cycle. Adv Virus Res 45: 113-151, 1995.
    • (1995) Adv Virus Res , vol.45 , pp. 113-151
    • Kielian, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.