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Part of the book series: Archives of Virology Supplementum ((ARCHIVES SUPPL,volume 1))

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Summary

Lysosomotropic agents, weak bases and ionophores, were used to study the mode of penetration of arenaviruses into cells. All drugs studied (ammonium chloride, chloroquine, amantadine, monensin) effectively inhibited replication of Pichinde, Mopeia, and Lassa viruses in BHK-21 and Vero cells. The experimental results indirectly indicate that endocytosis, using acid cellular endosomes, is a mode of entry of arenaviruses into cells. For prediction of arenavirus fusion protein we used an analysis of the elements of secondary and tertiary structure of precursor proteins of glycoproteins of five members of this virus family. Two regions of protein GP2 possessed properties that satisfied our criteria for selection of fusion peptides of enveloped viruses. One of the selected peptides was synthesized and model biophysical experiments demonstrated its ability to interact with lipid and to form single ion channels in the planar lipid bilayers, typical of fusion proteins of enveloped viruses. These data suggest that protein GP2 is the fusion protein of arenaviruses and that the fusion peptide is located in the immediate proximity to the N-end of this polypeptide.

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References

  1. Auperin DD, Romanovski V, Galinski M, Bishop DHL (1984) Sequence studies of Pichinde arenavirus S RNA indicate a novel coding strategy, an ambisense viral S RNA. J Virol 52: 897–904

    PubMed  CAS  Google Scholar 

  2. Auperin DD, Sasso DR, McCormick JB (1986) Nucleotide sequence of the glycoprotein gene and intergenic region of the Lassa virus S genome RNA. Virology 154: 155–167

    Article  PubMed  CAS  Google Scholar 

  3. Auperin DD, McCormick JB (1989) Nucleotide sequence of the Lassa virus ( Josiah strain) S genome RNA and amino acid sequence comparison of the N and GPC proteins to other arenaviruses. Virology 168: 421–425

    Google Scholar 

  4. Chou PY, Fasman GD (1978) Prediction of the secondary structure of proteins from their amino acid sequences. Adv Enzymol 47: 45–148

    PubMed  CAS  Google Scholar 

  5. Eband RM, Stertevant GM (1981) A calorimetric study of peptide—phospholipid interactions: the glucagon—dimyristoylphosphatidylcholine complex. Biochemistry 20: 4603–4606

    Article  Google Scholar 

  6. Franze-Fernandez MT, Zetina C, Japalucci S, Lucere MA, Bouisso C, Lopez R, Rey O, Daheli M, Cohen GN, Zakin MM (1987) Molecular structure and early events in the replication of Tacaribe arenavirus S RNA. Virus Res 7: 309–324

    Article  PubMed  CAS  Google Scholar 

  7. Gallaher WR (1987) Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell 50: 327–328

    Article  CAS  Google Scholar 

  8. Gamier J, Osquthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120: 97–120

    Article  Google Scholar 

  9. Glushakova SE, Lukashevich IS (1989) Early events in arenavirus replication are sensitive to lysosomotropic compounds. Arch Virol 104: 157–161

    Article  PubMed  CAS  Google Scholar 

  10. Hladky SB, Haydon DA (1972) Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel. Biochim Biophys Acta 274: 294–312

    Google Scholar 

  11. Jones DD (1975) Amino acid properties and side-chain orientation in proteins: a cross correlation approach. J Theor Biol 50: 167–183

    Article  PubMed  CAS  Google Scholar 

  12. Kempf G, Michel MR, Kohler U, Koblet H (1987) Can viral envelope proteins act as or induce proton channels? Biosci Rep 7: 761–769

    Article  PubMed  CAS  Google Scholar 

  13. Klein P, Kanehisa M, DeLisi C (1985) The detection and classification of membrane-spanning proteins. Biochim Biophys Acta 815: 468–476

    Article  PubMed  CAS  Google Scholar 

  14. Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105–132

    Article  PubMed  CAS  Google Scholar 

  15. Marsh M, Helenius A, Matlin K, Simons K (1983) Binding, endocytosis and degradation of enveloped animal viruses. Methods Enzymol 98: 260–266

    Article  PubMed  CAS  Google Scholar 

  16. Marsh M (1984) The entry of enveloped viruses into cells by endocytosis. Biochem J 218: 1–10

    PubMed  CAS  Google Scholar 

  17. Rao JKM, Argos P (1986) A conformational preference parameter to predict helices in integral membrane proteins. Biochim Biophys Acta 869: 197–214

    Article  CAS  Google Scholar 

  18. Romanowski V, Bishop DHL (1985) Conserved sequences and coding of two strains of lymphocytic choriomeningitis virus ( WE and ARM) and Pichinde arenavirus. Virus Res 2: 35–51

    Google Scholar 

  19. Romanowski V, Matsuura Y, Bishop DHL (1985) Complete sequence of the S RNA of lymphocytic choriomeningitis virus ( WE strain) compared to that of Pichinde arena-virus. Virus Res 3: 101–114

    Google Scholar 

  20. Rose GD, Roy S (1980) Hydrophobic basis of packing in globular proteins. Proc Natl Acad Sci USA 77: 4643–4647

    Article  PubMed  CAS  Google Scholar 

  21. Spear PG (1987) Virus-induced cell fusion. In: Sowers AE (ed) Cell fusion. Plenum, New York, pp 3–32

    Google Scholar 

  22. Terwilliger TC, Weissman L, Eisenberg D (1982) The structure of melittin in the form I crystals and its implication for melittin’s lytic and surface activities. Biophys J 37: 353–361

    Article  PubMed  CAS  Google Scholar 

  23. Welsh RM, Trowbridge RS, Kowalski JB, O’Connell CM, Pfau CJ (1971) Amantadine hydrochloride inhibition of early and late stages of lymphocytic choriomeningitis virus-cell interactions. Virology 45: 679–686

    Article  CAS  Google Scholar 

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© 1990 Springer-Verlag

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Glushakova, S.E., Lukashevich, I.S., Grinfeldt, A.E., Gotlib, V.A., Lev, A.A. (1990). Early events in infection with arenaviruses. In: Calisher, C.H. (eds) Hemorrhagic Fever with Renal Syndrome, Tick- and Mosquito-Borne Viruses. Archives of Virology Supplementum, vol 1. Springer, Vienna. https://doi.org/10.1007/978-3-7091-9091-3_14

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  • DOI: https://doi.org/10.1007/978-3-7091-9091-3_14

  • Publisher Name: Springer, Vienna

  • Print ISBN: 978-3-211-82217-3

  • Online ISBN: 978-3-7091-9091-3

  • eBook Packages: Springer Book Archive

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