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Viral Structure and Composition

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Abstract

The influenza viruses comprise three types of viruses that are closely related in structure, chemical composition, and biological activity. These viruses, types A, B, and C, are pleomorphic enveloped viruses bearing surface projections (peplomers or spikes). Influenza A and B viruses contain four major structural proteins and three proteins with RNA replicase and transcriptase activity (Table 3–1). Eight segments of linear, single-stranded RNA are contained in separate nucleocapsids—rodlike structures of nucleoprotein (NP) (Heggeness et al., 1982)— with which the replicase and transcriptase proteins PB1, PB2, and PA are in close association in an RNP complex. The interior of the virus particle is delimited by repeating units of the matrix or membrane (M) protein in all three viral subtypes. The external spikes of influenza A and B viruses number 400 to 500 (Ruigrok et al., 1984) and comprise two different glycoproteins, the hemagglutinin (HA) and neuraminidase (NA). In the case of influenza C virus, only seven RNA segments and a single external glycoprotein have been demonstrated.

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References

  • Air, G. M., and Compans, R. W., 1983, Influenza B and influenza C viruses, in: Genetics of Influenza Viruses (P. Palese and D. W. Kingsbury, eds.), Springer-Verlag, New York, pp. 280–304.

    Google Scholar 

  • Allen, A. K., Skehel, J. J., and Yuferov, V., 1977, The amino acid and carbohydrate composition of the neuraminidase of B/Lee/40 influenza virus, J. Gen. Virol 37:625–628.

    CAS  Google Scholar 

  • Apostolov, K., and Flewett, T. H., 1969, Further observations on the structure of influenza viruses A and C, J. Gen. Virol. 4:365–370.

    PubMed  CAS  Google Scholar 

  • Blok, J., Air, G. M., Laver, W. G., et al., 1982, Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane, Virology 119:109–121.

    PubMed  CAS  Google Scholar 

  • Blough, H. A., 1963, The effect of vitamin A alcohol on the morphology of myxoviruses. I. The production and comparison of artificially produced filamentous virus, Virology 19:349–358.

    PubMed  CAS  Google Scholar 

  • Blough, H. A., and Lawson, D. E. M., 1968, The lipids of paramyxoviruses: A comparative study of Sendai and Newcastle disease viruses, Virology 36:286–292.

    PubMed  CAS  Google Scholar 

  • Brown, L. E., Ward, C. W., and Jackson, D. C., 1982, Antigenic determinants of influenza virus hemagglutinin-IX. The carbohydrate side chains from an Asian strain, Mol. Immunol. 19:329–338.

    PubMed  CAS  Google Scholar 

  • Bucher, D. L., and Kilbourne, E. D., 1972, A (N2) neuraminidase of the X-7 influenza virus recombinant: Determination of molecular size and subunit composition of the active unit, J.. Virol. 10:60–66.

    PubMed  CAS  Google Scholar 

  • Caton, A. J., Brownlee, G. G., Yewdell, J. W., et al., 1982, The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (HI subtype), Cell 31:417–427.

    PubMed  CAS  Google Scholar 

  • Choppin, P. W., and Compans, R. W., 1975, The structure of influenza virus, in: The Influenza Virus and Influenza (E. D. Kilbourne, ed.), Academic Press, New York, pp. 15–47.

    Google Scholar 

  • Choppin, P. W., Murphy, J. S., and Tamm, I., 1960, Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: Independence of morphological and functional traits,J.. Exp. Med. 112:945–952.

    PubMed  CAS  Google Scholar 

  • Choppin, P. W., Murphy, J. S., and Stoeckenius, W., 1961, Surface structure of influenza virus filaments, Virology 13:548–550.

    PubMed  CAS  Google Scholar 

  • Clerx, J. P. M., Fuller, F., and Bishop, D. H. L., 1983, Tick-borne viruses structurally similar to orthomyxoviruses, Virology 127:205–219.

    PubMed  CAS  Google Scholar 

  • Colman, P. M., and Ward, C. W., 1985, Structure and diversity of the influenza virus neuraminidase, Curr. Top. Microbiol. Immunol. 114:177–225.

    PubMed  CAS  Google Scholar 

  • Colman, P. M., Varghese, J. N., and Laver, W. G., 1983, Structure of the catalytic and antigenic sites in influenza virus neuraminidase, Nature 303:41–44.

    PubMed  CAS  Google Scholar 

  • Compans, R. W., Dimmock, N. J., and Meier-Ewert, H., 1969, Effect of antibody to neuraminidase on the maturation and hemagglutinating activity of an influenza A virus, J.. Virol. 4:528–534.

    PubMed  CAS  Google Scholar 

  • Compans, R. W., Content, J., and Duesberg, P. H., 1972, Structure of the ribonucleoprotein of influenza virus, J. Virol. 10:795–800.

    PubMed  CAS  Google Scholar 

  • Cusack, S., Ruigrok, R. W. H., Krygsman, P. C. J., et al, 1985, Structure and composition of influenza virus. A small-angle neutron scattering study, J.. Mol. Biol. 186:565–582.

    PubMed  CAS  Google Scholar 

  • Desselberger, U., Racaniello, V. R., Zazra, J. J., et al., 1980, The 3 and 5-terminal sequences of influenza A, B and C virus RNA segments are highly conserved and show partial inverted complementarity, Gene 8:315–328.

    PubMed  CAS  Google Scholar 

  • Erickson, A. H., 1977, Different trypsin sensitivity of the hemagglutinin from antigenically similar recombinant influenza viruses ,doctoral dissertation. Department of Microbiology, Mount Sinai School of Medicine, Graduate School of Biological Sciences, The City University of New York, New York.

    Google Scholar 

  • Erickson, A. H., and Kilbourne, E. D., 1980, Mutation in the hemagglutinin of A/N-WS/33 influenza virus recombinants influencing sensitivity to trypsin and antigenic reactivity, Virology 107:320–330.

    PubMed  CAS  Google Scholar 

  • Fazekas de St. Groth, S., 1963, Steric inhibition: Neutralization of a virus-borne enzyme, Ann. N.Y. Acad. Sci. 103:674–687.

    Google Scholar 

  • Fields, S., Winter, G., and Brownlee, G. G., 1981, Structure of the neuraminidase gene from human influenza virus A/PR/8/34, Nature 290:213–217.

    PubMed  CAS  Google Scholar 

  • Groome, N. P., Belyavin, G., Landsdell, A., et al., 1977, Structure and composition of the N2 neuraminidase of influenza virus. Effect of carbohydrate content on the validity of molecular weight estimations, Biochim. Biophys. Acta 495:58–70.

    PubMed  CAS  Google Scholar 

  • Heggeness, M. H., Smith, P. R., Ulmanen, I., et al., 1982, Studies on the helical nucleocapsid of influenza virus, Virology 118:466–470.

    PubMed  CAS  Google Scholar 

  • Herrler, G., Nagele, A., Meier-Ewert, H., et al., 1981, Isolation and structural analysis of influenza C virion glycoproteins, Virology 113:439–451.

    PubMed  CAS  Google Scholar 

  • Herrler, G., Rott, R.,Klenk, H-D., et al., 1985, The receptor-destroying, enzyme of influenza C virus is neuraminate-O-acetylesterase. EM BO Journal 4:1503–1506.

    CAS  Google Scholar 

  • Huang, R. T. C., 1976, Sphingolipids of influenza viruses, Biochim. Biophys. Acta 424:90–97.

    PubMed  CAS  Google Scholar 

  • Huang, R. T. C., Wahn, K., Klenk, H.-D., et al., 1980, Fusion between cell membranes and liposomes containing the glycoprotein of influenza virus, Virology 104:294–302.

    PubMed  CAS  Google Scholar 

  • Jackson, D. C., Brown, L. E., and White, D. O., 1981, Antigenic determinants of influenza virus hemagglutinin. VI. Antigenic characterization of the oligosaccharide sidechains from HA of influenza virus hemagglutinins, J.. Gen. Virol 52:163–168.

    PubMed  CAS  Google Scholar 

  • Jennings, P. A., Finch, J. T., Winter, G., et al., 1983, Does the higher order structure of the influenza virus ribonucleoprotein guide sequence rearrangements in influenza viral RNA? Cell 34:619–627.

    PubMed  CAS  Google Scholar 

  • Karadaghi, S. E., Zakomirdin, J. A., Shimane, C., et al., 1984, Interaction of influenza virus proteins with planar bilayer lipid membranes. I. Characterization of their adsorption and incorporation into lipid bilayers, Biochim. Biophys. Acta 778:269–275.

    PubMed  Google Scholar 

  • Kates, M., Allison, A. C., Tyrrell, D. A. J., et al., 1961, Lipids of influenza virus and their relation to those of the host cell, Biochim. Biophys. Acta 52:455–466.

    CAS  Google Scholar 

  • Kawakami, K., Ishihama, A., and Hamaguchi, M., 1981, RNA polymerase of influenza virus. I. Comparison of the virion-associated RNA polymerase activity of various strains of influenza virus, J.. Biochem. 89:1751–1757.

    PubMed  CAS  Google Scholar 

  • Keil, W., Klenk, H.-D., and Schwarz, R. T., 1979, Carbohydrates of influenza virus. III. Nature of oligosaccharide-protein linkage in viral glycoproteins,J.. Virol. 31:253–256.

    PubMed  CAS  Google Scholar 

  • Keil, W., Geyer, R., Niemann, H., et al., 1984a, The carbohydrates of the hemagglutinin of influenza virus, in: Segmented Negative Strand Viruses (R. Compans and D. Bishop, eds.), Academic Press, New York, pp. 289–298.

    Google Scholar 

  • Keil, W., Niemann, H., Schwarz, R. T., et al., 1984b, Carbohydrates of influenza virus. V. Oligosaccharides attached to individual glycosylation sites of the hemagglutinin of fowl plague virus, Virology 133:77–91.

    PubMed  CAS  Google Scholar 

  • Kendal, A. P., and Eckert, E., 1972, The preparation and properties of 14C-carboxamidomethylated subunits from A/1957 influenza neuraminidase, Biochim. Biophys. Acta 258:484–495.

    PubMed  CAS  Google Scholar 

  • Kendal, A. P., and Madeley, C. R., 1970, Flocculation of influenza virus by specific antineuramini dase antibody, Arch. Ges. Virusforsch. 31:219–229.

    PubMed  CAS  Google Scholar 

  • Kharitonenkov, I. G., Siniakov, M. S., Grigoriev, V. B., et al., 1978, The length of the influenza virus spikes measured by photon correlation spectroscopy, FEBS Lett. 96:120–124.

    PubMed  CAS  Google Scholar 

  • Kilbourne, E. D., 1963, Influenza virus genetics, Prog. Med. Virol. 5:79–126.

    CAS  Google Scholar 

  • Kilbourne, E. D., 1969, Future influenza vaccines and the use of genetic recombinants, Bull. WHO 41:643–645.

    PubMed  CAS  Google Scholar 

  • Kilbourne, E. D., and Murphy, J. S., 1960, Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits. Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8, J.. Exp. Med. 111:387–406.

    PubMed  CAS  Google Scholar 

  • Kilbourne, E. D., Palese, P., and Schulman, J. L., 1975, Inhibition of viral neuraminidase as a new approach to the prevention of influenza, in: Perspectives in Virology ,Vol. IX (M. Pollard, ed.), Academic Press, New York, pp. 99–113.

    Google Scholar 

  • Klenk, H.-D., 1980, Processing of the haemagglutinin: Glycosylation and proteolytic cleavage, in: Structure and Variation in Influenza Virus (G. Laver and G. Air, eds.), Elsevier/North Holland, Amsterdam, pp. 213–222.

    Google Scholar 

  • Klenk, H.-D., Rott, R., Orlich, M., et al., 1975, Activation of influenza A viruses by trypsin treatment, Virology 68:426–439.

    PubMed  CAS  Google Scholar 

  • Klenk, H.-D., Keil, W., Niemann, H., et al., 1983, The characterization of influenza A viruses by carbohydrate analysis, Curr. Top. Microbiol. Immunol. 104:247–257.

    PubMed  CAS  Google Scholar 

  • Knossow, M., Daniels, R. S., Douglas, A. R., et al., 1984, Three-dimensional structure of an antigenic mutant of the influenza virus hemagglutinin, Nature 311:678–680.

    PubMed  CAS  Google Scholar 

  • Krystal, M., Young, J. F., Palese, P., et al., 1983, Sequential mutations in hemagglutinins of influenza B virus isolates: Definition of antigenic domains, Proc. Natl. Acad. Sci. U.S.A. 80:4527–4531.

    PubMed  CAS  Google Scholar 

  • Lamb, R. A., 1983, The influenza virus RNA segments and their encoded proteins, in: Genetics of Influenza Viruses (P. Palese and D. W. Kingsbury, eds.), New York, pp. 21–69.

    Google Scholar 

  • Laver, W. G., and Kilbourne, E. D., 1966, Identification in a recombinant influenza virus of structural proteins derived from both parents, Virology 30:493–501.

    PubMed  CAS  Google Scholar 

  • Laver, W. G., and Valentine, R. C., 1969, Morphology of the isolated hemagglutinin and neuraminidase subunits of influenza virus, Virology 38:105–119.

    PubMed  CAS  Google Scholar 

  • Laver, W. G., and Webster, R. G., 1966, The structure of influenza virus. IV. Chemical studies of the host antigen, Virology 30:104–115.

    PubMed  CAS  Google Scholar 

  • Lazarowitz, S. G., and Choppin, P. W., 1975, Enhancement of infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide, Virology 68:440–454.

    PubMed  CAS  Google Scholar 

  • Lazdins, I., Haslam, E. A., and White, D. O., 1972, The polypeptides of influenza virus. VI. Composition of the neuraminidase, Virology 49:758–765.

    PubMed  CAS  Google Scholar 

  • Londo, D. R., Davis, A. R., and Nayak, D. P., 1983, Complete nucleotide sequence of the nucleoprotein gene of influenza B virus, J.. Virol 47:642–648.

    PubMed  CAS  Google Scholar 

  • Martin, M. L., Palmer, E. L., and Kendal, A. P., 1977, Lack of characteristic hexagonal surface structure on a newly isolated influenza C virus, J.. Clin. Microbiol. 6:84–86.

    PubMed  CAS  Google Scholar 

  • Murti, K. G., Bean, W. J., Jr., and Webster, R. G., 1980, Helical ribonucleoproteins of influenza virus: An electron microscopic analysis, Virology 104:224–229.

    PubMed  CAS  Google Scholar 

  • Murti, K. G., and Webster, R. G., 1986, Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy, Virology 149:36–43.

    PubMed  CAS  Google Scholar 

  • Nakada, S., Creager, R. S., Krystal, M., et al., 1984a, Influenza C virus hemagglutinin: Comparison with influenza A and B virus hemagglutinins,J.. Virol. 50:118–124.

    PubMed  CAS  Google Scholar 

  • Nakada, S., Creager, R. S., Krystal, M., et al., 1984b, Complete nucleotide sequence of the influenza C/California/78 virus nucleoprotein gene, Virus Res. 1:433–441.

    PubMed  CAS  Google Scholar 

  • Nakada, S., Graves, P. N., Desselberger, U., et al., 1985, Influenza C virus RNA 7 codes for a nonstructural protein, J.. Virol. 56:221–226.

    PubMed  CAS  Google Scholar 

  • Nakamura, K., and Compans, R. W., 1979, Host cell and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza A viruses, Virology 95:8–23.

    PubMed  CAS  Google Scholar 

  • Nayak, D. P., 1980, Defective interfering influenza viruses, Annu. Rev. Microbiol. 34:619–644.

    PubMed  CAS  Google Scholar 

  • Nermut, M. V.,, 1972, Further investigation on the fine structure of influenza virus, J.. Gen. Virol. 17:317–331.

    PubMed  CAS  Google Scholar 

  • Nermut, M. V., and Frank, H., 1971, Fine structure of influenza A2 (Singapore) as revealed by negative staining, freeze-drying and freeze-etching, J.. Gen. Virol. 10:37–51.

    PubMed  CAS  Google Scholar 

  • Nestorowicz, A., Laver, G., and Jackson, D. C., 1985, Antigenic determinants of influenza virus hemagglutinin. X. A comparison of the physical and antigenic properties of monomeric and trimeric forms, J.. Gen. Virol. 66:1687–1695.

    PubMed  CAS  Google Scholar 

  • Pfeifer, J. B., and Compans, R. W., 1984, Structure of the influenza C glycoprotein gene as determined from cloned DNA, Virus Res. 1:281–296.

    PubMed  CAS  Google Scholar 

  • Pons, M. W., Schulze, I. T., Hirst, G. K., et al., 1969, Isolation and characterization of the ribonucleoprotein of influenza virus, Virology 39:250–259.

    PubMed  CAS  Google Scholar 

  • Racaniello, V. R., and Palese, P., 1979, Influenza B virus genome: Assignment of viral polypeptides to RNA segments,J. Virol. 29:361–373.

    PubMed  CAS  Google Scholar 

  • Robertson, J. S., Robertson, M. E. St. C., and Roditi, I. J., 1984, Nucleotide sequence of RNA segment 3 of the avian influenza A/FPV/Rostock/34 and its comparison with the corresponding segment of human strains A/PR/8/34 and A/NT/60/68, Virus Res. 1:73–79.

    CAS  Google Scholar 

  • Roditi, I. J., and Robertson, J. S., 1984, Nucleotide sequence of the avian influenza virus A/fowl plague/Rostock/34 segment 1 encoding the PB2 polypeptide, Virus Res. 1:65–71.

    CAS  Google Scholar 

  • Ruigrok, R. W. H., Andree, P. J., Hooft Van Huysduynen, R. A. M., et al., 1984, Characterization of three highly purified influenza virus strains by electronmicroscopy, J. Gen. Virol. 65:799–802.

    PubMed  CAS  Google Scholar 

  • Ruigrok, R. W. H., Krijgsman, P. C. J., deRonde-Verloop, F. M., et al., 1985, Natural heterogeneity of shape, infectivity and protein composition in an influenza A (H3N2) virus preparation, Virus. Res. 3:69–76.

    PubMed  CAS  Google Scholar 

  • Schmidt, M. F. G., 1982, Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses, Virology 116:327–338.

    PubMed  CAS  Google Scholar 

  • Schmidt, M. F. G., 1984, The transfer of myristic and other fatty acids on lipid and viral protein acceptors in cultured cells infected with Semliki Forest and influenza virus, EMBOJ. 3:2295–2300.

    CAS  Google Scholar 

  • Shaw, M. W., Lamb, R. A., Erickson, B. W., et al., 1982, Complete nucleotide sequence of the neuraminidase gene of influenza B virus, Proc. Natl. Acad. Sci. U.S.A. 79:6817–6821.

    PubMed  CAS  Google Scholar 

  • Shaw, M. W., Choppin, P. W., and Lamb, R. A., 1983, A previously unrecognized influenza B virus glycoprotein from a bicistronic mRNA that also encodes the viral neuraminidase, Proc. Natl. Acad. Sci. U.S.A. 80:4879–4883.

    PubMed  CAS  Google Scholar 

  • Singer, S. J., and Nicolson, G. L., 1972, The fluid mosaic model of the structure of cell membranes, Science 175:720–731.

    PubMed  CAS  Google Scholar 

  • Sivasubramanian, N., and Nayak, D. P., 1982, Sequence analysis of the polymerase 1 gene and the secondary structure prediction of polymerase 1 protein of human influenza virus A/WSN/33, J. Virol. 44:321–329.

    PubMed  CAS  Google Scholar 

  • Skehel, J. J., Hay, A. J., and Waterfield, M. D., 1980, Influenza-virus, in: Cell Membranes and Viral Envelopes ,Vol. 2 (H. A. Blough and J. M. Tiffany, eds.), Academic Press, London, pp. 647–681.

    Google Scholar 

  • Skehel, J. J., Stevens, D. J., Daniels, R. S., et al., 1984, A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody, Proc. Natl. Acad. Sci. U.S.A. 81:1779–1783.

    PubMed  CAS  Google Scholar 

  • Sleigh, M. J., Both, G. W., and Brownlee, G. G., 1979, A new method for the size estimation of the RNA genome segments of influenza virus, Nucleic Acids Res. 6:1309–1321.

    PubMed  CAS  Google Scholar 

  • Taylor, R. B., Duffus, W. P. H., Raff, M. C., et al., 1971, Redistribution and pinocytosis of lymphocyte surface immunoglobulin molecules induced by anti-immunoglobulin antibody, Nature (New Biol. 1 233:225–229.

    CAS  Google Scholar 

  • Tobita, K., and Kilbourne, E. D., 1974, Genetic recombination for antigenic markers of antigenically different strains of influenza B virus, J. Virol 13:347–352.

    PubMed  CAS  Google Scholar 

  • Varghese, J. N., Laver, W. G., and Colman, P. M., 1983, Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution, Nature 303:35–40.

    PubMed  CAS  Google Scholar 

  • Verhoryen, M., Fang, R., Min Jou, W., et al., 1980, Antigenic drift between the hemagglutinin of the Hong Kong influenza strains A/Aichi/2/68 and A/Victoria/3/75, Nature 286:771–775.

    Google Scholar 

  • Ward, C. W., 1981, Structure of the influenza virus hemagglutinin, Curr. Top. Microbiol. Immunol. 94/95:1–74.

    Google Scholar 

  • Ward, C. W., and Dopheide, T. A. A., 1979, Primary structure of the Hong Kong (H3) hemagglutinin, Br. Med. Bull. 35:51–56.

    PubMed  CAS  Google Scholar 

  • Ward, C. W., and Dopheide, T. A. A., 1980, The Hong Kong (H3) hemagglutinin. Complete amino acid sequence and oligosaccharide distribution for the heavy chain of A/Memphis/102/72, in: Structure and Variation of Influenza Virus (W. G. Laver and G. Air, eds.), Elsevier, Amsterdam, pp. 27–38.

    Google Scholar 

  • Ward, C. W., Murray, J. M., Roxburgh, C. M., et al., 1983, Chemical and antigenic characterization of the carbohydrate side chains of an Asian (N2) influenza virus neuraminidase, Virology 126:370–375.

    PubMed  CAS  Google Scholar 

  • Waterfield, M. D., Espelie, K., Elder, K., et al., 1979, Structure of the hemagglutinin of influenza virus, Br. Med. Bull. 35:56–67.

    Google Scholar 

  • Wiley, D. C., Wilson, I. A., and Skehel, J. J., 1981, Structural identification of the antibody-binding sites of Hong Kong influenza hemagglutinin and their involvement in antigenic variation, Nature 289:373–378.

    PubMed  CAS  Google Scholar 

  • Wiley, D. C., Wilson, I. A., and Skehel, J. J., 1984, The hemagglutinin membrane glycoprotein of influenza virus, Biol. Macromol. Assemblies 1:299–336.

    CAS  Google Scholar 

  • Wilson, I. A., Skehel, J. J., and Wiley, D. C., 1981, Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution, Nature 289:366–373.

    PubMed  CAS  Google Scholar 

  • Wilson, I. A., Ladner, R. C., Skehel, J. J., et al., 1983, The structure and role of the carbohydrate moieties of influenza virus hemagglutinin, Biochem. Soc. Trans. 11:145–147.

    CAS  Google Scholar 

  • Wilson, J. C., Tudor, L. R., and Darlington, R. W., 1977, Morphology of influenza virions from the infected host, Am. Soc. Microbiol. Abstr.

    Google Scholar 

  • Winter, G., and Fields, S., 1982, Nucleotide sequence of human influenza A/PR/8/34 segment 2, Nucleic Acids Res. 10:2135–2143.

    PubMed  CAS  Google Scholar 

  • Wrigley, N. G., 1979, Electron microscopy of influenza virus, Br. Med. Bull. 35:35–38.

    PubMed  CAS  Google Scholar 

  • Wrigley, N. G., Skehel, J. J., Charlwood, P. A., et al., 1973, The size and shape of influenza virus neuraminidase, Virology 51:525–529.

    PubMed  CAS  Google Scholar 

  • Wrigley, N. G., Brown, E. B., Daniels, R. S., et al., 1983, Electron microscopy of influenza haemagglutinin-monoclonal antibody complexes, Virology 131:308–314.

    PubMed  CAS  Google Scholar 

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© 1987 Edwin D. Kilbourne, M.D.

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Kilbourne, E.D. (1987). Viral Structure and Composition. In: Influenza. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5239-6_3

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