Abstract
The mammalian picornaviruses (from pico-small, and rna-containing a ribonucleate genome) comprise a large group of agents, which can presently be classified according to a scheme such as that shown in Table I.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
BUREES, A.T.H., FOX, S.M. and PARDOE, I.U. Evidence for the lack of glycoprotein in the encephalomyocarditis virus particle. J. Gen. Virol. (1975), 18, 33–49.
SCRABA, D.G., KAY, G.M. and COLTER, J. S. Physicochemical studies of the three variants of Mengo virus and their constituent ribonucleates. J. Mol. Biol. (1967) 26 67–79
BUREESS, A.T.H. and CLOTHIER, F.W. Particle weight and other biophysical properties of encephalomyocarditis virus. J. Gen. Virol. (1970), 6, 381–395.
TAMOCK, G.A., GIBBS, A.J. and COOPER, P.D. A re-examination of the molecular weight of poliovirus RNA. Biochem. Biophys. Res. Commun. (1970) 38 294–304
BROW, F., mmm, J.F.E. and STOTT, E.J. Molecular weight of rhinovirus ribonucleic acid. J. Gen. Virol. (1970), 8, 145–148.
HEWMAN, J.F.E., ROWLANDS, D.J. and BROWN, F. A physicochemical subgrouping of the mammalian picornaviruses. J. Gen.Virol. (1975), 18, 171–180.
SPECTOR, D.H. and BALTIMORE, D. Requirement of 3’-terminal polyadenylic acid for the infectivity of poliovirus RNA. Proc. Nat. Acad. Sci. U.S.A. (1974)> 71 2983–2987
BURNESS, A.T.H., PARDOE, I.U., DUFFY, E.M., BHALLA, R.B. and GOLDSTEIN, N.O. The size and location of the poly(A) tract in EMC virus RNA. J. Gen. Virol. (1977), 34 331–345
BROWN, P., NEWMAN, J., STOTT, J., PORTER, A., FRISBY, D., NEWTON, G., CAREY, N. and FELLNER, P. Poly(G) in animal viral RNAs. Nature (1974) 251 342–344
PEREZ-BERCOFF, E. and GANDER, M. The genomic ENA of Mengo virus. I. Location of the poly(C) tract. Virology (1977) 80, 426–429.
LEE, Y.P., NOMOTO, A., DETJEN, B.M. and WIMMEE, E. A protein covalently linked to poliovirus genome ENA. Proc. Nat. Acad. Sci. U.S.A. (1977), 74 59–63.
HRUBY, D.E. and EOBEETS, W.K. Encephalomyocarditis virus ENA. III. Presence of a genome-associated protein. J. Virol. (1978) 25, 413–415.
SANGAR, D.Y., ROWLANDS, D.J., HARRIS, T.J.E. and BEOWN, P. Protein covalently linked to foot-and-mouth disease virus ENA. Nature (1977), 268, 648–650
NOMOTO, A., DETJEN, B., POZZATTI, E. and WIMMEE, E. The location of the polio genome protein in viral ENAs and its implication for ENA synthesis. Nature (1977), 268, 208–213.
MAIZEL, J.Y. Evidence for multiple components in the structural protein of type 1 poliovirus. Biochem. Biophys. Ees. Commun. (1963), 13 483–489.
SHAPIRO, A.L., VINUELA, E. and MAIZEL, J.Y. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Ees. Commun. (1967) 28 815–820.
RUECKEET, E.E. On the structure and morphogenesis of picornaviruses. In Comprehensive Yirology, V0L.6. Praenkel-Conrat, H. and Wagner, E.E. eds. (1976), pp. 151–215. Plenum Press, New York.
ZIOLA, B.E. and SCRABA, D.G. Structure of the Mengo virion. III.Purification and amino acid compositions of the major capsid polypeptides. Virology, (1975), 64 228–235.
JACOBSON, M.P., ASSO, J. and BALTIMORE, D. Further evidence on the formation of poliovirus proteins. J. Mol. Biol. (1970) 49 657–669
STOLTZPUS, C.M. and ERUECKEET, E.E. Capsid polypeptides of Maus-Elberfeld virus. J. Virol. (1972), 10, 347–355.
ADAM, K.H. and STEOHMAIER, K. Isolation of the coat proteins of foot-and-mouth disease virus and analysis of the composition of N-terminal end groups. Biochem. Biophys. Ees. Common. (1974), 61, 185–192
CHLUMECKA, Y., D’OBRENAN, P. and COLTER, J.S. Isoelectric focusing studies of Mengo variants, their protein structxire units and constituent polypeptides. J. Gen.Virol. (1977) 35, 425–437.
KAY, C.M., COLTER, J.S. and OIKAWA, K. Circular dichroism studies on Mengo virus variants and their constituent ribonucleates. Can. J. Biochem. (1970), 48, 94O-943
ZIOLA, B.R., and SCRABA, D.G. Structure of the Mengo virion. IT. Amino and carboxyl-terminal analyses of the major capsid polypeptides. Virology (1976), 71, 111–121.
BURRELL, C.J. and COOPER, P.D. H-terminal aspartate, glycine and serine in poliovirus capsid proteins. J. Gen. Virol. (1973), 21, 443–451.
MATHEKA, H.D. and BACHRACH, H.L. N-terminal amino acid sequences in the major capsid proteins of foot-and-mouth disease virus types A, 0 and C. J. Virol. (1975), 16, 1248–1255.
BACHRACH, H.L., SWANEY, J.B. and TANDE WOUDE, G.P. Isolation of the structural polypeptides of foot-and-mouth disease virus and analysis of their C-terminal sequences. Virology (1975), 52, 520–528.
PINCH, J.T. and KLUG, A. Structure of poliomyelitis virus. Nature (1959), 189, 1709–1714.
FINCH, J.T. and KLUG, A. Arrangement of protein subunits and the distribution of nucleic acid in turnip yellow mosaic virus. II. Electron microscope studies. J. Mol. Biol. (1966) 15, 344–364.
MAYOR, H.D. Picornavirus symmetry. Tirology (1964) 22 156–160.
AGRAWAL, H.O. Studies on the structure of poliovirus. Arch. Gesamte Tirusforsch. (1966)12, 365–572.
HORNE, R.W. and NAGINGTON, J. Electron microscope studies of the development and structure of poliomyelitis virus. J. Mol. Biol. (1959), 1, 333–338.
RUECKERT, R.R., DUNKER, A.K. and STOLTZPUS, C.M. The structure of mouse-Elberfeld virus; a model. Proc. Nat. Acad. Sci. U.S.A. (1969) 62 912–919
DUNKER, A.K. and RUECKERT, R.R. Fragments generated by pH-dissociation of ME virus and their relation to the structure of the virion. J. Mol. Biol. (1971), 58, 217–235.
MAK, T.W., COLTER, J.S. and SCRABA, D.G. Structure of the Mengo virion. II. Physicochemical and electron microscopic analysis of degraded virus. Yirology (1974), 57 545–553.
TALBOT, P. and BROWN, I. A model for foot-and-mouth disease virus. J. Gen. Virol. (1972), 15, 165–170.
CASPAR, D.L.D. and KLUG, A. Physical principles in the construction of regular viruses. Cold Spring Harbor Symp. Quant. Biol. (1962), 27, 1–24.
JOHNSTON, M.D. and MARTIN, S.J. Capsid and procapsid proteins of a bovine enterovirus. J. Gen. Virol. (1971), 11, 71–79
MAIZEL, J.Y., PHILLIPS, B.A. and SUMMERS, D.F. Composition of artificially produced and naturally occurring empty capsids of poliovirus type 1. Virology (1967) 32, 692–699
CROWELL, R.L. and PHILLIPSON, L. Specific alterations of Coxsackie vims B5 eluted from Hela cells. J.Virol. (1971), 8, 509–515.
LONBER-GHOLM, K. and KORANT, B.D. Early interaction of rhinoviruses with host cells. J. Virol. (1972), 9 29–4O
KORANT, B.D., LONBER-GHOLM, K., NOBLE, J. and STASNY, J.T. Naturally occurring and artificially produced components of three rhinoviruses.Virology (1972) 48 71–86
KATAGIRI, S., AIKAWA, S. and HINUMA, Y. Stepwise degradation of poliovirus capsids by alkaline treatment. J. Gen. Virol. (1971) 13 101–109
LONBER-GHOLM, K. and YIN, F.H. Antigenic determinants of infective and inactivated human rhinovirus type 2. J. Virol. (1975), 12, 114–123.
BREINDL, M. YP4, the D-reactive part of poliovirus. Virology (1971), 46, 962–964
PHILIPSON, L., BEATRICE, S.T. and CROWELL, R.L. A structural model for picornaviruses as suggested from an analysis of ureadegraded virions and procapsids of Coxsackie virus B5. Virology (1975), 54, 69–79.
STUDY GROUP ON PICORNAYIRIDAE. Picornaviridae. Intervirology (1975), 4, 303–316.
LONBER-GHOLM, K. and PHILIPSON, L. Early interaction between animal viruses and cells. In Monographs in Tirology, Vol. 9, Melnick, J.L. ed. (1974), PP: 1–148. S. Karger, Basel.
MANDEL, B. Gharacterization of type 1 poliovirus by electrophoretic analysis. Virology (1971), 44, 554–568.
KORANT, B.D., LONBER-GHOLM, K., YIN, P.H. and NOBLE-HARYEY, J. Fractionation of biologically active and inactive populations of human rhinovirus type 2. Virology (1975), 63, 384–394
CARTHEW, P. and MARTIN, S.J. The iodination of bovine enterovirus particles. J. Gen. Virol. (1974) 24 525–534
LONBER-GHOLM, K. and BUTTERWORTH, B. Investigation of the structure of polio-and human-rhinovirions through the use of selective chemical reactivity. Virology (1976), 71, 207–216.
BURROUGHS, J.N., ROWLANDS, D.J., SANGAR, D.Y., TALBOT, P. and BROWN, F. Further evidence for multiple proteins in the foot-and-mouth disease virus particle. J. Gen. Virol. (1971), 13 75–84.
ROWLANDS, D.J., SANGAR, D.Y. and BROWN, F. Relationship of the antigenic structure of foot-and-mouth disease virus to the process of infection. J. Gen. Virol. (1971), 13, 85–93
GAYANAGH, D., SANGAR, D.Y., ROWLANDS, D.J. and BROWN, F. Immunogenic and cell attachment sites of FMDY; further evidence for their location in a single capsid polypeptide. J. Gen. Virol. (1977), 35, 149–158.
SANGAR, D.Y., ROWLANDS, D.J., GAYANAGH, D. and BROWN, F. Gharacterization of the minor polypeptides in the foot-and-mouth disease virus particle. J. Gen. Virol. (1976), 31, 35–46.
LUND, G.A., ZIOLA, B.R., SALMI, A. and SGRABA, D.G. Structure of the Mengo virion. V. Distribution of the capsid polypeptides with respect to the surface of the virus particle. Virology (1977), 78, 35–44.
PETERS, K. and RIGHARDS, F.M. Ghemical cross-linking reagents and problems in studies of membrane structure. Ann. Rev. Biochem. (1977), 46, 523–551.
HORDERN, J.S., LEONARD, J.D. and SGRABA, D.G. Manuscript in preparation.
ZIOLA, B.R. and SGRABA, D.G. Structure of the Mengo virion. I. Polypeptide and ribonucleate components of the virus particle. Virology (1974), 57, 551–542.
PAUCHA, E., SEEHAFER, J. and COLTER, J.S. Synthesis of viral-specific polypeptides in Mengo virus-infected L cells: evidence for asymmetric translation of the viral genome. Virology (1974), 61, 315–326.
REKOSH, D.M.K. The Molecular Biology of Picornaviruses. In The Molecular Biology of Animal Yiruses, Vol. 1. Nayak, D.P. ed. (1977), pp.65–110. Marcel Dekker Inc., New York.
EGGEN, K.L. and SHATKIN, A.J. In vitro translation of cardiovirus ribonucleic acid by mammalian cell-free extracts. J. Virol. (1972), 9 636–645
KORANT, B.D. Cleavage of viral precxirsor proteins iN vivo and in vitro. J. Virol. (1972), 10, 751–759.
KORANT, B.D. Cleavage of poliovirus-specific polypeptide aggregates. J. Virol. (1975), 12, 556–563.
TABER, R., REKOSH, D. and BALTIMORE, D. Effect of pactamycin on synthesis of poliovirus proteins: a method for genetic mapping. J. Virol. (1971), 8, 395–410.
LAWRENCE, C. and THACH, R.E. Identification of a viral protein involved in post-translational maturation of the encephalomyocarditis virus capsid precursor. J. Virol. (1975), 15, 918–928.
PHILLIPS, B.A. The morphogeneis of poliovirus. Current Topics in Microbiology and Immunology (1972), 58 156–174
JACOBSON, M.F. and BALTIMORE, D. Morphogenesis of poliovirus. I. Association of viral RNA with coat protein. J. Mol. Biol. (1968) 33, 369–378.
FERNAN-DEZTOMAS, C.B. and BALTIMORE, D. Morphogenesis of poliovimis. II. Demonstration of a new intermediate, the provirion. J. Virol. (1973), 12, 1122–1130.
MCGREGOR, S., HALL, L. and RUECKERT, R.R. Evidence for the existence of protomers in the assembly of encephalomyocarditis virus. J. Virol. (1975), 15, 1107–1120
MCGREGOR, S. and RUCKERT, R.R. Picornaviral capsid assembly: similarity of rhinovirus and enterovirus precursor subunits. J. Virol. (1977), 21, 548–553.
LEE, P.W.K., PAUCHA, E. and COLTER, J.S. Identification andpartial characterization of a new (50S) subviral particle in Mengo virus-infected cells. Virology (1978), 85, 286–295.
GHENDRON, Y., YAZOBSEN, E. and MIKHENJEYA, A. Study of some stages of poliovirus morphogenesis in MiO cells. J. Virol. (1972), 10, 261–266.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1979 Plenum Press, New York
About this chapter
Cite this chapter
Scraba, D.G. (1979). The Picornavirion: Structure and Assembly. In: Pérez-Bercoff, R. (eds) The Molecular Biology of Picornaviruses. NATO Advanced Study Institutes Series, vol 23. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1000-6_1
Download citation
DOI: https://doi.org/10.1007/978-1-4684-1000-6_1
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-1002-0
Online ISBN: 978-1-4684-1000-6
eBook Packages: Springer Book Archive