Skip to main content
NCBI home page
Transactions of the American Clinical and Climatological Association logoLink to Transactions of the American Clinical and Climatological Association
. 1984;95:138–156.

Membrane proteins and virus virulence.

P W Choppin
PMCID: PMC2279623  PMID: 6382744

Full text

PDF
138

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Buser F. Side reaction to measles vaccination suggesting the Arthus phenomenon. N Engl J Med. 1967 Aug 3;277(5):250–251. doi: 10.1056/NEJM196708032770507. [DOI] [PubMed] [Google Scholar]
  2. Choppin P. W. Measles virus and chronic neurological diseases. Ann Neurol. 1981 Jan;9(1):17–20. doi: 10.1002/ana.410090104. [DOI] [PubMed] [Google Scholar]
  3. Choppin P. W., Richardson C. D., Merz D. C., Hall W. W., Scheid A. The functions and inhibition of the membrane glycoproteins of paramyxoviruses and myxoviruses and the role of the measles virus M protein in subacute sclerosing panencephalitis. J Infect Dis. 1981 Mar;143(3):352–363. doi: 10.1093/infdis/143.3.352. [DOI] [PubMed] [Google Scholar]
  4. Choppin P. W., Richardson C. D., Merz D. C., Scheid A. Functions of surface glycoproteins of myxoviruses and paramyxoviruses and their inhibition. Ciba Found Symp. 1981;80:252–269. doi: 10.1002/9780470720639.ch16. [DOI] [PubMed] [Google Scholar]
  5. Choppin P. W., Scheid A. The role of viral glycoproteins in adsorption, penetration, and pathogenicity of viruses. Rev Infect Dis. 1980 Jan-Feb;2(1):40–61. doi: 10.1093/clinids/2.1.40. [DOI] [PubMed] [Google Scholar]
  6. Compans R. W., Holmes K. V., Dales S., Choppin P. W. An electron microscopic study of moderate and virulent virus-cell interactions of the parainfluenza virus SV5. Virology. 1966 Nov;30(3):411–426. doi: 10.1016/0042-6822(66)90119-x. [DOI] [PubMed] [Google Scholar]
  7. Connolly J. H., Allen I. V., Hurwitz L. J., Millar J. H. Measles-virus antibody and antigen in subacute sclerosing panencephalitis. Lancet. 1967 Mar 11;1(7489):542–544. doi: 10.1016/s0140-6736(67)92117-4. [DOI] [PubMed] [Google Scholar]
  8. ENDERS J. F., PEEBLES T. C. Propagation in tissue cultures of cytopathogenic agents from patients with measles. Proc Soc Exp Biol Med. 1954 Jun;86(2):277–286. doi: 10.3181/00379727-86-21073. [DOI] [PubMed] [Google Scholar]
  9. Fein R. L. Transurethral electrocautery procedures in patients with cardiac pacemakers. JAMA. 1967 Oct 2;202(1):101–103. doi: 10.1001/jama.202.1.101. [DOI] [PubMed] [Google Scholar]
  10. Gething M. J., White J. M., Waterfield M. D. Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2737–2740. doi: 10.1073/pnas.75.6.2737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Graves M. C., Silver S. M., Choppin P. W. Measles virus polypeptides synthesis in infected cells. Virology. 1978 May 1;86(1):254–263. doi: 10.1016/0042-6822(78)90025-9. [DOI] [PubMed] [Google Scholar]
  12. HENLE G., DEINHARDT F., GIRARDI A. Cytolytic effects of mumps virus in tissue cultures of epithelial cells. Proc Soc Exp Biol Med. 1954 Nov;87(2):386–393. doi: 10.3181/00379727-87-21390. [DOI] [PubMed] [Google Scholar]
  13. Hall W. W., Choppin P. W. Evidence for lack of synthesis of the M polypeptide of measles virus in brain cells in subacute sclerosing panencephalitis. Virology. 1979 Dec;99(2):443–447. doi: 10.1016/0042-6822(79)90026-6. [DOI] [PubMed] [Google Scholar]
  14. Hall W. W., Choppin P. W. Measles-virus proteins in the brain tissue of patients with subacute sclerosing panencephalitis: absence of the M protein. N Engl J Med. 1981 May 7;304(19):1152–1155. doi: 10.1056/NEJM198105073041906. [DOI] [PubMed] [Google Scholar]
  15. Hall W. W., Lamb R. A., Choppin P. W. Measles and subacute sclerosing panencephalitis virus proteins: lack of antibodies to the M protein in patients with subacute sclerosing panencephalitis. Proc Natl Acad Sci U S A. 1979 Apr;76(4):2047–2051. doi: 10.1073/pnas.76.4.2047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hall W. W., Sahgal V., Harter D. H., Choppin P. W. Abnormal levels of antibodies to measles-virus proteins in patient with mental retardation and seizures 24 years after measles encephalitis. Lancet. 1979 Nov 3;2(8149):967–968. doi: 10.1016/s0140-6736(79)92669-2. [DOI] [PubMed] [Google Scholar]
  17. Heggeness M. H., Smith P. R., Choppin P. W. In vitro assembly of the nonglycosylated membrane protein (M) of Sendai virus. Proc Natl Acad Sci U S A. 1982 Oct;79(20):6232–6236. doi: 10.1073/pnas.79.20.6232. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Helenius A., Kartenbeck J., Simons K., Fries E. On the entry of Semliki forest virus into BHK-21 cells. J Cell Biol. 1980 Feb;84(2):404–420. doi: 10.1083/jcb.84.2.404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Holmes K. V., Choppin P. W. On the role of the response of the cell membrane in determining virus virulence. Contrasting effects of the parainfluenza virus SV5 in two cell types. J Exp Med. 1966 Sep 1;124(3):501–520. doi: 10.1084/jem.124.3.501. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Homma M., Ouchi M. Trypsin action on the growth of Sendai virus in tissue culture cells. 3. Structural difference of Sendai viruses grown in eggs and tissue culture cells. J Virol. 1973 Dec;12(6):1457–1465. doi: 10.1128/jvi.12.6.1457-1465.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Horta-Barbosa L., Fuccillo D. A., Sever J. L., Zeman W. Subacute sclerosing panencephalitis: isolation of measles virus from a brain biopsy. Nature. 1969 Mar 8;221(5184):974–974. doi: 10.1038/221974a0. [DOI] [PubMed] [Google Scholar]
  22. Hsu M. C., Scheid A., Choppin P. W. Enhancement of membrane-fusing activity of sendai virus by exposure of the virus to basic pH is correlated with a conformational change in the fusion protein. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5862–5866. doi: 10.1073/pnas.79.19.5862. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Hsu M. C., Scheid A., Choppin P. W. Fusion of Sendai virus with liposomes: dependence on the viral fusion protein (F) and the lipid composition of liposomes. Virology. 1983 Apr 15;126(1):361–369. doi: 10.1016/0042-6822(83)90485-3. [DOI] [PubMed] [Google Scholar]
  24. Hsu M. C., Scheid A., Choppin P. W. Reconstitution of membranes with individual paramyxovirus glycoproteins and phospholipid in cholate solution. Virology. 1979 Jun;95(2):476–491. doi: 10.1016/0042-6822(79)90502-6. [DOI] [PubMed] [Google Scholar]
  25. Huang R. T., Rott R., Klenk H. D. Influenza viruses cause hemolysis and fusion of cells. Virology. 1981 Apr 15;110(1):243–247. doi: 10.1016/0042-6822(81)90030-1. [DOI] [PubMed] [Google Scholar]
  26. KOHN A. POLYKARYOCYTOSIS INDUCED BY NEWCASTLE DISEASE VIRUS IN MONOLAYERS OF ANIMAL CELLS. Virology. 1965 Jun;26:228–245. doi: 10.1016/0042-6822(65)90050-4. [DOI] [PubMed] [Google Scholar]
  27. Lazarowitz S. G., Choppin P. W. Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology. 1975 Dec;68(2):440–454. doi: 10.1016/0042-6822(75)90285-8. [DOI] [PubMed] [Google Scholar]
  28. Lazarowitz S. G., Compans R. W., Choppin P. W. Influenza virus structural and nonstructural proteins in infected cells and their plasma membranes. Virology. 1971 Dec;46(3):830–843. doi: 10.1016/0042-6822(71)90084-5. [DOI] [PubMed] [Google Scholar]
  29. Lenard J., Miller D. K. pH-dependent hemolysis by influenza, Semliki, Forest virus, and Sendai virus. Virology. 1981 Apr 30;110(2):479–482. doi: 10.1016/0042-6822(81)90079-9. [DOI] [PubMed] [Google Scholar]
  30. Lin F. H., Thormar H. Absence of M protein in a cell-associated subacute sclerosing panencephalitis virus. Nature. 1980 Jun 12;285(5765):490–492. doi: 10.1038/285490a0. [DOI] [PubMed] [Google Scholar]
  31. Machamer C. E., Hayes E. C., Zweerink H. J. Cells infected with a cell-associated subacute sclerosing panencephalitis virus do not express M protein. Virology. 1981 Jan 30;108(2):515–520. doi: 10.1016/0042-6822(81)90460-8. [DOI] [PubMed] [Google Scholar]
  32. Maeda T., Kawasaki K., Ohnishi S. Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4133–4137. doi: 10.1073/pnas.78.7.4133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. McSharry J. J., Compans R. W., Choppin P. W. Proteins of vesicular stomatitis virus and of phenotypically mixed vesicular stomatitis virus-simian virus 5 virions. J Virol. 1971 Nov;8(5):722–729. doi: 10.1128/jvi.8.5.722-729.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. McSharry J. J., Compans R. W., Lackland H., Choppin P. W. Isolation and characterization of the nonglycosylated membrane protein and a nucleocapsid complex from the paramyxovirus SV5. Virology. 1975 Oct;67(2):365–374. doi: 10.1016/0042-6822(75)90438-9. [DOI] [PubMed] [Google Scholar]
  35. Merz D. C., Scheid A., Choppin P. W. Immunological studies of the functions of paramyxovirus glycoproteins. Virology. 1981 Feb;109(1):94–105. doi: 10.1016/0042-6822(81)90474-8. [DOI] [PubMed] [Google Scholar]
  36. Merz D. C., Scheid A., Choppin P. W. Importance of antibodies to the fusion glycoprotein of paramyxoviruses in the prevention of spread of infection. J Exp Med. 1980 Feb 1;151(2):275–288. doi: 10.1084/jem.151.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Nagai Y., Klenk H. D., Rott R. Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology. 1976 Jul 15;72(2):494–508. doi: 10.1016/0042-6822(76)90178-1. [DOI] [PubMed] [Google Scholar]
  38. Norrby E., Enders-Ruckle G., Meulen V. Differences in the appearance of antibodies to structural components of measles virus after immunization with inactivated and live virus. J Infect Dis. 1975 Sep;132(3):262–269. doi: 10.1093/infdis/132.3.262. [DOI] [PubMed] [Google Scholar]
  39. Norrby E., Gollmar Y. Identification of measles virus-specific hemolysis-inihibiting antibodies separate from hemagglutination-inhibiting antibodies. Infect Immun. 1975 Feb;11(2):231–239. doi: 10.1128/iai.11.2.231-239.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Norrby E., Penttinen K. Differences in antibodies to the surface components of mumps virus after immunization with formalin-inactivated and live vaccines. J Infect Dis. 1978 Nov;138(5):672–676. doi: 10.1093/infdis/138.5.672. [DOI] [PubMed] [Google Scholar]
  41. Payne F. E., Baublis J. V., Itabashi H. H. Isolation of measles virus from cell cultures of brain from a patient with subacute sclerosing panencephalitis. N Engl J Med. 1969 Sep 11;281(11):585–589. doi: 10.1056/NEJM196909112811103. [DOI] [PubMed] [Google Scholar]
  42. ROIZMAN B. Polykaryocytosis. Cold Spring Harb Symp Quant Biol. 1962;27:327–342. doi: 10.1101/sqb.1962.027.001.031. [DOI] [PubMed] [Google Scholar]
  43. Richardson C. D., Choppin P. W. Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action. Virology. 1983 Dec;131(2):518–532. doi: 10.1016/0042-6822(83)90517-2. [DOI] [PubMed] [Google Scholar]
  44. Richardson C. D., Scheid A., Choppin P. W. Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the F1 or HA2 viral polypeptides. Virology. 1980 Aug;105(1):205–222. doi: 10.1016/0042-6822(80)90168-3. [DOI] [PubMed] [Google Scholar]
  45. Scheid A., Caliguiri L. A., Compans R. W., Choppin P. W. Isolation of paramyxovirus glycoproteins. Association of both hemagglutinating and neuraminidase activities with the larger SV5 glycoprotein. Virology. 1972 Dec;50(3):640–652. doi: 10.1016/0042-6822(72)90418-7. [DOI] [PubMed] [Google Scholar]
  46. Scheid A., Choppin P. W. Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology. 1974 Feb;57(2):475–490. doi: 10.1016/0042-6822(74)90187-1. [DOI] [PubMed] [Google Scholar]
  47. Scheid A., Choppin P. W. Isolation and purification of the envelope proteins of Newcastle disease virus. J Virol. 1973 Feb;11(2):263–271. doi: 10.1128/jvi.11.2.263-271.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Scheid A., Choppin P. W. Protease activation mutants of sendai virus. Activation of biological properties by specific proteases. Virology. 1976 Jan;69(1):265–277. doi: 10.1016/0042-6822(76)90213-0. [DOI] [PubMed] [Google Scholar]
  49. Scheid A., Choppin P. W. Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virology. 1977 Jul 1;80(1):54–66. doi: 10.1016/0042-6822(77)90380-4. [DOI] [PubMed] [Google Scholar]
  50. Scott T. F., Bonanno D. E. Reactions to live-measles-virus vaccine in children previously inoculated with killed-virus vaccine. N Engl J Med. 1967 Aug 3;277(5):248–250. doi: 10.1056/NEJM196708032770506. [DOI] [PubMed] [Google Scholar]
  51. Silver S. M., Scheid A., Choppin P. W. Loss on serial passage of rhesus monkey kidney cells of proteolytic activity required for Sendai virus activation. Infect Immun. 1978 Apr;20(1):235–241. doi: 10.1128/iai.20.1.235-241.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Skehel J. J., Bayley P. M., Brown E. B., Martin S. R., Waterfield M. D., White J. M., Wilson I. A., Wiley D. C. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc Natl Acad Sci U S A. 1982 Feb;79(4):968–972. doi: 10.1073/pnas.79.4.968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Skehel J. J., Waterfield M. D. Studies on the primary structure of the influenza virus hemagglutinin. Proc Natl Acad Sci U S A. 1975 Jan;72(1):93–97. doi: 10.1073/pnas.72.1.93. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Wechsler S. L., Weiner H. L., Fields B. N. Immune response in subacute sclerosing panencephalitis: reduced antibody response to the matrix protein of measles virus. J Immunol. 1979 Aug;123(2):884–889. [PubMed] [Google Scholar]
  55. White J., Matlin K., Helenius A. Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses. J Cell Biol. 1981 Jun;89(3):674–679. doi: 10.1083/jcb.89.3.674. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Transactions of the American Clinical and Climatological Association are provided here courtesy of American Clinical and Climatological Association

RESOURCES