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Issue
Vet. Res.
Volume 32, Number 5, September-October 2001
Page(s) 475 - 489
DOI https://doi.org/10.1051/vetres:2001139
How to cite this article Vet. Res. (2001) 475-489
  1. Aminoff D., Methods for the quantitative estimation of N-acetyl-neuraminic acid and their application to hydrolysates of sialomucoids, Biochem. J. 81 (1961) 384-392 [PubMed].
  2. Anderson S. G., The reaction between red cells and viruses of the influenza group: Studies with Newcastle disease, Aust. J. Exp. Biol. Med. Sci. 25 (1947) 163-174.
  3. Appleyard G., Oram J.D., The assay of influenza antineuraminidase activity by an elution inhibition technique, J. Gen. Virol. 34, (1977) 137-144.
  4. Bang F.B., Foard M. A., The effect of Newcastle disease virus on chicken red blood cells. I. Variation in agglutination patterns with different strains of virus, Am. J. Hyg. 55 (1952) 363-372 [PubMed].
  5. Bang F.B., Libert R., Agglutination of red cells altered by the action of Newcastle disease virus. I. The effect of chicken sera from infected birds on sensitized cells, Bull. Johns Hopkins Hosp. 85 (1949) 416-430 [PubMed].
  6. Bang F.B., Libert R., The effect of Newcastle disease virus on chicken red blood cells. II. A study of the adsorption, sensitization and elution process, Am. J. Hyg. 55 (1952) 363-385 [PubMed].
  7. Burnet F.M., The haemolytic action of Newcastle disease virus. I. The two types of interaction between virus and red cells, Aust. J. Exp. Biol. Med. Sci. 28 (1950) 299-309 [PubMed].
  8. Burnet F.M., Anderson, S.G., Modification of human red cells by virus action. II. Agglutination of modified human red cells by sera from cases of infectious mononucleosis, Brit. J. Exp. Pathol. 27 (1946) 236-244.
  9. Burnet F.M., Beveridge W.I.B., Mcewin J., Boake W. C., Studies on the Hirst haemagglutination reaction with influenza and Newcastle disease viruses. I. Partial dissociation of haemagglutinin and infective activity of Newcastle disease virus, Aust. J. Exp. Biol. Med. Sci. 23 (1945) 177-192.
  10. Colman P.M., Hoyne P.A., Lawrence M.C., Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase, J. Virol. 67 (1993), 2972-2980.
  11. Crennell S., Takimoto T., Portner A., Taylor G., Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat. Struct. Biol. 7 (2000) 1068-1074.
  12. Elliott M.A., Elliott H.G., McGuire J., Smith K.D., Regarding the specificity of Newcastle disease virus sialidase, Glycobiology 6 (1996) 5-12.
  13. Epa V.C., Modeling the paramyxovirus hemagglutinin-neuraminidase protein, Proteins Struct. Funct. Genet. 29 (1997) 264-281.
  14. Galinski M.S., Wechsler S.L., The molecular biology of the paramyxovirus genus, in: Kingsbury D. W. (Ed), The Paramyxoviruses, Plenum Press, New York, 1991, pp. 41-72.
  15. Garcia-Sastre A., Cabezas J.A., Villar E., Proteins of Newcastle disease virus envelope: interaction between the outer hemagglutinin-neuraminidase glycoprotein and the inner non-glycosylated matrix protein, Biochem. Biophys. Acta 999 (1989) 171-175.
  16. Gibbons R.A., Physio-chemical methods for the determination of the purity, molecular size and shape of glycoproteins, in: Gottschalk A. (Ed.), Glycoproteins. Their Composition, Structure and Function, Elsevier Publ. Comp., Amsterdam, 1972, pp. 31-140.
  17. Graham E.R.B., Fetuin, in: Gottschalk A. (Ed.), Glycoproteins. Their Composition, Structure and Function, Elsevier Publ. Comp., Amsterdam, 1972, pp. 717-729.
  18. Granoff A., Henle W., A small hemagglutinating component in preparations of Newcastle disease virus, J. Immunol. 72 (1954) 329-339 [PubMed].
  19. Graves I.L., Incorporation of radioactivity from 14C-sugars into macromolecule in polio-infected or guanidine-treated HeLa cells, J. Gen. Virol. 4 (1969) 101-109 [PubMed].
  20. Graves I.L., Utilization of radioactive carbon from glucose in biosynthesis of deoxyribonucleic acid, ribonucleic acid, polyglucose, and protein in vaccinia virus-infected HeLA cells, Am. J. Vet. Res. 30 (1969) 647-653 [PubMed].
  21. Graves I.L., Concerning the extraction, separation, and labeling with 14C-glucose of HeLa cell polyglucose, RNA and DNA and a comparison of the molecular weights and buoyant densities of polyglucose from poliovirus-infected and noninfected cultures, Biopolymers 9 (1970) 11-28 [PubMed].
  22. Graves I.L., Elution-inhibition antibody to Newcastle disease virus isolated from wild birds, Microbiology meetings, American Society of Microbiology, Washington, DC (abstract 5-196), May 4-9,1979, p. 272.
  23. Graves I.L., Influenza viruses in birds of the Atlantic flyway, Avian Dis. 36 (1992) 1-10 [CrossRef] [PubMed].
  24. Graves I.L., The neuraminidase of Newcastle disease virus inhibited in the elution-inhibition reaction, Vet. Res. 27 (1996) 45-54 [PubMed].
  25. Graves I.L., Newcastle disease virus in birds of the Atlantic flyway: isolations, hemagglutination-inhibition and elution-inhibition antibody profiles, Vet. Res. 27 (1996) 209-218 [PubMed].
  26. Graves I.L., Heat inactivation of the neuraminidase and haemagglutinin estimated in the agglutination-separation reactions using red blood cells sensitized with Newcastle disease virus, Vet. Res. 30 (1999) 383-392 [PubMed].
  27. Haywood A.M., Virus receptors: binding, adhesion strengthening, and changes in viral structure, J. Virol. 68 (1994) 1-5 [PubMed].
  28. Herrier G., Reuter G., Rott R., Klenk H.D., Schauer, R., N-acetyl-9-O-acetylneuraminic acid, the receptor determinant for influenza C virus, is a differentiation marker on chicken erythrocytes, Biol. Chem. Hoppe- Seyler 368 (1987) 451-454 [PubMed].
  29. Karzon D.T., Bang F.B., The pathogenesis of infection with a virulent (CG 179) and an avirulent (B) strain of Newcastle disease virus in the chicken. I. Comparative rates of viral multiplication. II. Development of antibody. J. Exp. Med. 93 (1951) 267-296.
  30. Lamb R.A., Kolakofsky D., The Paramyxoviruses, in: Field B.N., Knipe D.M., Howley P.M. (Eds.), Fundamental virology 3rd Ed., Lippincott Raven, Philadelphia, Pa. 1996, pp. 577-604.
  31. Langedijk J.P.M., Daus F.J., van Oirschot J.T., Sequence and structure alignment of paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin, J. Virol. 71 (1997) 6155-6167 [PubMed].
  32. Leeuw O., Peeters B., Complete nucleotide sequence of Newcastle disease virus: evidence for the existence of a new genus within the subfamily Paramyxovirinae, J. Gen. Virol. 80 (1999) 131-136 [PubMed].
  33. Markwell M. A.K., New frontiers opened by the exploration of host cell receptors, in: Kingsbury D.W. (Ed.), The Paramyxoviruses, Plenum Press, New York, 1991, pp. 407-422.
  34. McGinnes L.W., Sergel T., Morrison T.G., Mutations in the transmembrane domain of the HN protein of Newcastle disease virus affect the structure and activity of the protein, Virology 196 (1993) 101-110 [CrossRef] [PubMed].
  35. Mirza A.M., Sheehan J.P., Hardy L.W., Glickman R.L., Iorio R.M., Structure and function of a membrane anchor-less form of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus, J. Biol. Chem. 268 (1993) 21425-21431 [PubMed].
  36. Morrison T.G., Portner A., Structure, function, and intracellular processing of the glycoproteins of paramyxoviridae. in: Kingsbury D.W. (Ed.), The Paramyxoviruses, Plenum Press, New York, 1991, pp. 347-382.
  37. Munoz-Barroso I., Cobaleda C., Zhadan G., Shnyrov V., Villar E., Dynamic properties of Newcastle disease virus envelope and their relations with viral hemagglutinin-neuraminidase membrane glycoprotein, Biochem. Biophys. Acta 1327 (1997) 17-31.
  38. Neitchev V.Z., Dumanova L.P., Effects of the components of Newcastle disease virus on the structural order of lipid assemblies, Mol. Biol. Rep. 16 (1992) 27-31 [CrossRef] [PubMed].
  39. Peeples M.E., Paramyxovirus M proteins: pulling it all together and taking it on the road, in: Kingsbury D. W. (Ed.) The Paramyxoviruses, Plenum Press, New York, 1991, pp. 427-456.
  40. Powell J.A., Kato K., Milgrom F., Antibodies to Newcastle disease virus in various human diseases, Int. Arch. Allergy Appl Immunol. 76 (1985) 331-335 [PubMed].
  41. Reuter G., Schauer R., Determination of sialic acids, in: Lennarz W., Hart G.W. (Eds.), Methods in Enzymology, Academic Press, San Diego, 230, 1994, pp. 168-199.
  42. Rott R., Antigenicity of Newcastle disease virus, in: Hanson R.P. (Ed.), Newcastle Disease Virus An Evolving Pathogen, University of Wisconsin Press, Madison and Milwaukee 1964, pp. 133-146.
  43. Sakaguchi T., Toyoda T., Gotch B., Inocencio N.M., Kuma K., Nagai Y., Newcastle disease virus evolution: multiple lineages defined by sequence variability of the haemagglutinin-neuraminidase gene, Virology 169 (1989) 260-272 [CrossRef] [PubMed].
  44. Schauer R., Sialic acids and their role as biological masks, Trends Biochem. Sci. 10 (1985) 357-360 [CrossRef].
  45. Seal B., King D., Bennett J., Characterization of Newcastle disease virus vaccines by biological properties and sequence analysis of the hemagglutinin-neuraminidase protein gene, Vaccine 14 (1996) 761-766 [CrossRef] [PubMed].
  46. Sheehan J.P., Iorio R.M., A single amino acid substitution in the hemagglutinin-neuraminidase of Newcastle disease virus results in a protein deficient in both functions, Virology 189 (1992) 778-781 [CrossRef] [PubMed].
  47. Siebert H.C., Tajkhorshid E., von der Lieth C.W., Kleineidam S.K., Schauer R., Kaptein R., Gabius H.J., Vliegenthart J.F.G., Knowledge-based homology modeling and experimental determination of amino acid side chain accessibility by the laser photo CINDP (chemically induced dynamic nuclear polarization) approach in solution: Lessons from the small sialidase of Clostridium perfringens, J. Mol. Model. 2 (1996) 446-455 [CrossRef].
  48. Takimoto T., Taylor G.L., Crennell S.J., Scroggs R.A., Portner A., Crystallization of Newcastle disease virus hemagglutinin-neuraminidase glycoprotein, Virology 270 (2000) 208-214 [CrossRef] [PubMed].
  49. Traving C., Schauer R., Structure, function and metabolism of sialic acids, Cell Mol. Life Sci. 54 (1998) 1330-1340 [CrossRef] [PubMed].
  50. Varghese J.N., Coleman P.M., van Donkelaar, A., Blick, T.J., Sahasrabudhe A., McKimm-Breschkin J.L., Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases, Proc. Natl. Acad. Sci. USA, 94 (1997) 11808-11812.
  51. Wang Z., Iorio R.M., Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain, J. Gen. Virol. 80 (1999) 749-753 [PubMed].
  52. Weiss R.A., Brown J.H., Cusack S., Paulson J.C, Skehel J.J., Wiley D.C., Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid, Nature (London) 333 (1988) 426-431 [CrossRef].
  53. Wilson C., Gilmore R., Morrison T., Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus, Mol. Cell. Biol. 10 (1990) 449-457 [PubMed].