Antigenicity of the Measles Virus Haemagglutinin Studied by Using Synthetic Peptides

References

1. Alexander S., Elder J. H. 1984; Carbohydrate dramatically influences immune reactivity of antisera to viral glycoprotein antigens. Science 226:1328–1330
   [Google Scholar]
2. Alkhatib G., Briedis D. I. 1986; The predicted primary structure of the measles virus hemagglutinin. Virology 150:479–490
   [Google Scholar]
3. Carter M. J., Willcocks M. M., Loffler S., Ter Meulen V. 1982; Relationships between monoclonal antibody-binding sites on the measles virus haemagglutinin. Journal of General Virology 63:113–120
   [Google Scholar]
4. Dyson H.J., Cross K. J., Houghten R.A., Wilson I.A., Wright P. E., Lerner R.A. 1985; The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn. Nature, London 318:480–483
   [Google Scholar]
5. Ferguson M., Reed S. E., Minor P. D. 1986; Reactivity of anti-peptide and anti-poliovirus type 3 monoclonal antibodies with synthetic peptides. Journal of General Virology 67:2527–2531
   [Google Scholar]
6. Fujinami R. S., Oldstone M. B. A. 1981; Failure to cleave measles virus fusion protein in lymphoid cells. Journal of Experimental Medicine 154:1489–1499
   [Google Scholar]
7. Gerald C., Buckland R., Barker R., Freeman G., Wild T. F. 1986; Measles virus haemagglutinin gene: cloning, complete nucleotide sequence analysis and expression in COS cells. Journal of General Virology 67:2695–2703
   [Google Scholar]
8. Giraudon P., Wild T. F. 1985; Correlation between epitopes on hemagglutinin of measles virus and biological activities: passive protection by monoclonal antibodies is related to their hemagglutination inhibiting activity. Virology 144:46–58
   [Google Scholar]
9. Green N., Alexander H., Olson A., Alexander S., Shinnick T.M., Sutcliffe J.G., Lerner R. A. 1982; Immunogenic structure of the influenza virus hemagglutinin. Cell 28:477–487
   [Google Scholar]
10. Guo D., Mant C. T., Taneja A. K., Parker J. M. R., Hodges R. S. 1986; Prediction of peptide retention times in reversed-phase HPLC: determination of retention coefficients of amino acid residues of model synthetic peptides. Journal of Chromatography 359:499–517
    [Google Scholar]
11. Janin J. 1979; Surface and inside volumes in globular proteins. Nature, London 277:491–492
    [Google Scholar]
12. Karplus P. A., Schulz G. E. 1985; Prediction of chain flexibility in proteins. Naturwissenschaften 72:212–215
    [Google Scholar]
13. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriphage T4. Nature, London 221:680–685
    [Google Scholar]
14. Lerner R. A. 1982; Tapping the immunological repertoire to produce antibodies of predetermined specificity. Nature, London 299:592–596
    [Google Scholar]
15. Lund G. A., Salmi A. A. 1981; Purification and characterization of measles virus haemagglutinin protein G. Journal of General Virology 56:185–193
    [Google Scholar]
16. Niman H.L., Houghten R.A., Walker L.E., Reisfeld R.A., Wilson I.A., Hogle J.M., Lerner R.A. 1983; Generation of protein-reactive antibodies by short peptides is an event of high frequency: implications for the structural basis of immune recognition. Proceedings of the National Academy of SciencesU.S.A. 804949–4953
    [Google Scholar]
17. Norrby E., Gollmar Y. 1972; Appearance and persistence of antibodies against different virus components after regular measles infections. Infection and Immunity 6:240–247
    [Google Scholar]
18. Norrby E., Mufson M. A., Alexander H., Houghten R. A., Lerner R. A. 1987; Site-directed serology with synthetic peptides representing the large glycoprotein G of respiratory syncytial virus. Proceedings of the National Academy of SciencesU.S.A. 846572–6576
    [Google Scholar]
19. Parker J. M. R., Hodges R. S. 1985; I. Photoaffinity probes provide a general method to prepare synthetic peptide-conjugates. Journal of Protein Chemistry 3:465–478
    [Google Scholar]
20. Parker J. M. R., Guo D., Hodges R. S. 1986; New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X- ray-derived accessible sites. Biochemistry 25:5425–5432
    [Google Scholar]
21. Salmi A., Lund G. 1984; Immunoassays for measles virus nucleocapsid antigen: effect of antigen-antibody complexes. Journal of General Virology 65:1655–1663
    [Google Scholar]
22. Salonen R., Ilonen J., Salmi A. 1988; Measles virus infection of unstimulated blood mononuclear cells in vitro: antigen expression and virus production preferentially in monocytes. Clinical and Experimental Immunology 71:224–228
    [Google Scholar]
23. Sheshberadaran H., Norrby E. 1986; Characterization of epitopes on the measles virus hemagglutinin. Virology 151:1–9
    [Google Scholar]
24. Sheshberadaran H., Payne L. 1988; Protein antigen-monoclonal antibody contact sites investigated by limited proteolysis of monoclonal antibody-bound antigen: protein ‘footprinting’. Proceedings of the National Academy of SciencesU.S.A. 851–5
    [Google Scholar]
25. Strynadka N. C. J., Redmond M. J., Parker J. M. R., Scraba D.G., Hodges R.S. 1988; Use of Synthetic peptides to map the antigenic determinants of glycoprotein D of herpes simplex virus. Journal of Virology 62:3474–3483
    [Google Scholar]
26. Ter Meulen V., Carter M. I. 1984; Measles virus persistency and disease. Progress in Medical Virology 30:44–61
    [Google Scholar]
27. Ter Meulen V., Löffler S., Carter M. J., Stephenson J. R. 1981; Antigenic characterization of measles and SSPE virus haemagglutinin by monoclonal antibodies. Journal of General Virology 57:357–364
    [Google Scholar]
28. Vainionpää R., Ziola B., Salmi A. 1978; Measles virus polypeptides in purified virions and in infected cells. Ada pathologica et microbiologica scandinavica B86:379–385
    [Google Scholar]
29. Varsanyi T. M., Morein B., Löve A., Norrby E. 1987; Protection against lethal measles virus infection in mice by immune-stimulating complexes containing the hemagglutinin or fusion protein. Journal of Virology 61:3896–3901
    [Google Scholar]
30. Vartio T., Zardi L., Balza E., Towbin H., Vaheri A. 1982; Monoclonal antibodies in analysis of cathepsin G sdigested proteolytic fragments of human plasma fibronectin. Journal of Immunological Methods 55:309–318
    [Google Scholar]
31. Walter G. 1986; Production and use of antibodies against synthetic peptides. Journal of Immunological Methods 88:149–161
    [Google Scholar]
32. Wright P.E., Dyson H.J., Rance M., Ostresh J., Houghten R.A., Wilson I.A., Lerner R.A. 1986; Antipeptide antibodies and the disorder-order phenomenon. In Vaccines ’8615–19 Chanock R. M., Lerner R. A., Brown F. New York: Cold Spring Harbor Laboratory;
    [Google Scholar]