Accessibility of peptides displayed on filamentous bacteriophage virions: Susceptibility to proteinases

Biological Chemistry

Volumn 378, Issue 6, 1997, Pages 523-530

  Terry, Tamsin D ^a   Malik, Pratap ^a   Perham, Richard N ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Epitopes; Gene manipulation; Immunogenicity; Peptide libraries; Phage display; Vaccines

Indexed keywords

CHYMOTRYPSIN; PEPTIDE; PROTEINASE; TRYPSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE; CARBOXY TERMINAL SEQUENCE; IMMUNOGENICITY; MOLECULAR INTERACTION; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; VIRION;

ENTEROBACTERIA PHAGE FD; FILAMENTOUS BACTERIOPHAGE; MIRIDAE; UNIDENTIFIED BACTERIOPHAGE;

EID: 0030876036     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.6.523     Document Type: Article

References (38)

1. Armstrong, J., Perham, R.N., and Walker, J.E. (1981). Domain structure of bacteriophage fd adsorption protein. FEBS Lett. 135, 167-172.
2. Armstrong, J., Hewitt, J.A., and Perham, R.N. (1983). Chemical modification of the coat protein in bacteriophage fd and orientation of the virion during assembly and disassembly. EMBO J. 2, 1641-1646.
3. Ausubel, P.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. (1995). Current Protocols in Molecular Biology. (New York: John Wiley and Sons Inc.).
4. Cesareni, G. (1992). Peptide display on filamentous bacteriophage capsids. A new powerful tool to study protein-ligand interactions. FEBS Lett. 307, 66-70.
5. Cortese, R., Felici, F., Galfre, G., Luzzago, A., Monaci, P., and Nicosia, A. (1994). Epitope discovery using peptide libraries displayed on bacteriophage. Trends Biotech. 12, 262-267.
6. Felici, F., Castagnoli, L., Musacchio, A., Jappelli, R., and Cesareni, G. (1991). Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector. J. Mol. Biol. 222, 301-310.
7. Fontana, A., Vita, C., Dalzoppo, D., and Zambonin, M. (1989). Limited proteolysis as a tool to detect structure and dynamic features of globular proteins: studies on thermolysin. In: Methods in Protein Sequence Analysis, B. Wittmann-Liebold, ed. (Berlin: Springer-Verlag), pp. 315-325.
8. Greenwood, J., Willis, A.E., and Perham, R.N. (1991 ). Multiple display of foreign peptides on a filamentous bacteriophage. J. Mol. Biol. 220, 821-827.
9. Hart, S.L., Knight, A.M., Harbottle, R.P., Mistry, A., Hunger, H.-D., Cutler, D.F., Williamson, R., and Coutelle, C. (1994). Cell binding and internalization by filamentous bacteriophage displaying a cyclic Arg-Gly-Asp containing peptide. J. Biol. Chem. 269, 12468-12474.
10. Hoess, R.H. (1993). Bacteriophage display of peptides and protein domains. Curr. Opin, Struct. Biol. 3, 572-579.
11. Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K., and Pease, L.R. (1989). Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77, 61-68.
12. Hubbard, S.J., Campbell, S.F., and Thornton, J.M. (1991). Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. J. Mol. Biol. 220, 507-530.
13. Hubbard, S.J., Eisenmenger, F., and Thornton, J.M. (1994). Modelling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Science 3, 757-768.
14. Iannolo, G., Minenkova, O.O., Petruzzelli, R., and Cesarini, G. (1995). Modifying filamentous bacteriophage capsid: limits in the size of the major capsid protein. J. Mol. Biol. 248, 835-844.
15. Il'ichev, A.A., Minenkova, O.O., Tat'kov, S.I., Karpyshev, N.N., Eroshkin, A.M., Petrenko, V.A., and Sandakhchiev, L.S. (1989). Production of a viable variant of bacteriophage M13 with incorporated foreign peptide in the major envelope protein. Doklady Akademii Nauk. S.S.S.R. 307, 481-483.
16. Jelinek, R., Terry, T.D., Gesell, J.J., Malik, P., Perham, R.N., and Opella, S.J. (1997). NMR structure determination of the principal neutralizing determinant of HIV-1 displayed on filamentous bacteriophage coat protein. J. Mol. Biol. 266, 649-655.
17. Kang, A.S., Barbas, C.F., Janda, K.D., Benkovic, S.J., and Lerner, R.A. (1991). Linkage recognition and replication functions by assembling combinatorial antibody Fab libraries along bacteriophage surfaces. Proc. Natl. Acad. Sci. USA 88, 4363-4366.
18. Kay, B.K., Winter, J., and McCafferty, J. (eds.) (1996). Phage Display of Peptides and Proteins (San Diego: Academic Press).
19. Kishchenko, G., Batliwala, H., and Makowski, L. (1994). Structure of a foreign peptide displayed on the surface of bacteriophage M13. J. Mol. Biol. 241, 208-213.
20. Malik, P., Terry, T.D., Gowda, L.R., Langara, A., Petukhov, S.A., Symmons, M.F., Welsh, L.C., Marvin, D.A., and Perham, R.N. (1996). Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage. J. Mol. Biol. 260, 9-21.
21. Malik, P., and Perham, R.N. (1996). New vectors for peptide display on the surface of filamentous bacteriophage. Gene 171, 49-51.
22. Marvin, D.A., Hale, R.D., Nave, C., and Helmer Citterich, M. (1994). Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages. J. Mol. Biol. 235, 260-286.
23. Matthews, D.J., and Wells, J.A. (1993). Substrate phage: selection of protease substrates by monovalent phage display. Science 260, 1113-1117.
24. Minenkova, O.O., Il'ichev, A.A., Kishchenko, G.P., and Petrenko, V.A. (1993). Design of specific immunogens using filamentous bacteriophage as the carrier. Gene 128, 85-88.
25. Model, P., and Russel, M. (1988). Filamentous bacteriophage. In: The Bacteriophages, Vol. 2, R. Calendar, ed. (New York: Plenum Press), pp. 375-456.
26. Novotny, J., and Bruccoleri, R.E. (1987). Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility. FEBS Lett. 211, 185-189.
27. Price, N.C., and Johnson, C.M. (1989). Proteinases as probes of conformation of soluble proteins. In: Proteolytic Enzymes: A Practical Approach, R.J. Beynon and J.S. Bond, eds. (Oxford: Oxford University Press), pp. 163-180.
28. Rasched, I., and Oberer, E. (1986). Ff coliphages: structural and functional relationships. Microbiol. Rev. 50, 401-427.
29. Rossomondo, E.F., and Zinder, N.D. (1968). Studies on the bacteriophage fl. I. Alkali-induced disassembly of the bacteriophage into DNA and protein. J. Mol. Biol. 36, 387-399.
30. Russel, M. (1991). Filamentous bacteriophage assembly. Mol. Microbiol. 5, 1607-1613.
31. Schwind, P., Kramer, H., Kremser, A., Ramsberger, U., and Rasched, I. (1992). Subtilisin removes the surface layer of the bacteriophage fd coat. Eur. J. Biochem. 210, 431-436.
32. Scott, J.K. Discovering peptide ligands using epitope libraries. (1992). Trends Biochem. Sci. 17, 241-245.
33. Smith, G.P., and Scott, J.K. (1993). Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol. 217, 228-257.
34. Symmons, M.F., Welsh, L.C., Nave, C., Marvin, D.A., and Perham, R.N. (1995). Matching electrostatic charge between DNA and coat protein in filamentous bacteriophage. Fibre diffraction of charge-deletion mutants. J. Mol. Biol. 245, 86-91.
35. Veronese, F. di M., Willis, A.E., Boyer-Thompson, C., Appella, E., and Perham, R.N. (1994). Structural mimicry and enhanced immunogenicity of peptide epitopes displayed on filamentous bacteriophage. The V3 loop of HIV-1 gp120. J. Mol. Biol. 243, 167-172.
36. Vorm, O., Roepstorff, P., and Mann, M. (1994). Improved resolution and very high sensitivity in MALDI TOF of matrix surfaces made by fast evaporation. Anal. Chem. 66, 3281-3287.
37. Willis, A.E., Perham, R.N., and Wraith, D. (1993). Immunological properties of foreign peptides in multiple display on a filamentous bacteriophage. Gene 128, 79-83.
38. Winter, G., Griffiths, A.D., Hawkins, R.E., and Hoogenboom, H.R. (1994). Making antibodies by phage display technology. Ann. Rev. Immunol. 12, 433-455.