Abstract
Synthetic peptides offer several unique approaches to studying molecular and cellular interactions. Not only do these peptides provide A. large quantity of material for experimental analysis, but they also offer A. degree of homogeneity that is difficult to obtain through routine biochemical purification. Only during the last several years has the ability to use these peptides for dissecting biochemical interactions begun to be explored. For example, synthetic peptides are now being utilized frequently to generate antisera specific for sequenced genes. This approach has been successfully applied to detecting and characterizing viral and cellular proteins (Neumann et al., 1985; Walter et al., 1981; Walter and Doolittle, 1983) as well as to generate neutralizing antibodies in animals (Chow et al., 1985). In addition to serving as an antigenic stimulus, however, peptides may be used as A. biochemical probe to analyze molecular interactions, either as agonists or antagonists. The functional domain of epidermal growth factor involved in cell stimulation has been delineated by the methodical use of small peptides to mimic the effect of the intact molecule (Komoriya et al, 1984). Complex interactions such as cell binding to the substratum have been brought to A. more elementary level by realizing that the peptide Asp XX Gly serves as an apparent fibronectin attachment site (Pierschbacher and Ruoslahti, 1984).
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
Bailey, G., Miller, D., and Lenard, J., 1984, Effects of DEAE-dextran on infection and hemolysis by VSV. Evidence that non-specific electrostatic interactions mediate effective binding of VSV to cells, Virology 133:111–118.
Blumenthal, R., 1987, Membrane fusion, Curr. Top. Membrane Transport 29: (in press).
Chow, M., Yabrov, R., Bittle, J., Hogle, J., and Baltimore, D., 1985, Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VPI induce neutralizing antibodies, Proc. Natl Acad Sci. USA. 82:910–914.
Citovsky, V., and Loyter, A., 1985, Fusion of Sendai virions or reconstituted Sendai virus envelopes with liposomes or erythrocyte membranes lacking virus receptors, J. Biol. Chem. 260:12072–12077.
Crimmins, D. L., Mehard, W. B., and Schlesinger, S., 1983, Physical properties of A. soluble form of the glycoprotein of vesicular stomatitis virus at neutral and acidic pH, Biochemistry 22:5790–5796.
Eidelman, O., Schlegel, R., Tralka, T., and Blumenthal, R., 1984, pH-dependent fusion induced by vesicular stomatitis virus glycoprotein reconstituted into phospholipid vesicles, J. Biol. Chem. 259:4622–4628.
Florkiewicz, R., and Rose, J., 1984, A. cell line expressing vesicular stomatitis virus glycoprotein fuses at low pH, Science 225:721–723.
Gething, M.-J., White, J., and Waterfield, M., 1978, Purification of the fusion protein of Sendai virus: Analysis of the NH2-terminal sequence generated during precursor activation, Proc. Natl. Acad. Sci. USA. 75:2737–2740.
Hsu, M.-G., Scheid, A., and Choppin, P., 1983, Fusion of Sendai Virus with liposomes: Dependence on the viral fusion protein (F) and the lipid composition of liposomes, Virology 126:361–369.
Knutton, S., and Pasternak, G., 1979, The mechanism of cell-cell fusion, Trends Biochem. Sci. 4:220–223.
Komoriya, A., Hortsch, M., Meyers, G., Smith, M., Kanety, H., and Schlessinger, J., 1984, Biologically active synthetic fragments of epidermal growth factor: Localization of A. major receptor-binding region, Proc. Natl. Acad. Sci. USA. 81:1351–1355.
Neumann, D., Gershoni, J., Fridkin, M., and Fuchs, S., 1985, Antibodies to synthetic peptides as probes for the binding site on the a-subunit of the acetylcholine receptor, Proc. Natl. Acad. Sci. USA. 82:3490–3493.
Pierschbacher, M., and Ruoslahti, E., 1984, Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule, Nature (Lond.) 309:30–33.
Richardson, C., and Choppin, P., 1983, Oligopeptides that specifically inhibit membrane fusion by paramyxovirus: Studies on the site of action, Virology 131:518–532.
Richardson, C., Scheid, A., and Choppin, P., 1980, Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the F1or HA2viral polypeptides, Virology 105:205–222.
Riedel, H., Kondor-Koch, C., and Garoff, H., 1984, Cell surface expression of fusogenic vesicular Stomatitis virus G protein from cloned cDNA, EMBO J. 3:1477–1483.
Rose, J., and Gallione, C., 1981, Nucleotide sequences of mRNAs encoding the vesicular stomatitis G and M proteins determined from cDNA clones containing the complete coding regions, J. Virol. 39:519–528.
Scheid, A., and Choppin, P., 1974, Identification of biological activities of paramyxovirus glycoprotein: Activation of cell fusion, hemolysis, and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus, Virology 57:475–490.
Scheid, A., Graves, M., Silver, S., and Choppin, P., 1978, Studies on the structure and function of paramyxovirus glycoproteins. In Negative Strand Viruses and the Host Cell (Scheid, A., Graves, M., Silver, S., and Choppin, P., eds.), pp. 183–193, Academic Press, New York.
Schlegel, R., and Wade, M., 1985, Biologically active peptides of the vesicular stomatitis virus glycoprotein, J. Virol. 53:319–323.
Schlegel, R., Tralka, T., Willingham, M., and Pastan, I., 1983, Inhibition of VSV binding and infectivity by phosphatidylserine: is phosphatidylserine A. VSV-binding site? Cell 32: 639–646.
Skehel, J. J., Bayley, P. M., Brown, E. B., Martin, S. R., Waterfield, M. D., White, J. N., Wilson, I. A., and Wiley, D. C., 1982, Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion, Proc. Natl. Acad. Sci. USA. 79:968–972.
Stegmann, T., Hoekstra, D., Scherphof, G., and Wilshut, J., 1985, Kinetics of pH-dependent fusion between influenza virus and liposomes, Biochemistry 24:3107–3113.
Walter, G., and Doolittle, R., 1983, Antibodies against synthetic peptides, in: Genetic Engineering: Principles and Methods, Vol. 5 (J. Setlow and A. Hollsender, eds.), pp. 61–91, Plenum Press, New York.
Walter, G., Hutchinson, M., Hunter, T., and Eckhart, W., 1981, Antibodies specific for the polyoma virus middle-size tumor antigen, Proc. Natl. Acad. Sci. USA. 78:4882–4886.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1987 Springer Science+Business Media New York
About this chapter
Cite this chapter
Schlegel, R. (1987). Probing the Function of Viral Fusion Proteins with Synthetic Peptides. In: Sowers, A.E. (eds) Cell Fusion. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9598-1_2
Download citation
DOI: https://doi.org/10.1007/978-1-4757-9598-1_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-9600-1
Online ISBN: 978-1-4757-9598-1
eBook Packages: Springer Book Archive