Abstract
Peptide antibodies recognize epitopes with amino acid residues adjacent in sequence (“linear” epitopes). Such antibodies can be made to virtually any sequence and have been immensely important in all areas of molecular biology and diagnostics due to their versatility and to the rapid growth in protein sequence information. Today, peptide antibodies can be routinely and rapidly made to large numbers of peptides, including peptides with posttranslationally modified residues, and are used for immunoblotting, immunocytochemistry, immunohistochemistry, and immunoassays. In the future, peptide antibodies will continue to be immensely important for molecular biology, TCR- and MHC-like peptide antibodies may be produced routinely, peptide antibodies with predetermined conformational specificities may be designed, and peptide-based vaccines may become part of vaccination programs.
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References
Sela M, Schechter B, Schechter I, Borek F (1967) Antibodies to sequential and conformational determinants. Cold Spring Harbor Symp Quant Biol 32:537–545
Amit AG, Mariuzza RA, Phillips SE, Poljak RJ (1986) Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science 233:747–753
Colman PM, Laver WG, Varghese JN, Baker AT, Tulloch PA, Air GM, Webster RG (1987) Three-dimensional structure of a complex of antibody with influenza virus neuraminidase. Nature 326:358–363
Sheriff S, Silverton EW, Padlan EA, Cohen GH, Smith-Gill SJ, Finzel BC, Davies DR (1987) Three-dimensional structure of an antibody-antigen complex. Proc Natl Acad Sci U S A 84:8075–8079
Mariuzza RA, Phillips SE, Poljak RJ (1987) The structural basis of antigen-antibody recognition. Annu Rev Biophys Biophys Chem 16:139–159
Colman PM, Tulip WR, Varghese JN, Tulloch PA, Baker AT, Laver WG, Air GM, Webster RG (1989) Three-dimensional structures of influenza virus neuraminidase-antibody complexes. Philos Trans R Soc Lond B Biol Sci 323:511–518
Scherf T, Hiller R, Naider F, Levitt M, Anglister J (1992) Induced peptide conformations in different antibody complexes: molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints. Biochemistry 31:6884–6897
Sutcliffe JG, Shinnick TM, Green N, Liu FT, Niman HL, Lerner RA (1980) Chemical synthesis of a polypeptide predicted from nucleotide sequence allows detection of a new retroviral gene product. Nature 287:801–805
Walter G, Scheidtmann KH, Carbone A, Laudano AP, Doolittle RF (1980) Antibodies specific for the carboxy- and amino-terminal regions of simian virus 40 large tumor antigen. Proc Natl Acad Sci U S A 77:5197–5200
Lerner RA, Green N, Alexander H, Liu FT, Sutcliffe JG, Shinnick TM (1981) Chemically synthesized peptides predicted from the nucleotide sequence of the hepatitis B virus genome elicit antibodies reactive with the native envelope protein of Dane particles. Proc Natl Acad Sci U S A 78:3403–3407
Bittle JL, Houghten RA, Alexander H, Shinnick TM, Sutcliffe JG, Lerner RA, Rowlands DJ, Brown F (1982) Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature 298:30–33
Pfaff E, Mussgay M, Böhm HO, Schulz GE, Schaller H (1982) Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus. EMBO J 1:869–874
Posnett DN, McGrath H, Tam JP (1988) A novel method for producing anti-peptide antibodies. Production of site-specific antibodies to the T cell antigen receptor beta-chain. J Biol Chem 263:1719–1725
Tam JP (1988) Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system. Proc Natl Acad Sci U S A 85:5409–5413
Hansen PR, Holm A, Houen G (1993) Solid-phase peptide synthesis on proteins. Int J Pept Protein Res 41:237–245
Li GX, Zhou YJ, Yu H, Li L, Wang YX, Tong W, Hou JW, Xu YZ, Zhu JP, Xu AT, Tong GZ (2012) A novel dendrimeric peptide induces high level neutralizing antibodies against classical swine fever virus in rabbits. Vet Microbiol 156:200–204
Petrasovits LA (2014) Protein blotting protocol for beginners. Methods Mol Biol 1099:189–199
Kurien BT, Dorri Y, Dillon S, Dsouza A, Scofield RH (2011) An overview of Western blotting for determining antibody specificities for immunohistochemistry. Methods Mol Biol 717:55–67
Wheeler MJ (2013) Immunoassay techniques. Methods Mol Biol 1065:7–25
Wild D (ed) (2013) The immunoassay handbook. Elsevier, Oxford
Brooks SA (2012) Basic immunocytochemistry for light microscopy. Methods Mol Biol 878:1–30
Ramos-Vara JA (2011) Principles and methods of immunohistochemistry. Methods Mol Biol 691:83–96
Davies D (2012) Cell separations by flow cytometry. Methods Mol Biol 878:185–199
Givan AL (2011) Flow cytometry: an introduction. Methods Mol Biol 699:1–29
Isono E, Schwechheimer C (2010) Co-immunoprecipitation and protein blots. Methods Mol Biol 655:377–387
Uljon SN, Mazzarelli L, Chait BT, Wang R (2000) Analysis of proteins and peptides directly from biological fluids by immunoprecipitation/mass spectrometry. Methods Mol Biol 146:439–452
Dahan R, Reiter Y (2012) T-cell-receptor-like antibodies—generation, function and applications. Expert Rev Mol Med. doi:10.1017/erm.2012.2
Neumann F, Sturm C, Hülsmeyer M, Dauth N, Guillaume P, Luescher IF, Pfreundschuh M, Held G (2009) Fab antibodies capable of blocking T cells by competitive binding have the identical specificity but a higher affinity to the MHC-peptide-complex than the T cell receptor. Immunol Lett 125:86–92
Naz RK, Dabir P (2007) Peptide vaccines against cancer, infectious diseases, and conception. Front Biosci 12:1833–1844
Yamada A, Sasada T, Noguchi M, Itoh K (2013) Next-generation peptide vaccines for advanced cancer. Cancer Sci 104:15–21
Paduch M, Koide A, Uysal S, Rizk SS, Koide S, Kossiakoff AA (2013) Generating conformation-specific synthetic antibodies to trap proteins in selected functional states. Methods 60:3–14
Lu SM, Hodges RS (2002) A de novo designed template for generating conformation-specific antibodies that recognize alpha-helices in proteins. J Biol Chem 277:23515–23524
Sutcliffe JG, Shinnick TM, Green N, Lerner RA (1983) Antibodies that react with predetermined sites on proteins. Science 219:660–666
Shinnick TM, Sutcliffe JG, Green N, Lerner RA (1983) Synthetic peptide immunogens as vaccines. Annu Rev Microbiol 37:425–446
Brown F (1988) Use of peptides for immunization against foot-and-mouth disease. Vaccine 6:180–182
Van Regenmortel MH (1993) Synthetic peptides versus natural antigens in immunoassays. Ann Biol Clin (Paris) 51:39–41
Van Regenmortel MH, Briand JP, Muller S, Plaue S (Eds) (1988) Synthetic polypeptides as antigens. Laboratory techniques in biochemistry and molecular biology vol 19. Elsevier: Amsterdam
Van Regenmortel MH (2001) Antigenicity and immunogenicity of synthetic peptides. Biologicals 29:209–213
Fournel S, Muller S (2003) Synthetic peptides in the diagnosis of systemic autoimmune diseases. Curr Protein Pept Sci 4:261–274
Papini AM (2009) The use of post-translationally modified peptides for detection of biomarkers of immune-mediated diseases. J Pept Sci 15:621–628
Merrifield RB (1963) Solid phase peptide synthesis. I The synthesis of a tetrapeptide. J Am Chem Soc 85:2149–2154
Merrifield RB (1969) Solid-phase peptide synthesis. Adv Enzymol Relat Areas Mol Biol 32:221–296
Atherton E, Sheppard RC (1989) Solid Phase peptide synthesis: a practical approach. IRL Press, Oxford, England. ISBN 0-19-963067-4
Braciale TJ, Morrison LA, Sweetser MT, Sambrook J, Gething MJ, Braciale VL (1987) Antigen presentation pathways to class I and class II MHC-restricted T lymphocytes. Immunol Rev 98:95–114
Parker DC (1993) T cell-dependent B cell activation. Annu Rev Immunol 11:331–360
Fairchild PJ (1998) Presentation of antigenic peptides by products of the major histocompatibility complex. J Pept Sci 4:182–194
Appella E, Padlan EA, Hunt DF (1995) Analysis of the structure of naturally processed peptides bound by class I and class II major histocompatibility complex molecules. EXS 73:105–119
Maffei A, Harris PE (1998) Peptides bound to major histocompatibility complex molecules. Peptides 19:179–198
Blaydes JP, Vojtesek B, Bloomberg GB, Hupp TR (2000) The development and use of phospho-specific antibodies to study protein phosphorylation. Methods Mol Biol 99:177–189
Miller DL, Potempska A, Wegiel J, Mehta PD (2011) High-affinity rabbit monoclonal antibodies specific for amyloid peptides amyloid-β40 and amyloid-β42. J Alzheimers Dis 23:293–305
Terpe K (2003) Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 60:523–533
Holm BE, Bergmann AC, Hansen PR, Koch C, Houen G, Trier NH (2014) Antibodies with specificity for native and denatured forms of ovalbumin differ in reactivity between enzyme-linked immunosorbent assays. APMIS. doi:10.1111/apm.12329
Soria-Guerra RE, Nieto-Gomez R, Govea-Alonso DO, Rosales-Mendoza S (2014) An overview of bioinformatics tools for epitope prediction: implications on vaccine development. J Biomed Inform S1532–0464(14):00233. doi:10.1016/j.jbi.2014.11.003
Ansari HR, Raghava GP (2013) In silico models for B-cell epitope recognition and signaling. Methods Mol Biol 993:129–138
Ponomarenko JV, van Regenmortel MHV (2009) B-cell epitope prediction. In: Bourne PE, Gu J (eds) Structural bioinformatics. Wiley, New York, NY, pp 849–879
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Houen, G. (2015). Peptide Antibodies: Past, Present, and Future. In: Houen, G. (eds) Peptide Antibodies. Methods in Molecular Biology, vol 1348. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2999-3_1
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DOI: https://doi.org/10.1007/978-1-4939-2999-3_1
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