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. 2002 Nov 11;49(2):209–219. doi: 10.1016/0166-0934(94)90045-0

Strategies for mapping and imitating viral B-cell epitopes

John Cason 1,∗
PMCID: PMC7173103  PMID: 7529771

Abstract

Identification of viral B-cell epitopes is of importance in the selection of peptides for inclusion into subunit vaccines, the development of virus-specific serological tests and understanding the interaction of antibodies with viruses at a molecular level. B-cell epitopes can often be determined unequivocally by X-ray analyses of antibody-antigen complexes. This technique is, however, time-consuming and alternative strategies have now been developed for identifying epitopes. This article provides an overview of approaches which are currently available for mapping and imitating B-cell epitopes.

Keywords: Virus, Epitope mapping, Antibody

References

  1. Al Moudallal Z., Briand J.P., Van Regenmortel M.H.V. Monoclonal antibodies as probes of the antigenic structure of tobacco mosaic virus. EMBO J. 1982;1:1005–1010. doi: 10.1002/j.1460-2075.1982.tb01285.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alter H.J., Purcell R.H., Shih J.W., Melpolder J.C., Houghton M., Choo Q.-L., Kuo G. Detection of antibodies to hepatitis C virus in prospectively followed transfusion recipients with acute and chronic non-A non-B hepatitis. N. Engl. J. Med. 1989;321:1494–1500. doi: 10.1056/NEJM198911303212202. [DOI] [PubMed] [Google Scholar]
  3. Basgoz N., Qudri I., Navarro D., Sears A., Lennette E., Youngblom J., Pereira L. The amino terminus of human cytomegalovirus glycoprotein B contains epitopes that vary among strains. J. Gen. Virol. 1992;73:983–988. doi: 10.1099/0022-1317-73-4-983. [DOI] [PubMed] [Google Scholar]
  4. Bentley G., Roittot M.M., Poljak R.J. Three dimensional structure of an idiotope/anti-idiotope complex. Nature. 1990;348:254–257. doi: 10.1038/348254a0. [DOI] [PubMed] [Google Scholar]
  5. Boehringer . 1991. Boehringer Mannheim catalogue; p. 232. [Google Scholar]
  6. Carter J.J., Yaegashi N., Jenison S.A. Expression of human papillomavirus proteins in yeast Saccharomyces cerevisiae. Virology. 1991;182:513–521. doi: 10.1016/0042-6822(91)90592-y. [DOI] [PubMed] [Google Scholar]
  7. Cason J., Kambo P.K., Jewers R.J., Chrystie I.L., Best J.M. Mapping of linear B-cell epitopes on capsid proteins of bovine papillomavirus: identification of three external type-restricted epitopes. J. Gen. Virol. 1993;74:2669–2677. doi: 10.1099/0022-1317-74-12-2669. [DOI] [PubMed] [Google Scholar]
  8. Cason J., Patel D., Naylor J., Lunney D., Shepherd P.S., Best J.N., McCance D.J. Identification of immunogenic regions of the major coat protein of human papillomavirus type 16 that contain type-restricted epitopes. J. Gen. Virol. 1989;70:2973–2987. doi: 10.1099/0022-1317-70-11-2973. [DOI] [PubMed] [Google Scholar]
  9. Choo Q.-L., Kuo G., Weimer A.J., Overby L.R., Bradley D.W., Houghton M. Isolation of a cDNA clone derived from a blood borne non-A non-B viral hepatitis genome. Science. 1989;244:359–362. doi: 10.1126/science.2523562. [DOI] [PubMed] [Google Scholar]
  10. Cwirla S.E., Peters E.A., Barrett R.W., Dower W.J. Vol. 87. 1990. Peptides on phage, a vast library of peptides for identifying ligands; pp. 6378–6382. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Doel T.R., Gale C., Brooke G., DiMarchi R. Immunization against foot-and-mouth disease virus with synthetic peptides representing the C-terminal region of VP1. J. Gen. Virol. 1988;69:2403–2406. doi: 10.1099/0022-1317-69-9-2403. [DOI] [PubMed] [Google Scholar]
  12. Drapeau G.R., Boily Y., Houmard J. Purification and properties of an extracellular protease of Staphlococcus aureus. J. Biol. Chem. 1972;247:6720–6726. [PubMed] [Google Scholar]
  13. Geysen M.S., Rodda T., Mason T.J. A priori delineation of a peptide which mimics a discontinuous antigenic determinant. Mol. Immunol. 1986;23:709–715. doi: 10.1016/0161-5890(86)90081-7. [DOI] [PubMed] [Google Scholar]
  14. Geysen M.S., Rodda T., Mason G., Triubbick G., Schoofs P. Strategies for epitope analysis using synthetic peptide synthesis. J. Immunol. Methods. 1987;102:259–265. doi: 10.1016/0022-1759(87)90085-8. [DOI] [PubMed] [Google Scholar]
  15. Harper M., Lema F., Boulot G., Poljak R.J. Antigen specificity and cross reactivity of monoclonal antilysozyme antibodies. Mol. Immunol. 1987;24:97–108. doi: 10.1016/0161-5890(87)90081-2. [DOI] [PubMed] [Google Scholar]
  16. Houghten R.A., Pinilla C., Blondelle S.E., Appel J.R., Dooley C.T., Cuervo J.H. Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature. 1991;354:84–86. doi: 10.1038/354084a0. [DOI] [PubMed] [Google Scholar]
  17. Kant A., Koch G., Van Roozelaar D.J., Küsters J.G., Poelwijk F.A.J., Van der Zeijst B.A.M. Localization of antigenic sites defined by neutralizing monoclonal antibodies on the S1 avian infectious bronchitis virus glycopeptide. J. Gen. Virol. 1992;73:591–596. doi: 10.1099/0022-1317-73-3-591. [DOI] [PubMed] [Google Scholar]
  18. Kirnbauer R., Booy Y., Cheng N. Vol. 89. 1992. Papillomavirus L1 major capsid protein self assembles into virus like particles that are highly immunogenic; pp. 12180–12184. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Kohli E., Maurice L., Vauthernot J.F., Bourgeois C., Bour J.B., Cohen J., Pathier P. Localization of group specific antigens on the major capsid protein of group A rotavirus. J. Gen. Virol. 1992;73:907–914. doi: 10.1099/0022-1317-73-4-907. [DOI] [PubMed] [Google Scholar]
  20. Lam K.S., Salmon S.E., Hersh E.M., Hruby V.J., Kazmierski W.M., Knapp R.J. A new type of synthetic peptide library for identifying ligand-binding activity. Nature. 1991;354:82–84. doi: 10.1038/354082a0. [DOI] [PubMed] [Google Scholar]
  21. Langedijk J.P.M., Back N.K.T., Durden P.J., Goudsmit P.J., Meloen R.H. Neutralizing activity of antipeptide antibodies against the principle neutralization domain of human immunodeficiency virus type 1. J. Gen. Virol. 1991;72:2519–2526. doi: 10.1099/0022-1317-72-10-2519. [DOI] [PubMed] [Google Scholar]
  22. Laver W.G., Air G.M., Webster R.G., Smith-Gill S.J. Epitopes on protein antigens: misconceptions and realities. Cell. 1990;61:553–556. doi: 10.1016/0092-8674(90)90464-p. [DOI] [PubMed] [Google Scholar]
  23. Lehninger A.L. Worth; New York: 1976. p. 106. (Biochemistry). [Google Scholar]
  24. Luytjes W., Geerts D., Posthumus W., Meloen R., Spaan W. Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses. J. Virol. 1989;63:1408–1412. doi: 10.1128/jvi.63.3.1408-1412.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Makela O. Single lymph node cells producing heteroclitic bacteriophage antibody. J. Immunol. 1965;95:378–386. [PubMed] [Google Scholar]
  26. Meloen R.H., Puyk W.C., Meijer D.J.A., Lankof H., Posthumus W.P.A., Schaaper W.M.M. Antigenicity and immunogenicity of synthetic peptides of foot-and-mouth disease virus. J. Gen. Virol. 1987;68:305–314. doi: 10.1099/0022-1317-68-2-305. [DOI] [PubMed] [Google Scholar]
  27. Minor P.D., Ferguson M., Evans D.M.A., Almond J.W., Icenogle J.P. Antigenic structure of polioviruses of serotypes 1,2 and 3. J. Gen. Virol. 1986;67:1283–1291. doi: 10.1099/0022-1317-67-7-1283. [DOI] [PubMed] [Google Scholar]
  28. Minor P.D., Evans D.M.A., Ferguson M., Schild G.C., Westrop G., Almond J.W. Principal and subsidiary antigenic sites of VP1 involved in the neutralization of poliovirus type 3. J. Gen. Virol. 1985;65:1159–1165. doi: 10.1099/0022-1317-66-5-1159. [DOI] [PubMed] [Google Scholar]
  29. Muller S., Plaue S., Samama J.P., Valette M., Briand J.P., Van Regenmortel M.H.V. Antigenic properties and protective capacity of a cyclic peptide corresponding to site A of influenza virus haeagglutinin. Vaccine. 1990;8:308–314. doi: 10.1016/0264-410x(90)90086-2. [DOI] [PubMed] [Google Scholar]
  30. Parry N., Fox G., Rowlands D., Brown F., Fry E., Acharya R., Logan D., Stuart D. Structural and serological evidence of a novel mechanism of antigenic variation in foot-and-mouth disease virus. Nature. 1990;347:569–572. doi: 10.1038/347569a0. [DOI] [PubMed] [Google Scholar]
  31. Papsidero L.D., Sheu M., Ruscetti F.W. Human immunodeficiency virus type-1 neutralizing monoclonal antibodies which react with p-17 core protein: characterization and epitope mapping. J. Virol. 1989;63:267–272. doi: 10.1128/jvi.63.1.267-272.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Parmley S.F., Smith G.P. Antibody-selectable filamentous fd phage vectors: affinity purification of target genes. Gene. 1988;73:305–318. doi: 10.1016/0378-1119(88)90495-7. [DOI] [PubMed] [Google Scholar]
  33. Prasad B.V.V., Burns J.W., Marietta E., Estes M.K., Chiu W. Localization of vp4 neuytraliza-tion in rotavirus by three dimensional cryo-electron microscopy. Nature. 1990;354:476–479. doi: 10.1038/343476a0. [DOI] [PubMed] [Google Scholar]
  34. Rao K.V.S., Panda S.K., Manivel V. Macromolecular self-association of a synthetic peptide derived from hepatitis B surface antigen: construction of a quaternary epitope. Vaccine. 1992;10:204–208. doi: 10.1016/0264-410x(92)90152-a. [DOI] [PubMed] [Google Scholar]
  35. Roitt I., Brostoff J., Male D. The generation of antibody diversity. Churchill-Livingstone; London: 1985. Immunology; p. 9.2. [Google Scholar]
  36. Scott J.K., Smith G.P. Searching for peptide ligands with an epitope library. Science. 1990;249:386–390. doi: 10.1126/science.1696028. [DOI] [PubMed] [Google Scholar]
  37. Sherry B., Mosser A.G., Colonno R.J., Rureckert R.R. Use of monoclonal antibodies to identify four neutralization immunogens on a common cold picornavirus, human rhinovirus 14. J. Virol. 1986;57:246–257. doi: 10.1128/jvi.57.1.246-257.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Skern T., Neubauer C., Frasel L., Grundler P., Sommergrubber W., Zorn M., Kuechler E., Blaas D. A neutralizing epitope on human rhinovirus type 2 includes amino acid residues between 153 and 164 of virus capsid protein VP2. J. Gen. Virol. 1987;68:315–323. doi: 10.1099/0022-1317-68-2-315. [DOI] [PubMed] [Google Scholar]
  39. Smith G.P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 1985;228:1315–1317. doi: 10.1126/science.4001944. [DOI] [PubMed] [Google Scholar]
  40. Van Regenmortel M.H.V. Structural and functional approaches to the study of protein antigenicity. Immunol. Today. 1989;8:266–272. doi: 10.1016/0167-5699(89)90140-0. [DOI] [PubMed] [Google Scholar]
  41. Xie Q.-C., McCahon D., Crowther J.R., Belsham G.J., McCullough K.C. Neutralization of foot-and-mouth disease virus can be mediated through any of at least three separate antigenic sites. J. Gen. Virol. 1987;68:1637–1647. doi: 10.1099/0022-1317-68-6-1637. [DOI] [PubMed] [Google Scholar]

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