28
Views
6
CrossRef citations to date
0
Altmetric
Original Article

Exploiting Molecular Mimicry: Defining Rules of the Game

, , &
Pages 157-180 | Published online: 10 Jul 2009

References

  • Mond J. J., Lees A., Snapper C. M. T cell-independent antigens type 2. [Review]. Annual Review of Immunology 1995; 13(655)655–692
  • Shikhman A. R. M.W.C. Trick and treat: toward peptide mimic vaccines. Nature Biotechnology 1997; 15: 512–513
  • Kieber-Emmons T., Luo J.-P., Qiu P., Chang T. Y., Blaszczyk-Thurin O. I.M., et al. Vaccination with carbohydrate peptide mimotopes promotes anti-tumor responses. Nature Biotechnology 1999; 17(7)660–665
  • Agadjanyan M., Luo P., Westerink M. A., Carey L. A., Hutchins W., Steplewski Z., et al. Peptide mimicry of carbohydrate epitopes on human immunodeficiency virus [see comments]. Nature Biotechnology 1997; 15(6)547–551
  • Westerink M. A.J., Giardina P. C., Apicella M. A., Kieber-Emmons T. Peptide mimicry of the meningococcal group C capsular polysaccharide. Proc. Natl. Acad. Sci. 1995; 92: 4021–4025
  • Kieber-Emmons T., Monzavi-Karbassi B., Wang B., Luo P., Weiner D. B.W. Cutting edge: DNA immunization with minigenes of carbohydrate mimotopes induce functional anti-carbohydrate antibody response. Journ. of Immunology 2000; 165: 623–627
  • Raychaudhuri S., Kang C. Y., Kaveri S. V., Kieber-Emmons T., Kohler H. Tumor idiotype vaccines. VII. Analysis and correlation of structural, idiotypic, and biologic properties of protective and nonprotective Ab2. J. Immunol. 1990; 145(2)760–767
  • Cheng H. L., Sood A. K., Ward R. E., Kieber-Emmons T., Kohler H. Structural basis of stimulatory anti-idiotypic antibodies. Mol. Immunol. 1988; 25(1)33–40
  • Stein K. E., Soderstrom T. Neonatal administration of idiotype or antiidiotype primes for protection against Escherichia coli K13 infection in mice. Journal of Experiment Medicine 1984; 160(4)1001–1011
  • Klaerner H. G., Dahlberg P. S., Acton R. D., Battafarano R. J., Uknis M. E., Johnston J. W., et al. Immunization with antibodies that mimic LPS protects against gram negative bacterial sepsis. Journal of Surgical Research 1997; 69(2)249–254
  • Westerink M. A., Campagnari A. A., Wirth M. A., Apicella M. A. Development and characterization of an anti-idiotype antibody to the capsular polysaccharide of Neisseria meningitidis serogroup C. Infection & Immunity 1988; 56(5)1120–1127
  • McNamara M. K., Ward R. E., Kohler H. Monoclonal idiotope vaccine against Streptococcus pneumoniae infection. Science 1984; 226(4680)1325–1326
  • Gulati S., McQuillen D. P., Sharon J., Rice P. A. Experimental immunization with a monoclonal anti-idiotope antibody that mimics the Neisseria gonorrhoeae lipooligosaccharide epitope 2C7. Journal of Infectious Diseases 1996; 174(6)1238–1248
  • An L. L., Hudson A. P., Prendergast R. A., O'Brien T. P., Stuart E. S., Whittum H. J., et al. Biochemical and functional anligenic mimicry by a polyclonal anti-idiotypic antibody for chlamydial exoglycolipid antigen. Pathobiology 1997; 65(5)229–240
  • Schreiber J. R., Patawaran M., Tosi M., Lennon J., Pier G. B. Anti-idiotype-induced, lipopolysaccharide-specific antibody response to Pseudomonas aeruginosa. Journal of Immunology 1990; 144(3)1023–1029
  • Schreiber J. R., Nixon K. L., Tosi M. F., Pier G. B., Patawaran M. B. Anti-idiotype-induced, lipopolysaccharide-specific antibody response to Pseudomonas aeruginosa. II. Isotype and functional activity of the anti-idiotype-induced antibodies. Journal of Immunology 1991; 146(1)188–193
  • Schreiber J. R., Pier G. B., Grout M., Nixon K., Patawaran M. Induction of opsonic antibodies to Pseudomonas aeruginosa mucoid exopolysaccharide by an anti-idiotypic monoclonal antibody. Journal of Infectious Diseases 1991; 164(3)507–514
  • Diakun K. R., Malta K. L. Synthetic antigens as immunogens: Part III. Specificity analysis of an anti-anti-idiotypic antibody to a carbohydrate tumor-associated antigen. Journal of Immunology 1989; 142(6)2037–2040
  • Tsuyuoka K., Yago K., Hirashima K., Ando S., Hanai N., Saito H., et al. Characterization of a T cell line specific to an anti-Id antibody related to the carbohydrate antigen, sialyl SSEA-1, and the immunodominant T cell antigenic site of the antibody. Journal of Immunology 1996; 157(2)661–669
  • Furuya A., Yoshida H., Hanai N. Development of anti-idiotype monoclonal antibodies for Sialyl Le(a) antigen. Anticancer Research 1992; 12(1)27–31
  • Schmolling J., Reinsberg J., Wagner U., Krebs D. Antiidiotypic antibodies in ovarian cancer patients treated with the monoclonal antibody B72.3. Hybridoma 1995; 14(2)183–186
  • Viale G., Grassi F., Pelagi M., Alzani R., Menard S., Miotti S., et al. Anti-human tumor antibodies induced in mice and rabbits by “internal image” anti-idiotypic monoclonal immunoglobulins. Journal of Immunology 1987; 139(12)4250–4255
  • Sen G., Chakraborty M., Foon K. A., Reisfeld R. A., Bhattacharya C. M. Induction of IgG antibodies by an anti-idiotype antibody mimicking disialoganglioside GD2. Journal of Immunotherapy 1998; 21(1)75–83
  • Chapman P. B., Houghton A. N. Induction of IgG antibodies against GD3 ganglioside in rabbits by an anti-idiotypic monoclonal antibody. Journal of Clinical Investigation 1991; 88(1)186–192
  • Minasian L. M., Yao T. J., Steffens T. A., Scheinberg D. A., Williams L., Riedel E., et al. A phase 1 study of anti-GD3 ganglioside monoclonal antibody R24. Cancer 1995; 75(9)2251–2257
  • Kanda S., Takeyama H., Kikumoto Y., Morrison S. L., Morton D. L., Irie R. F. Both VH and VI. regions contribute to the antigenicity of anti-idiotypic antibody that mimics melanoma associated ganglioside GM3. Cell Biophysics 1994; 25(65)65–74
  • Burritt J. B., Bond C. W., Doss K. W., Jesaitis A. J. Filamentous phage display of oligopeptide libraries. [Review] [102 refs]. Analytical Biochemistry 1996; 238(1)1–13
  • Cortese R., Monaci P., Nicosia A., Luzzago A., Felici F., Galfre G., et al. Identification of biologically active peptides using random libraries displayed on phage. [Review] [47 refs]. Current Opinion in Biotechnology 1995; 6(1)73–80
  • Cwirla S. E., Peters E. A., Barrett R. W., Dower W. J. Peptides on phage: a vast library of peptides for identifying ligands. Proceedings of the National Academy of Sciences of the United States of America 1990; 87(16)6378–6382
  • Harris S. L., Craig L., Mehroke J. S., Rashed M., Zwick M. B., Kenar K., et al. Exploring the basis of peptide-carbohydrate crossreactivity: evidence for discrimination by peptides between closely related anti-carbohydrate antibodies. Proceedings of the National Academy of Sciences of the United Slates of America 1997; 94(6)2454–2459
  • Hoess R., Brinkmann U., Handel T., Pastan I. Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody B3. Gene 1993; 128(1)43–49
  • Lane D. P., Stephen C. W. Epitope mapping using bacteriophage peptide libraries. [Review] [31 refs]. Current Opinion in Immunology 1993; 5(2)268–271
  • Oldenburg K. R., Loganathan D., Goldstein I. J., Schultz P. G., Gallop M. A. Peptide ligands for a sugar-binding protein isolated from a random peptide library. Proceedings of the National Academy of Sciences of the United States of America 1992; 89(12)5393–5397
  • Scott J. K., Smith G. P. Searching for peptide ligands with an epitope library. Science 1990; 249(4967)386–390
  • Scott J. K. Discovering peptide ligands using epitope libraries. [Review]. Trends in Biochemical Sciences 1992; 17(7)241–245
  • Smith G. P., Scott J. K. Libraries of peptides and proteins displayed on filamentous phage. Methods in Enzymology 1993; 217(228)228–257
  • Valadon P., Scharff M. D. Enhancement of ULISAs for screening peptides in epitope phage display libraries. Journal of Immunological Methods 1996; 197(1–2)171–179
  • Valadon P., Nussbaum G., Boyd L. F., Margulies D. H., Scharff M. D. Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans. Journal of Molecular Biology 1996; 261(1)11–22
  • Zhang H., Zhong Z., Pirofski L. A. Peptide epitopes recognized by a human anti-cryptococcal glucuronoxylomannan antibody. Infection & Immunity 1997; 65(4)1158–1164
  • Pinilla C., Chendra S., Appel J. R., Houghten R. A. Elucidation of monoclonal antibody polyspecificity using a synthetic combinatorial library. Peptide Research 1995; 8(5)250–257
  • Lescar J., Pellegrini M., Souchon H., Tello D., Poljak R. J., Peterson N., et al. Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme. Journal of Biological Chemistry 1995; 270(30)18067–18076
  • Phalipon A., Folgori A., Arondel J., Sgaramella G., Fortugno P., Cortese R., et al. Induction of anti-carbohydrate antibodies by phage library-selected peptide mimics. European Journal of Immunology 1997; 27(10)2620–2625
  • Scott J. K., Loganathan D., Easley R. B., Gong X., Goldstein I. J. A family of concanavalin A-binding peptides from a hexapeptide epitope library. Proceedings of the National Academy of Sciences of the United States of America 1992; 89(12)5398–5402
  • Shikhman A. R., Cunningham M. W. Immunogical mimicry between N-acetylbeta-D-glucosamine and cytokeratin peptides. Evidence for a microbially driven anti-keratin antibody response. Journal of Immunology 1994; 152(9)4375–4387
  • Shikhman A. R., Greenspan N. S., Cunningham M. W. Cytokeratin peptide SFGSGFGGGY mimics N-acetyl-beta-D-glucosamine in reaction with antibodies and lectins, and induces in vivo anti-carbohydrate antibody response. Journal of Immunology 1994; 153(12)5593–5606
  • Taki T., Ishikawa D., Hamasaki H., Handa S. Preparation of peptides which mimic glycosphingolipids by using phage peptide library and their modulation on β-galactosidase activity. Febs Letters 1997; 418(1–2)219–223
  • Qiu J., Luo P., Wasmund K., Sleplewski Z., Kieber-Emmons T. Towards the development of peptide mimotopes of carbohydrate antigens as cancer vaccines [In Process Citation]. Hybridoma 1999; 18(1)103–112
  • Young A. C., Valadon P., Casadevall A., Scharff M. D., Sacchettini J. C. The three-dimensional structures of a polysaccharide binding antibody to Cryptococcus neoiformans and its complex with a peptide from a phage display library: implications for the identification of peptide mimotopes. Journal of Molecular Biology 1997; 274(4)622–634
  • Ghiara J. B., Ferguson D. C., Satterthwait A. C., Dyson H. J., Wilson I. A. Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site. Journal of Molecular Biology 1997; 266(1)31–39
  • Murali R., Kieber-Emmons T. Molecular recognition of a peptide mimic of the Lewis Y antigen by an anti-Lewis Y antibody. Journal Molecular Recognition 1998, in press
  • Thurin-Blaszczyk M., Murali R., Westerink M. A.J., Steplewski M.-Z., Co S., Kieber-Emmons T. Molecular recognition of the Lewis Y antigen by monoclonal antibodies. Protein Engineering 1996; 9: 101–113
  • Jeffrey P. D., Bajorath J., Chang C. Y., Yelton D., Hellstrom I., Hellstrom K. E., et al. The X-ray structure of an anti-tumour antibody in complex with antigen [see comments]. Nature Structural Biology 1995; 2(6)466–471
  • Imberty A., Mikros E., Koca J., Mollicone R., Oriol R., Perez S. Computer simulation of histo-blood group oligosaccharides: energy maps of all constituting disaccharides and potential energy surfaces of 14 ABH and Lewis carbohydrate antigens. Glycoconjugate Journal 1995; 12(3)331–349
  • Mukhopadhyay C., Bush C. A. Molecular dynamics simulation of Lewis blood groups and related oligosaccharides. Biopolymers 1991; 31(14)1737–1746
  • Lemieux R. U., Bock K. The conformational analysis of oligosaccharides by H-NMR and HSEA calculation. Archives of Biochemistry & Biophysics 1983; 221(1)125–134
  • Jones G., Willett P. Docking small-molecule ligands into active sites. [Review]. Current Opinion in Biotechnology 1995; 6(6)652–656
  • Bohm H. J. LUDI: rule-based automatic design of new substituents for enzyme inhibitor leads. J. Comput. Aided Mol. Des. 1992; 6(6)593–606
  • Gillmor S. A., Cohen F. E. New strategies for pharmaceutical design. [Review] [24 refs]. Receptor 1993; 3(3)155–163
  • Luo P., Canziani G., Cunto-Amesty G., Kieber-Emmons T. A molecular basis for functional peptide mimicry of a carbohydrate antigen. J. Biol. Chem. 2000; 268(1)
  • Murali R., Kieber-Emmons T. Molecular recognition of a peptide mimic of the Lewis Y antigen by an anti-Lewis Y antibody. Journal of Molecular Recognition 1997; 10: 269–276
  • Kaur K. J., Khurana S., Salunke D. M. Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety. Journal of Biological Chemistry 1997; 272(9)5539–5543
  • Luo P., Agadjanyan J.-M., Qiu P., Westcrink M. A.J., Steplewski Z., Kieber-Emmons T. Antigenic and immunological mimicry of peptide mimotopes of adenocarcinoma associated carbohydrate antigens. Molecular Immunology 1998; 35(13)865–879
  • Pon R. A., Lussier M., Yang Q. L., Jennings H. J. N-Propionylated group B meningococcal polysaccharide mimics a unique bactericidal capsular epitope in group B Neisseria meningitidis. J. Exp. Med. 1997; 185(11)1929–1938
  • Brisson J. R., Uhrinova S., Woods R. J., van der Zwan M., Jarrell H. C., Paoletti L. C., et al. NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives. Biochemistry 1997; 36(11)3278–3292
  • Robijn G. W., Imberty A., van den Berg D. J., Ledeboer A. M., Kamerling J. P., Vliegenthart J. R, et al. Predicting helical structures of the exopolysaccharide produced by Lactobacillus sake 0–1. Carbohydr. Res. 1996; 288: 57–74
  • Evans S. V., Sigurskjold B. W., Jennings H. J., Brisson J. R., To R., Tse W. C., et al. Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 A resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for α-(28)-polysialic acid. Biochemistry 1995; 34(20)6737–6744
  • Kieber-Emmons T., Ward M. M., Ward R. E., Kohler H. Structural considerations in idiotype vaccine design. Monogr. Allergy 1987; 22: 126–133
  • Kieber-Emmons T., Jameson B. A., Morrow W. J. The gp120-CD4 interface: structural, immunological and pathological considerations. Biochim. Biophys. Acta. 1989; 989(3)281–300
  • Monfardini C., Kieber E. T., Von J. M., O'Malley Feldt B., Rosenbaum H., Godillot A. P., et al. Recombinant antibodies in bioactive peptide design. Journal of Biological Chemistry 1995; 270(12)6628–6638
  • Monfardini C., Kieber-Emmons T., Voet D., Godillot A. P., Weiner D. B., Williams W. V. Rational design of granulocyte-macrophage colony-stimulating factor antagonist peptides. J. Biol. Chem. 1996; 271(6)2966–2971
  • Prammer K. V., Boyer J., Ugen K., Shattil S. J., Kieber-Emmons T. Bioactive Arg-Gly-Asp conformations in anti-integrin GPiib-iiia antibodies. Receptor 1994; 4: 93–108
  • Williams W. V., Moss D. A., Kieber-Emmons T., Cohen J. A., Myers J. N., Weiner D. B., et al. Development of biologically active peptides based on antibody structure. Proc. Natl. Acad. Sci. USA 1989; 86(14)5537–5541, [published erratum appears in Proc. Natl. Acad. Sci. USA, 86(20): 8044, October 1989]
  • Williams W. V., Kieber-Emmons T., VonFeldt J., Greene M. I., Weiner D. B. Design of bioactive peptides based on antibody hypervariable region structures. Development of conformationally constrained and dimeric peptides with enhanced affinity. J. Biol. Chem. 1991; 266(8)5182–5190
  • Williams W. V., Kieber-Emmons T., Weiner D. B., Rubin D. H., Greene M. I. Contact residues and predicted structure of the reovirus type 3-receptor interaction. J. Biol. Chem. 1991; 266(14)9241–9250
  • Craig L., Sanschagrin P. C., Rozek A., Lackie S., Kuhn L. A., Scott J. K. The role of structure in antibody cross-reactivity between peptides and folded proteins. Journal of Molecular Biology 1998; 281(1)183–201
  • Stern B., Denisova G., Buyaner D., Raviv D., Gershoni J. M. Helical epitopes determined by low-stringency antibody screening of a combinatorial peptide library. Faseb Journal 1997; 11(2)147–153
  • Mer G., Kelienberger E., Lefevre J. P. Alpha-helix mimicry of a β-turn. J. Mol. Biol. 1998; 281(2)235–240
  • Thurin J., Thurin M., Kimoto Y., Herlyn M., Lubeck M. D., Elder D. E., et al. Monoclonal antibody-defined correlations in melanoma between levels of GD2 and GD3 antigens and antibody-mediated cytotoxicity. Cancer Res. 1987; 47(5)1229–1233
  • Luo P., Agadjanyan J.-M., Qiu P., Westerink M. A.J., Steplewski Z., Kieber-Emmons T. Antigenic and immunological mimicry of peptide mimotopes of adenocarcinoma associated carbohydrate antigens. Molecular Immunology 1998, in press
  • Pichla S. L., Murali R., Burnett R. M. The crystal structure of a Fab fragment to the melanoma-associated GD2 ganglioside. Journal of Structural Biology 1997; 119(1)6–16
  • Nardelli B., Tam J. P. The MAP system. A flexible and unambiguous vaccine design of branched peptides. Pharm. Biotechnol. 1995; 6: 803–819
  • Stein K. E., Zopf D. A., Miller C. B., Johnson B. M., Mongini P. K., Ahmed A., et al. Immune response to a thymus-dependent form of B512 dextran requires the presence of Lyb-5+ lymphocytes. J. Exp. Med. 1983; 157(2)657–666
  • Snapper C. M., Mond J. J. A model for induction of T cell-independent humoral immunity in response to polysaccharide antigens. J. Immunol. 1996; 157(6)2229–2233
  • Castano A. R., Tangri S., Miller J. E., Holcombe H. R., Jackson M. R., Huse W. D., et al. Peptide binding and presentation by mouse GDI [see comments]. Science 1995; 269(5221)223–226

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.