Strategies for Mimicking Neisserial Saccharide Epitopes as Vaccines

References

• Brooks G. F., Lammel C. J. Humoral immune response to gonococcal infections. Clin. Micro. Rev. 1989; 2S: S5–S10
   Google Scholar
• Kita E., Matsuura H., Kashiba S. A mouse model for the study of gonococcal genital infection. J. Infect. Dis. 1981; 143: 67–70
   Google Scholar
• Taylor-Robinson D., Furr P., Hetherington C. Neisseria gonnhoeae colonises the genital tract of oestradiol-treated germfree female mice. Micro. Path. 1990; 9: 369–374
   Google Scholar
• Tramont E. C., Boslego J., Chung R., McChesney D. C., Ciak J., Sadoff J., Piziak M., Brinton C., Wood S., Bryan J. Parenteral gonococcal pilus vaccine. The Pathogemic neisseriae, G. K. Schoolnik, G. F. Brooks, S. Falkow, C. E. Frasch, J. S. Knapp, J. A. McCutchan, S. A. Morse. American Society for Microbiology, Washington, DC 1985; 316–322
   Google Scholar
• Tramont E. C. Gonococcal vaccines. Clin. Micro. Rev. 1989; 2S
   Google Scholar
• Cohen I. R., Kellogg D. S., Norins L. C. Serum antibody response in experimental human gonorrhea: immunoglobulins G, A, and M. Br. J. Ven. Dis. 1969; 45: 325–327
   Google Scholar
• Tramont E. C., Ciak J. Antigonococcal antibodies in genital secretions. Immunobiology of Neisseria gonorrhoeae, G. F. Brooks, E. C. Gotschlich, W. D. Sawyer, F. E. Young. American Society for Microbiology, Washington, DC 1978; 274–278
   Google Scholar
• Lammel C. J., Sweet R. L., Rice P. A., Knapp J. S., Schoolnik G. K., Heilbron D. C., Brooks G. F. Antibody-antigen specificity in the immune response to infection with Neisseria gonorrhoeae. J. Infect. Dis. 1985; 152: 990–1001
   Google Scholar
• Rice P. A. Molecular basis for serum resistance in Neisseria gonorrhoeae. Clin. Microbiol. Rev. 1989; 2S: S112–S117
   Google Scholar
• Cannon J., Buchanan T., Sparling P. Confirmation of association of protein I serotype of Neisseria gonorrhoeae with ability to cause disseminated infection. Infect. Immun. 1983; 40: 816–819
   Google Scholar
• Sparling P. Biology of Neisseria gonorrhoeae. Sexually Transmitted Diseases, K. K. Holmes, P. A. Mardh, P. F. Sparling, P. J. Weisner, J. W. Cates, S. M. Lemon, W. E. Stamm. McGraw-Hill, New York 1990
   Google Scholar
• Ram S., McQuillen D. P., Gulati S., Elkins C., Pangburn M. K., Rice P. A. Binding of complement factor H to loop 5 of porin protein 1A: a molecular mechanism of serum resistance of non-sialylated Neisseria gonorrhoeae. J. Exp. Med. 1998; 187: 671–680
   Google Scholar
• Ram S., McQuillen D. P., Boden R., Gulati S., Pangburn M. K., Rice P. A. Neisseria gonorrhoeae regulate the classical pathway by directly binding C4-binding protein. Mol. Immunol. 1998; 35: 398, (Abstr.)
   Google Scholar
• Densen P., Gulati S., Rice P. A. Specificity of antibodies against Neisseria gonorrhoeae that stimulate neutrophil chemotaxis. J. Clin. Invest. 1987; 80: 78–87
   Google Scholar
• Apicella M. A., Westerink M. A.J., Morse S. A., Schneider H., Rice P. A., Griffiss J. M. Bactericidal antibody response of normal human serum to the lipooligosaccharide of Neisseria gonorrhoeae. J. Infect. Dis. 1986; 153: 520–526
   PubMed Web of Science ®Google Scholar
• Ross S. C, Densen P. Opsonophagocytosis of Neisseria gonorrhoeae: interaction of local and disseminated isolates with complement and neutrophils. J. Infect. Dis. 1985; 151: 33–41
   Google Scholar
• Brinton C., Bryan J., Dillon J., Guerina N., Jacobson L., Kraus S., Labik A., Lee S., Levine A., Lim S., Mc Michael J., Polen S., Rogers K., To A., To S. Uses of pili in gonorrhea control: role of bacterial pili in disease, purification, and properties of gonococcal pili, and progress in the development of a gonococcal pilus vaccine for gonorrhea. Immunobiology of Neisseria gonorrhoea, G. F. Brooks, E. C. Gotschlich, K. K. Holmes, W. D. Sawyer, F. E. Young. American Society for Microbiology, Washington, DC 1978; 155–178
   Google Scholar
• Boslego J. W., Tramont E. C., Chung R. C., McChesney D. G., Ciak J., Sadoff J. C., Piziak M. V., Brown J. D., Brinton C. C., Wood S. W., Bryan J. R. Efficacy trial of a parenteral gonococcal pilus vaccine in men. Vaccine 1991; 9: 154–162
   PubMed Web of Science ®Google Scholar
• Hagblom P., Segal E., Billyard E., So M. Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae. Nature 1985; 315: 156–158
   PubMed Web of Science ®Google Scholar
• Sparling P. P., Cannon J. G., So M. Phase and antigenic variation of pili and outer membrane protein II of Neisseria gonorrhoeae. J. Inject. Dis. 1986; 153: 196–201
   Google Scholar
• Rice P. A.E.W., Hook I II, Blake M. S., Kaslow R. S., Gulati S., Kohl P. K., Van Radden M., Buchanan T. M. A possible influence of vaccine induced Por, LOS, and Rmp antibodies on the outcome of intraurethral challenge with Neisseria gonorrhoeae. Neisseria 94, J. S. Evans, S. E. Yost, M. C.J. Maiden, I. M. Feavers. S.C.C., WinchesterEngland 1994; 483–484
   Google Scholar
• Gulati S., Rice P. A., Blake M., Sarafian S. K., Morse S. A., Quentin-Millet M. J., Arminjon F. Antibody responses in six volunteers immunized with a gonococcal protein I vaccine. Neisseriae 1990, M. Achtmann, P. Kohl, C. Marchal, G. Morelli, A. Seiler, B. Thiesen. Walter dc Gruyter & Co., BerlinGermany 1991; 229–234
   Google Scholar
• Yamasaki R., Schneider H., Griffiss J. M., Mandrell R. Epitope expression of gonococcal lipooligosaccharide (LOS). Importance of the lipoidal moiety for expression of an epitope that exists in the oligosaccharide moiety of LOS. Mol. Immunol. 1988; 25: 799–809
   Google Scholar
• Kayhty H., Karanko V., Peltola H., Makela P. H. Serum antibodies after vaccination with Haemophilus influenzae type b capsular polysaccharide and responses to reimmunization: no evidence of immunologic tolerance or memory. Pediatrics 1984; 74: 857–865
   PubMed Web of Science ®Google Scholar
• Mosier D. E., Zaldivar N. M., Goldings E., Mond J., Scher I., Paul W. E. Formation of antibody in the newborn mouse: study of T-cell-independent antibody response. J. Infect. Dis. 1977; 136: S14–S19
   Google Scholar
• Stead A., Main S., Ward M., Walt P. Studies on lipopolysaccharide isolated from strains of Neisseria gonorrhoeae. J. Gen. Microb. 1975; 88: 123–131
   Google Scholar
• Schneider H., Hale T. L., Zollinger W. D., Seid R., Hammack C. A., Jr, Griffiss J. M. Heterogeneity of molecular size and antigenic expression within lipooligosaccharides of individual strains of Neisseria gonorrhoeaeNeisseria meningitidis. Infect. Immun. 1984; 45: 544–549
   PubMedGoogle Scholar
• Mandrell R., Schneider H., Apicella M., Zollinger W., Rice P. A., Griffiss J. M. Antigenic and physical diversity of Neisseria gonorrhoeae lipooligosaccharides. Infect. Immun. 1986; 54: 63–69
   Google Scholar
• Mandrell R. E., Griffiss J. M., Macher B. A. Lipooligosaccharides (LOS) of Neisseria gonorrhoeae, Neisseria meningitidis have components that are immunochemically similar to precursors of human blood group antigens. Carbohydrate sequence specificity of the mouse monoclonal antibodies that recognize crossreacting antigens on LOS and human erythrocytes. J. Exp. Med. 1988; 168: 107–126
   PubMedGoogle Scholar
• Gibson B. W., Webb J. W., Yamasaki R., Fisher S. J., Burlingame A. L., Mandrell R. E., Schneider H., Griffiss J. M. Structure and heterogeneity of the oligosaccharides from the lipopolysaccharides of a pyocin-resistant Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. USA 1989; 86: 17–21
   Google Scholar
• Yamasaki R., Nasholds W., Schneider H., Apicella M. A. Epitope expression and partial structural characterization of F62 lipooligosaccharide (LOS) of Neisseria gonorrhoeae: IgM monoclonal antibodies (3F11 and 1–1-M) recognize non-reducing termini of the LOS components. Mol. Immunol. 1991; 28: 1233–1242
   Google Scholar
• Yamasaki R., Bacon B. E., Nasholds W., Schneider H., Griffiss J. M. Structural determination of oligosaccharides derived from lipooligosaccharide of Neisseria gonorrhoeae F62 by chemical, enzymatic, and two-dimensional NMR methods. Biochemistry 1991; 30: 10566–10575
   Google Scholar
• Yamasaki R., Kerwood D. E., Schneider H., Quinn K. P., Griffiss J. M., Mandrell R. E. The structure of lipooligosaccharide produced by Neisseria gonorrhoeae, strain 15253, isolated from a patient with disseminated infection: evidence for a new glycosylation pathway of gonococcal lipooligosaccharide. J. Biol. Chem. 1994; 269: 30345–30351
   PubMed Web of Science ®Google Scholar
• Kerwood D. E., Schneider H., Yamasaki R. Structural analysis of lipooligosaccharide produced by Neisseria gonorrhoeae, strain MS1 Imk (variant A): a precursor for a gonococcal lipooligosaccharide associated with virulence. Biochemistry 1992; 31: 12760–12768
   Google Scholar
• Yamasaki R., Koshino H., Kurono S., Nishinaka Y., McQuillen D. P., Kume A., Gulati S., Rice P. A. Structural and immunochemical characterization of a Neisseria gonorrhoeae epitope defined by a monoclonal antibody 2C7; the antibody recognizes a conserved epitope on specific lipo-oligosaccharides in spite of the presence of human carbohydrate epitopes. J. Biol. Chem. 1999; 51: 36550–36558
   Google Scholar
• Rice P. A., Kasper D. L. Characterization of gonococcal antigens responsible for induction of bactericidal antibody in disseminated infection: the role of gonococcal endotoxins. J. Clin. Invest. 1977; 60: 1149–1158
   Google Scholar
• Apicella M. A., Shero M., Jarvis G. A., Griffiss J. M., Mandrell R. E., Schneider H. Phenotypic variation in epitope expression of the Neisseria gonorrhoeae lipooligosaccharide. Infect. Immun. 1987; 55: 1755–1761
   PubMed Web of Science ®Google Scholar
• Schneider H., Griffiss J. M., Boslego J. W., Hitchcock P. J., Zahos K. M., Apicella M. A. Expression of paragloboside-like lipooligosaccharides may be a necessary component of gonococcal pathogenesis in men. J. Exp. Med. 1991; 174: 1601–1605
   PubMed Web of Science ®Google Scholar
• Schneider H., Hammack C. A., Apicella M. A., Griffiss J. M. Instability of expression of lipooligosaccharides and their epitopes in Neisseria gonorrhoeae. Infect. Immun. 1988; 56: 942–976
   PubMed Web of Science ®Google Scholar
• Gotschlich E. C. Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipo-oligosaccharide. J. Exp. Med. 1994; 180: 2181–2190
   PubMed Web of Science ®Google Scholar
• Jennings M., Hood D., Peak R., Virji M., Moxon E. Molecular analysis of a locus for the biosynthesis and phase-variable expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis. Mol. Microbiol. 1995; 18: 729–740
   Google Scholar
• Banerjee A., Wang R., Uljon S. N., Rice P. A., Gotschlich E. C., Stein D. C. Identification of the gene (lgtG) encoding the lipooligosaccharide b chain synthesizing glucosyl transferase from Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. USA 1998; 95: 10872–10877
   Google Scholar
• Mandrell R., Griffiss J., Macher B. Lipooligosaccharides (LOS) of Neisseria gonorrhoeae and Neisseria meningitidis have components that are immunochemically similar to precursors of human blood group antigens. Carbohydrate sequence specificity of the mouse monoclonal antibodies that recognize crossreacting antigens on LOS and human erythrocytes. J. Exp. Med. 1998; 168: 107–126
   Google Scholar
• Mandrell R. E. Further antigenic similarities of Neisseria gonorrhoeae lipooligosaccharides and human glycosphingolipids. Infect. Immun. 1992; 60: 3017–3020
   Google Scholar
• John C. M., Griffiss J. M., Apicella M. A., Mandrell R. E., Gibson B. W. The structural basis for pyocin resistance in Neisseria gonorrhoeae lipooligosaccharides. J. Biol. Chem. 1991; 266: 19303–19311
   Google Scholar
• Jennings H. J., Lugowski C., Ashton F. E. The structure of an R-type oligosaccharide core obtained from some lipopolysaccharides of Neisseria meningitidis. Carbohydr. Res. 1983; 121: 233–241
   PubMed Web of Science ®Google Scholar
• Parsons N. J., Patel P. V., Tan E. L., Andrade J. R.C., Nairn C. A., Goldner M., Cole J. A., Smith H. Cytidine 5′-monophospho-N-acetyl neuraminic acid and a low molecular weight factor from human red blood cells induce lipopolysaccharide alteration in gonococci when conferring resistance to killing by human serum. Microb. Pathog. 1988; 5: 303–309
   PubMed Web of Science ®Google Scholar
• Fox A., Curry A., Rowland P., Lancaster S., Dennis M., Nicholas J., Cole J., Smith H. A surface polysaccharide forms when gonococci are converted to serum resistance by cytidine 5′-monophospho-N-acetyl neuraminic acid. FEMSLETT 1989; 75–80
   Google Scholar
• Parsons N. J., Cole J. A., Smith H. Resistance to human serum of gonococi in urethral exuadates is reduced by neuraminidase. Proc. R. Soc. Lond. B. 1990; 241: 3–5
   Google Scholar
• Patel P., Martin P., Goldner M., Parsons N., Smith H. Red blood cells, a source of factors which induce Neisseria gonorrhoeae to resistance to complement-mediated killing by human serum. J. Gen. Microbiol. 1984; 130: 2767–2770
   Google Scholar
• Patel P. V., Veale D. R., Fox J. E., Martin P. M., Parsons N. J., Smith H. Fractionation of guinea pig serum for an inducer of gonococcal resistance to killing by human serum: active fractions containing glucopeptides similar to those from human red blood cells. J. Gen. Microbiol. 1984; 130: 2757–2766
   Google Scholar
• Patel P. V., Martin P. M., Tan E. L., Nairn C. A., Parsons N. J., Goldner M., Smith H. Protein changes associated with induced resistance of neiseria gonorrhoeae to killing by human serum are relatively minor. J. Gen. Microbiol. 1988; 134: 499–507
   Google Scholar
• Patel P. V., Parsons N. J., Andrade J. R.C., Nairn C. A., Tan E. L., Goldner M., Cole J. A., Smith H. White blood cells including polymorphonuclear phagocytes contain a factor which includes gonococcal resistance to complement-mediated serum killing. FEMS Microbiol. Lett. 1988; 50: 173–184
   Google Scholar
• Mandrell R. E., Lesse A. J., Sugai J. V., Shero M., Griffiss J. M., Cole J. A., Parsons N. J., Smith H., Morse S. A., Apicella M. A. In vitro, in vivo modification of Neisseria gonorrhoeae lipooligosaccharide epitope structure by sialylation. J. Exp. Med. 1990; 171: 1649–1664
   PubMed Web of Science ®Google Scholar
• Apicella M. A., Mandrell R. E., Shero M., Wilson M., Griffiss J. M., Brooks G. F., Fenner C., Breen C. F., Rice P. A. Modification by sialic acid of Neisseria gonorrhoeae lipooligosaccharide epitope expression in human urethral exudates: an immunoelectron microscopic analysis. J. Infect. Dis. 1990; 162: 506–512
   Google Scholar
• McQuillen D. P., Gulati S., Ram S., Turner A. K., Jani D. B., Heeren T. C., Rice P. A. Complement processing and immunoglobulin binding to Neisseria gonorrhoeae determined in vitro simulates in vivo effects. J. Infect. Dis. 1999; 179: 124–135
   PubMed Web of Science ®Google Scholar
• Estabrook M., Christopher N., Griffs J., Baker C., Mandrell R. Sialylation and human neutrophil killing of group C Neisseria meningitidis. J. Infect. Dis. 1992; 166: 1079–1085
   PubMedGoogle Scholar
• Frangipane J., Rest R. Anaerobic growth and cytidine 5′monophospho-n-acetylnuraminie acid act synergistically to induce high level serum resistance in Neisseria gonorrhoeae. Infect. Immun. 1993; 61: 1657–1666
   Google Scholar
• Kim J. J., Zhou D., Mandrell R. E., Griffiss J. M. Effect of exogenous sialylation of the lipooligosaccharide of Neisseria gonorrhoeae on opsonophagocytosis. Infect. Immun. 1992; 60: 4439–4442
   Google Scholar
• Elkins C., Carbonetti N., Varela V., Stirewalt D., Klapper D., Sparling P. Antibodies to N-terminal peptides of gonococcal porin are bactericidal when gonococcal lipooligasaccharide is not sialylated. Mol. Microbiol. 1992; 6: 2617–2628
   PubMedGoogle Scholar
• Gulati S., McQuillen D. P., Mandrell R. E., Jani D. B., Rice P. A. Immunogenicity of Neisseria gonorrhoeae lipooligosaccharide epitope, 2C7, widely expressed in vivo with no immunochemical similarity to human glycosphingolopids. J. Infect. Dis. 1996; 174: 1223–1237
   PubMed Web of Science ®Google Scholar
• Rice P. A., Kasper D. L. Characterization of serum resistance of Neisseria gonorrhoeae that disseminate: roles of blocking antibody and gonococcal outer membrane proteins. J. Clin. Invest. 1982; 70: 157–167
   PubMed Web of Science ®Google Scholar
• Ram S., Sharma A. K., Simpson S. D., Gulati S., McQuillen D. P., Pangburn M. K., Rice P. A. A novel sialic acid binding site of Factor H mediates serum resistance of sialylated Neisseria gonorrhoeae. J. Exp. Med. 1998; 187: 743–752
   PubMed Web of Science ®Google Scholar
• Jerne N. K. Towards a network theory of the immune system. Ann. Immunol. Inst. Pasteur. 1974; 125C: 373–389
   PubMedGoogle Scholar
• Bowen R., Bona C. Stimulation of lymphocytic clones by anti-idiotypic antibodies: basis for development of idiotypic vaccines. Antiidiotypic Vaccines. Vol. 3, P.-A. Cazanave. Springer-Verlag, New York 1991; 8
   Google Scholar
• Stein K. E., Soderstrom T. Neonatal administration of idiotype or antiidiotype primes for protection against Escherichia coli infection in mice. J. Exp. Med. 1984; 160: 1001–1011
   PubMed Web of Science ®Google Scholar
• Westerink M. A.J., 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. Infect. Immun. 1988; 56: 1120–1127
   Google Scholar
• 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. USA 1995; 92: 4021–4025
   Google Scholar
• McNamara M. K., Wardand R. E., Kohler H. Monoclonal idiotope vaccine against Streptococcus pneumoniae infection. Science 1984; 226: 1325–1326
   PubMedGoogle Scholar
• McNamara-Ward M., Ward R. J.-E., Huang H., Kohler H. Idiotype vaccine against Streptococcus pneumoniae—a precursor study. J. Immunol. 1987; 139: 2775–2780
   Google Scholar
• 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. J. Immunol 1991; 146: 188–193
   Google Scholar
• 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. J. Infect. Dis. 1991; 164: 507–514
   PubMedGoogle Scholar
• Brossay L., Paradis G., Pépin A., Mourad W., Cot L., ÉHébert J. Idiotype and anti-anti-idiotype antibodies to Neisseria gonorrhoeae lipooligosaccharides with bactericidal activity but no cross-reactivity with red blood cell antigens. J. Immunol. 1993; 151: 234–243
   Google Scholar
• Magliani W., Polonelli L., Conti S., Salati A., Rocca P., Cusumano V., Mancuso G., Teti G. Neonatal mouse immunity against group B streptococcal infection by maternal vaccination with recombinant anti-idiotypes. Nat. Med. 1998; 4: 705–709
   PubMedGoogle Scholar
• Westerink M. A.J., Muller E., Apicella M. A. Anti-idiotypic antibodies to bacterial capsular polysaccharides. Idiotypic Network and Discuses, J. Cerny, J. Hiernaux. American Society for Microbiology, Washington, DC 1990; 107–119
   Google Scholar
• Gulali S., McQuillen D. P., Sharon J., Rice P. A. Experimental immunization with a monoclonal anti-idiotope antibody that mimics the Neisseria gonorrhoeae Lipooligasaccharide epitope 2C7. J. Infect. Dis. 1996; 174: 1238–1248
   Google Scholar
• Herlyn D., Zaloudik J., Somasundaram R., Jacob L., Benden A., Mastangelo M. Anti-idiotype vaccine in colorectal cancer patients. Hybridoma 1993; 12: 515–520
   Google Scholar
• Foon K. A., Chakraborty M., John W. J., Sherratt A., Kohler H., Bhattacharya-Chatterjee M. Immune response to the carcinoembryonic antigen in patients treated with an anti-idiotype antibody vaccine. J. Clin. Invest. 1995; 96: 334–342
   PubMed Web of Science ®Google Scholar
• Chatterjee M., Mrozek E., Vaickus L., Oseroff A., Stoll H., Russell D., Kohler H., Foon K. A. Antiidiotype (Ab2) vaccine therapy for cutaneous T-cell lymphoma. Ann. N. Y. Acad. Sci. 1993; 690: 376–377
   PubMedGoogle Scholar
• Hutchins W., Kieber-Emmons T., Carlone G., Westerink M. Human immune response to a peptide mimic of Neisseria meningitidis serogroup C in human PBMC-SCID mice. Hybridoma 1999; 18: 121–129
   Google Scholar
• Scott J., Smith G. Searching for peptide ligands with an epitope library. Science 1990; 249: 386
   PubMed Web of Science ®Google Scholar
• Cortese R., Monaci P., Nicosia A., Luzzago A., Felici F., Galfre F., Pessi A., Tramontano A., Sollazzo M. Identification of biological active peptides using random libraries displayed on phage. Curr. Opin. Biotechnol. Annu. Rev. 1995; 6: 73–80
   Google Scholar
• Felici F., Luzzago A., Monaci P., Nicosia A., Sollazzo M., Traboni C. Peptide and protein display on the surface of filamentous bacteriophage. Biotechnol. Annu. Rev. 1995; 1: 149
   Google Scholar
• Daniels D., Lane D. The characterisation of p53 binding phage isolated from phage peptide display libraries. J. Mol. Biol. 1994; 4: 639–652
   Google Scholar
• Geysen H. M., Rodda S. J., Mason T. J. A priori delineation of a peptide which mimics a discontinuous antigenic determinant. Mol. Immunol. 1986; 23: 709–715
   PubMedGoogle Scholar
• Parmley S., Smith G. Antibody selectable filamentous Id phage vectors: affinity purification of target ganes. Gene 1988; 73: 305–318
   PubMed Web of Science ®Google Scholar
• Smith G. P. Surface presentation of protein epitopes using bacteriophage expression systems. Curr. Opin. Biotech. 1991; 2: 668–673
   PubMedGoogle Scholar
• Valadon P., Nussbaum G., Boyd L., Margulies D., Scharff M. Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans. J. Mol. Biol. 1996; 261: 11–22
   PubMedGoogle Scholar
• Zhang H., Zhong Z., Pirofski L. Peptide epitopes recognized by a human anticryptococcal glucuronoxylomannan antibody. Infect. Immun. 1997; 65: 1158–1164
   PubMed Web of Science ®Google Scholar
• Pincus S. H., Smith M. J., Jennings H. J., Burritt J. B., Glee P. M. Peptides that mimic the group B streptococcal type III capsular polysaccharide antigen. J. Immunol. 1998; 160: 293–298
   Google Scholar
• Lu Z., Murray K., Van Cleave V., La Value E., Stahl M., McCoy J. Expression of Thioredoxin Random Peptide Libraries on the Escherichia coli cell surface as functional fusionsto flagellin. A system designed for exploring protein protein interactions. Bio/Technology 1995; 13: 366–372
   PubMed Web of Science ®Google Scholar
• Scott J. K., Loganathan D., Easley R. B., Gong X., Goldstein I. J. A family of canavalin A-binding peptides from a hexapeptide epitope library. Proc. Natl. Acad. Sci. USA 1993; 89: 5398
   Google Scholar
• Oldenburg K., Loganathan D., Goldstein L., Schultz P., Gallop M. Peptide ligands for a sugar-binding protein isolated from random peptide library. Proc. Null. Sci. USA 1992; 89: 5393–5397
   PubMed Web of Science ®Google Scholar
• Hoess R., Brinkmann U. T.H., Pastan I. Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody B3. Gene 1993; 128: 43–49
   PubMed Web of Science ®Google Scholar
• Kieber-Emmons T., Monzavi-Karbassi B., Wang B., Luo P., Weiner D. Cutting edge: DNA immunization with minigenes of carbohydrate mimotopes induce functional anti-carbohydrate antibody response. J. Immun. 2000; 165: 623–627
   PubMed Web of Science ®Google Scholar
• Tanghe A., Denis O., Lambrecht B., Motte V., van den Berg T., Huygen K. Tuberculosis DNA vaccine encoding Ag85A is immunogenic and protective when administered by intramuscular needle injection but not by epidermal gene gunbombardment. Infect. Immun. 2000; 68: 3854–3860
   PubMed Web of Science ®Google Scholar