Preferential selection of Cys-constrained peptides from a random phage-displayed library by anti-glucitollysine antibodies

Journal of Peptide Science

Volumn 14, Issue 11, 2008, Pages 1216-1221

  Rojas, Gertrudis ^a   Pupo, Amaury ^b   Del Rosario Aleman, Maria ^a   Santiago Vispo, Nelson ^a  

^a CENTER FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Cuba)

^b CENTER OF MOLECULAR IMMUNOLOGY   (Cuba)

Author keywords

Disulfide bridges; Glucitollysine; Peptide library; Phage display

Indexed keywords

CYSTEINE; DISULFIDE; EPITOPE; GLUCITOLLYSINE ANTIBODY; MONOCLONAL ANTIBODY; PEPTIDE ANTIBODY; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANTIBODY AFFINITY; ANTIGENICITY; ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; IMMUNOREACTIVITY; MOLECULAR CLONING; NONHUMAN; PEPTIDE ANALYSIS; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DATABASE; PROTEIN ISOLATION; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; CLONING, MOLECULAR; CYSTEINE; DISULFIDES; EPITOPES; ESCHERICHIA COLI; LYSINE; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES; SERUM ALBUMIN, BOVINE; SORBITOL;

EID: 57849084792     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1061     Document Type: Article

References (17)

1. Smith GP. Filamentous fusion page: Novel expression vectors that display cloned antigens on the virion surface. Science 1985; 228: 1315-1317.
2. Deroo S, Muller CP. Antigenic and immunogenic phage displayed mimotopes as substitute antigens: applications and limitations. Comb. Chem. High Throughput Screen. 2001; 4: 75-110.
3. Taylor RM, Burritt JB, Baniulis D, Foubert TR, Lord CI, Dinauer M, Parkos CA, Jesaitis AJ. Site-specific inhibitors of NADPH oxidase activity and structural probes of flavocytochrome b: Characterization of six monoclonal antibodies to the p22 phox subunit. J. Immunol. 2004; 173: 7349-7357.
4. Lopez-Requena A, Mateo de Acosta C, Moreno E, Gonzalez Puchades Y, Talavera A, Vispo NS, Vazquez AM, Perez Gangliosides, Ab1 and Ab2 antibodies I. Towards a molecular dissection of an idiotype-anti-idiotype system. Mol. Immunol. 2007; 44: 423-433.
5. Wang L-F, Yu M. Epitope identification and discovery using phage display libraries: Applications in vaccine development diagnostics. Curr. Drug Targets 2004; 5: 1-15.
6. Smith GP, Petrenko VA. Phage display. Chem. Rev. 1997; 97: 391-410.
7. Felici F, Castagnoli L, Musacchio A, Japelli R, Cesareni G. Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector. J. Mol. Biol. 1991; 222: 301-310.
8. Luzzago A, Felici F, Tramontano A, Pessi A, Cortese R. Mimicking of discontinuous epitopes by phage-displayed peptides, I. Epitope mapping of human H ferritin using a phage library of constrained peptides. Gene 1993; 128: 51-57.
9. Sorell L, Lopez J, Gabrysiak B, Perez ME, Rodriguez M. Monoclonal antibodies against non-enzymatically glycated (NEG) proteins. Their use in quantitative ELISA for NEG serum proteins measurement. Biotecnol. Apl. 1992; 9: 121-129.
10. Curtiss LK, Witztum JL. A novel method for generating regionspecific monoclonal antibodies to modified proteins. Application to the identification of human glucosylated low density lipoproteins. J. Clin. Invest. 1983; 72: 427-1438.
11. Harris SL, Craig L, Mehroke JS, Rashed M, Zwick MB, Kenar K, Toone EJ, Greenspan N, Auzanneau F-I, Marino-Albernas J-R, Pinto BM, Scott JK. Exploring the basis of peptide-carbohydrate crossreactivity: evidence for discrimination by peptides between closely related anti-carbohydrate antibodies. Proc. Natl. Acad. Sci. U.S.A. 1997; 94: 2454-2459.
12. Zhang F, Yu M, Weiland E, Morrissy C, Zhang N, Westbury H, Wang L-F. Characterization of epitopes for neutralizing monoclonal antibodies to classical swine fever virus E2 and Erns using phage-displayed random peptide library. Arch. Virol. 2006; 151: 37-54.
13. Palacios-Rodriguez Y, Gazarian T, Rowley M, Majluf-Cruz A, Gazarian KJ. Collection of phage-peptide probes for HIV-1 immunodominant loop-epitopes. J. Microbiol. Methods 2007; 68: 225-235.
14. Menendez A, Chow KC, Pan OCC, Scott JK. Human immunodeficiency virus type 1-neutralizing monoclonal antibody 2F5 is multispecific for sequences flanking the DKW core epitope. J. Mol. Biol. 2004; 338: 311-327.
15. Vanhoorelbeke K, Depraetere H, Romijn RAP, Huizinga EG, De Maeyer M, Deckmyn H. A consensus tetrapeptide selected by phage display adopts the conformation of a dominant discontinuous epitope of a monoclonal anti-VWF antibody that inhibits the von Willebrand factor-collagen interaction. J. Biol. Chem. 2003; 278: 37815-37821.
16. Orning L, Rian A, Campbell A, Brady J, Fedosov SN, Bramlage B, Thompson K, Quadros EV. Characterization of a monoclonal antibody with specificity for holo-transcobalamin. Nutr. Metab. 2006; 3: 3-13.
17. Marks JD, Hoogenboom HR, Bonnert TP, McCafferty J, Griffiths AD, Winter G. By-passing immunization-human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 1991; 222: 581-597.